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A comprehensive review on tyrosinase inhibitors

Samaneh Zolghadri, Asieh Bahrami, Mahmud Tareq Hassan Khan and 4 more

Journal of Enzyme Inhibition and Medicinal Chemistry · 2019 · Review · CC BY

doi:10.1080/14756366.2018.1545767

Abstract

Tyrosinase is a multi-copper enzyme which is widely distributed in different organisms and plays an important role in the melanogenesis and enzymatic browning. Therefore, its inhibitors can be attractive in cosmetics and medicinal industries as depigmentation agents and also in food and agriculture industries as antibrowning compounds. For this purpose, many natural, semi-synthetic and synthetic inhibitors have been developed by different screening methods to date. This review has focused on the tyrosinase inhibitors discovered from all sources and biochemically characterised in the last four decades.

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From PubMed Central, U.S. National Library of Medicine, as current on Oct 16, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

1Browning of fruits, fungi and vegetables and hyperpigmentation in human skin are two common undesirable phenomena. Tyrosinase is the main enzyme recognised as responsible for this enzymatic browning and melanogenesis in mammals,. This encouraged researchers and scientists to focus on the identification, isolation, synthesis and characterisation of new potent tyrosinase inhibitors for various application in the food, cosmetics and medicinal industries. However, very few inhibitors are qualified for clinical use and skin-whitening agents. Moreover, as the clinical and industrial demands for tyrosinase inhibitors increase, in vitro assays and improved screening techniques are also undergoing rapid development for in vitro high-throughput screening tyrosinase inhibitors and putative skin-whitening agents. In other words, sensitive and correct assay methods for screening and development of effective tyrosinase inhibitors are of great importance. For this purpose, several spectrophotometric, chromatographic, electrophoretic, radiometric, and electrochemical assays have been applied and developed by researchers so far. Recently, a novel fluorescent biosensor and tyrosinase-based thin-layer chromatography-autography have been suggested for tyrosinase inhibitor screening.

2Additionally, further improvements of in vitro detection methods for rapidly screening tyrosinase inhibitors may be achieved through using virtual screening and construction of quantitative structure–activity relationship (QSAR) models of inhibitors,. Thus, a combination of bioinformatics simulation and biological in vitro analysis will be useful to understand the functional mechanisms of the tested compounds,,,. Lately, Gao et al. have performed a virtual screening from Traditional Chinese medicine (TCM) and predicted tyrosinase inhibition by 3 D QSAR pharmacophore models. For more information about successful utilisation of computational tools like QSAR-based and ligand-based virtual screening, a review published by Khan in 2012 organised and summarised novel and potent inhibitors of the enzyme. Furthermore, with regard to tyrosinase inhibition importance, several other reviews have presented the organisation of tyrosinase inhibitors from natural, semi- and full synthetic sources,51–62.

3The present review also focuses on the tyrosinase inhibitors discovered from all sources, including synthetic compounds, extracts and active ingredients of natural products, virtual screening and structure-based molecular docking studies published in the last four decades. We hope that the knowledge offered in this review serves as an updated comprehensive database contributing to the development of new safe and efficient anti-tyrosinase agents for the prevention of browning in plant-derived foods, seafood and hyperpigmentation treatments.

The role of tyrosinase in the melanin biosynthesis

4Melanins, the main pigment primarily responsible in the skin, hair and eyes pigmentation of human, are produced by melanocytes through melanogenesis. Melanogenesis and skin pigmentation are the most important photoprotective factor in response to ultraviolet radiation damaging from the sun and skin photo-carcinogenesis. The abnormal loss of melanin and depigmentation can be a serious facial esthetic and dermatological problem among human. On the contrary, the increased melanin synthesis and accumulation of these pigments occur in many types of skin disorders, including Acanthosis nigricans, Cervical Poikiloderma, melasma, Periorbital hyperpigmentation, Lentigines, neuro-degeneration associated with Parkinson’s disease and skin cancer risk. Although melanogenesis is a complicated process represented by numerous enzymatic and chemical reactions, the enzymes such as tyrosinase and other tyrosinase-related proteins (TYRP1 and TYRP2) have a critical role in melanin synthesis. Tyrosinase is a multifunctional copper-containing metalloenzyme with dinuclear copper ions, which plays as a rate-limiting enzyme in the synthesis of melanin (Figure 1),. Also, tyrosinase constitutes the primary cause for undesired browning of fruits and vegetables as well as diseases resulting from overproduction of melanin. Therefore, controlling the activity of enzyme by tyrosinase inhibitors is an essential endeavor for treating hypopigmentary disorders of mammals and enzymatic browning of fruits and fungi. To date, numerous effective inhibitors are identified and developed for using in the medical and cosmetic products, as well as food bioprocessing and agricultural industries and environmental industries. However, in medicine, tyrosinase inhibitors are a class of important clinical antimelanoma drugs but only a few compounds are known to serve as effective and safe tyrosinase inhibitors.

Mushroom tyrosinase properties

5Tyrosinases have been isolated and purified from different sources such as some plants, animals and microorganisms. Although many of them (such as human) have been sequenced, only few of them have been characterised. Recently, a novel tyrosinase produced by Sahara soil actinobacteria have been isolated and biochemically charactrised with the aim to identify novel enzymes with exclusive features for biotechnological applications. However, among different sources of tyrosinase, mushroom tyrosinase from Agaricus bisporus is a major and cheap source of tyrosinase with high similarity and homology compared to human tyrosinase. Because of these good properties, the structural, functional and biochemical characteristics of mushroom tyrosinase have been studied extensively as a model system for screening of tyrosinase inhibitors and melanogenic studies, enzyme-catalysed reactions and enzyme-inhibitor structural studies so far,. Tyrosinase from Agaricus bisporus is a 120 kDa tetramer with two different subunits, heavy and light, which was the first isolated by Bourquelot and Bertrand in 1895. It has three domains and two copper binding sites which bind to six histidine residues and interact with molecular oxygen in the tyrosinase active site. Also, a disulfide linkage stabilise its structure. Recently, a 50 kDa tyrosinase isoform from Agaricus bisporus (H-subunit) have been purified with a high specific tyrosinase activity of more than 38,000 U/mg.

Reaction mechanism

6Tyrosinase (EC 1.14.18.1) has two activities in its catalytic cycle, see Figure 2,, a monophenolase activity where it hydroxylates monophenols (e.g l-tyrosine) to o-diphenols (e.g. l-dopa) and a diphenolase activity where tyrosinase oxidises o-diphenols to o-quinones (o-dopaquinone). At the same time of these enzymatic reactions, there are different chemical reactions coupled where two molecules of o-dopaquinone react their-selves generating an o-diphenol molecule (L-dopa) and a dopachrome molecule.

7Diphenolase activity can be independently studied, when tyrosinase reacts with an o-diphenol (see Figure 2). The form met-tyrosinase (Em) binds the o-diphenol (D) originating the complex EmD. This complex oxidises the o-diphenols transforming it to o-quinone and the enzyme is converted into the form deoxy-tyrosinase (Ed). Ed has a very big affinity for the molecular oxygen originating the form oxy-tyrosinase (Eox), which binds another o-diphenol molecule and originating the complex EoxD. After that, the o-diphenol is oxidised again to o-quinone and the form Em is formed again completing the catalytic cycle. However, after these enzymatic reactions, two o-quinone molecules (e.g. o-dopaquinone) react generating dopachrome and regenerating a molecule of o-diphenol.

8As mentioned before, we can independently study the diphenolase activity. However, it is not applicable for the monophenolase activity, see Figure 2, because the chemical reactions of diphenolase activity have to occur at the same time of monophenolase activity. Tyrosinase shows the monophenolase activity with a lag period. This period is the time that the enzyme requires to accumulate a quantity of o-diphenol in reaction medium and is proportional to the quantity of monophenol used. Figure 2 shows the new complexes appeared in the monophenolase activity: EoxM (oxy-tyrosinase bound to monophenol) and EmM (met-tyrosinase bound to monophenols). EoxM is active and is transformed into EmD, which is an intermediate of the catalytic cycle. o-Quinones formed by these two oxidation cycle spontaneously react with each other to form oligomers.

Tyrosinase inhibition

9Due to the critical role of tyrosinase in the melanogenesis and browning process, several investigations have been reported for the identification of tyrosinase inhibitor from both natural (fungi, bacteria, plants) and synthetic sources so far. General speaking, tyrosinase inhibitors are examined in the presence of a monophenolic substrate such as tyrosine or a diphenolic substrate such as l-dopa, and activity is assessed based on dopachrome formation.

Inhibition mechanism

10Among different types of compounds such as specific tyrosinase inactivators and inhibitors, o-dopaquinone scavengers, alternative enzyme substrates, nonspecific enzyme inactivators and denaturants, only specific tyrosinase inactivators and reversible inhibitors actually bind to the enzyme as true inhibitors and really inhibit its activity:Specific tyrosinase inactivators. They are called suicide inactivators or mechanism-based inhibitors. This group of compounds can be considered very interested from a pharmacological point of view, in hyperpigmentation processes (Figure 3).

11Specific tyrosinase inactivators. They are called suicide inactivators or mechanism-based inhibitors. This group of compounds can be considered very interested from a pharmacological point of view, in hyperpigmentation processes (Figure 3).

12To explain the suicide inactivation of tyrosinase, mainly two mechanisms have been proposed,. Accordingly, Haghbeen et al. have suggested that the conformational changes, triggered by the substrate then mediated by the solvent molecules, in the tertiary and quaternary structures of tyrosinase, might be the real reason for the suicide inactivation. On the other hand, however, based on reports, it was found that acetylation of tyrosine residues with N-acetylimidazole protects mushroom tyrosinase from the suicide inactivation in the presence of its catecholic substrate, 4-[(4-methylbenzo) azo]-1,2-benzenediol without any major impact on the secondary structure of enzyme.

13The studies about the kinetics of suicide inactivation of tyrosinase have been carried out with several o-diphenolic substrates, ascorbic acid, l- and d-dopa and with different aminophenols and o-diamines. The authors have established that the suicide inactivation could occur after the transference of a proton to the peroxide group on the active site of oxy-tyrosinase,, also it has been proposed that the monophenols do not inactivate the enzyme,.

14The chemical structure of the different substrates is diverse, but the process always requires a step of oxidation/reduction: o-diphenols,, ascorbic acid, aminophenols and o-diamines, hydroxyhydroquinone, tetrahydrobiopterines, tetrahydrofolic acid and NADH.Generally, the mode of inhibition by “true inhibitors” is one of these four types: competitive, uncompetitive, mixed type (competitive/uncompetitive), and noncompetitive. A competitive inhibitor can bind to a free enzyme and prevents substrate binding to the enzyme active site. Regarding the property that tyrosinase is a metalloenzyme, copper chelators such as many aromatic acids, phenolic and poly-phenolic compounds, a few non-aromatic compounds, can inhibit tyrosinase competitively by mimicking the substrate of tyrosinase,. Recently, it was found that d-tyrosine negatively regulates melanin synthesis by inhibiting tyrosinase activity, competitively. In addition, l-tyrosine has been shown as an inhibitor.

15Generally, the mode of inhibition by “true inhibitors” is one of these four types: competitive, uncompetitive, mixed type (competitive/uncompetitive), and noncompetitive. A competitive inhibitor can bind to a free enzyme and prevents substrate binding to the enzyme active site. Regarding the property that tyrosinase is a metalloenzyme, copper chelators such as many aromatic acids, phenolic and poly-phenolic compounds, a few non-aromatic compounds, can inhibit tyrosinase competitively by mimicking the substrate of tyrosinase,. Recently, it was found that d-tyrosine negatively regulates melanin synthesis by inhibiting tyrosinase activity, competitively. In addition, l-tyrosine has been shown as an inhibitor.

16In contrast, an uncompetitive inhibitor can bind only to the enzyme-substrate complex and a mixed (competitive and uncompetitive mixed) inhibitor can bind to both forms of free enzyme and enzyme-substrate complex. Finally, noncompetitive inhibitors bind to a free enzyme and an enzyme–substrate complex with the same equilibrium constant. Non-competitive and mixed-inhibition are frequent modes observed in the kinetics studies on mushroom tyrosinase activities. Phthalic acid and cinnamic acid hydroxypyridinone derivatives are two examples of mixed type inhibitors of mono-phenolase activity. Also, some compounds such as phthalic acid and terephthalic acid, D-(−)-arabinose, brazilein, thymol analogs were demonstrated as mixed-type effector examples of di-phenolase activity. Furthermore, other compounds such as bi-pyridine derivatives, two thiadiazole derivatives barbarin, chlorocinnamic acids, propanoic acid, some N-(mono- or dihydroxybenzyl)-N-nitrosohydroxylamines and p-alkylbenzaldehydes inhibited catecholase activity of mushroom tyrosinase uncompetitively. Some derivatives of thiazoles are examples for noncompetitive tyrosinase inhibition.

17In addition to determining the inhibition mechanism, inhibitory strength which is expressed as the IC50 value (the concentration of inhibitor at which 50% of your target is inhibited) should be calculated in the enzyme kinetics studies and inhibitor screening to compare the inhibitory strength of an inhibitor with others. However, the IC50 values may be incomparable due to the varied assay conditions (different substrate concentrations, incubation time, and different sources of tyrosinase) but a positive control can be used for this purpose. Although, some researchers have not calculated IC50 and have not applied a positive control in their studies but, fortunately, in most studies conducted for screening new tyrosinase inhibitors, the popular whitening agents, such as kojic acid, arbutin or hydroquinone, were used as a positive control at the same time. However, among different types of mushroom tyrosinase inhibitors, some inhibitors such as hydroquinone arbutin, kojic acid,, azelaic acid, l-ascorbic acid, ellagic acid and tranexamic acid have been reported as skin-whitening agents in the cosmetic industry but there are a few reports failed to confirm their effect as an agent to lighten skin in clinical trials despite the safety of this compound. Recently, Mann et al., have compared the inhibitory effects of hydroquinone, arbutin and kojic acid by human tyrosinase and mushroom tyrosinase. They have found hydroquinone and arbutin and kojic acid (IC50 > 500 µmol/L) weekly inhibits human tyrosinase. In contrast, a resorcinyl-thiazole derivative, thiamidol, is a most potent inhibitor of human tyrosinase (IC50 of 1.1 µmol/L) but inhibits mushroom tyrosinase weakly (IC50 = 108 µmol/L). Also, deoxyarbutin, a novel reversible tyrosinase inhibitor with effective in vivo skin lightening potency, have been reported due to its increased skin penetration and binding affinity to human tyrosinase. In another research, Sugimoto et al. have investigated a comparison of inhibitory effects of alpha-arbutin and arbutin with human tyrosinase and they have found α-arbutin is stronger than arbutin.

Natural tyrosinase inhibitor sources

18Natural sources including plants, bacteria and fungi have recently become of increasing interest for their antityrosinase activity by producing bioactive compounds. A number of researchers prefer to identify inhibitors from natural sources due to their less toxicity and better bioavalibility, especially for food, cosmetic and medicinal applications.

Plants

19It is well known that phenolic compounds are the largest group of phytochemicals found in plants, which are mainly the factors responsible for the activities in plant extracts. Tyrosinase inhibitory activity of many plant extracts was carried out to find new sources of anti-tyrosinase compounds. For example, anti-tyrosinase activities of the following plants have been reported by various researchers: Asphodelus microcarpus, Morus nigra L, Greyia radlkoferi Szyszyl, Limonium tetragonum, Arctostaphylos uva-ursi, Pleurotus ferulae, Agastache rugosa Kuntze fermented with Lactobacillus rhamnosus and Lactobacillus paracasei, Artemisia aucheri Boiss, Cassia tora, S. brevibracteata subsp, Rhodiola crenulata, Alpinia officinarum Hance and Zanthoxylum bungeanum Maxim, Mangifera indica, Podocarpus falcatus, Momordica charantia, Cymbopogon citrates, Greyia flanaganii (IC50 = 32.62 µg/ml), Vitis vinifera Leaf extracts (IC50 = 3.84 mg/mL) and Inula britannica L.. Also, tyrosinase inhibitory activity of 91 native plants from central Argentina was carried out by Chiari et al.,. Their results approved the inhibitory activity of these extracts against tyrosinase: Achyrocline satureioides, Artemisia verlotiorum, Cotoneaster glaucophylla, Dalea elegans, Flourensia campestris, Jodina rhombifolia, Kageneckia lanceolata, Lepechinia floribunda, Lepe-chinia meyenii, Lithrea molleoides, Porlieria microphylla, Pterocaulon alopecuroides, Ruprechtia apetala, Senna aphylla, Sida rhombifolia, Solanum argentinum, Tagetes minuta, and Thalictrum decipiens. Besides, plants from the Moraceae family including genera Morus species, Artocarpus, Maclura (Cudrania), Broussonetia, Milicia (Chlorophora), and Ficus have shown in vitro tyrosinase inhibition. Also, ethanolic and methanolic extracts of some other plants such as Ardisia elliptica Thunb, Phyllanthus acidus (L.) Skeels, Rhinacanthus nasutus L. Kurz (IC50 value of 271.50 µg/ml), Arbutus andrachne L. (IC50 = 1 mg/mL), Withania somnifera L. Dunal and Solanum nigrum L. berries, Pulmonaria officinalis and Centarium umbellatum and Camel’s foot creeper leaves (Bauhinia vahlii) significantly inhibited tyrosinase activity, too. Quispe et al. have screened tyrosinase inhibitory properties of Peruvian medicinal plants. Among these plant extracts, Hypericum laricifolium Juss, Taraxacum officinale F.H.Wigg. (IC50 value of 290.4 µg/ml), and Muehlenbeckia vulcanica Meisn (IC50 value of 280.1 µg/ml) showed the greatest anti-tyrosinase activity. Furthermore, tyrosinase inhibitory activity of mangrove plants in Micronesia, Korean indigenous plants, plants from Brazilian Cerrado, five traditional medicinal plants from Iran, ethanol extracts from medicinal and edible plants cultivated in Okinawa, seashore plants, some tropical plants and Bangladeshi indigenous medicinal plants, have been investigated by various researchers. Bonesi et al. have reported recent trends in the discovery of tyrosinase inhibitors from plant sources.

Fungi and bacteria

20Fungi from different genera such as Aspergillus sp., Trichoderma sp., Paecilomyces sp., Phellinus linteus, Daedalea dickinsii, Dictyophora indusiata along with a liquid culture of Neolentinus lepideus have been reported as a source of novel tyrosinase inhibitor by producing bioactive compounds. Also, there have been several reports on tyrosinase inhibitors from some marine fungi species such as Myrothecium sp. isolated from algae and Pestalotiopsis sp. Z233. Also, there are several reports on tyrosinase inhibition by bacterial species and their metabolites. Among them, Streptomyces sp., such as S. hiroshimensis TI-C3 isolated from soil, an actinobacterium named Streptomyces swartbergensis sp. Nov. and Streptomyces roseolilacinus NBRC 12815 are potential bacterial sources of tyrosine inhibitors. Moreover, some tyrosinase inhibitors have been reported from a gram-negative marine bacterium Thalassotalea sp. Pp2-459 and a toxic strain of the cyanobacterium, Oscillatoria agardhii. Interestingly, some probiotics such as Lactobacillus sp. which are used in the fermentation process have been investigated as natural tyrosinase inhibitor sources. Based on the studies, it has been confirmed that the physiological activities of fermented extracts are considerably higher than those of unfermented extracts and their cytotoxic activity is lower as compared to unfermented extracts. Recently, tyrosinase inhibitory four different lactic acid bacteria (LAB) strains isolated from dairy cow feces have been proved by Ji et al..

21Finally, in an updated review by Fernandes from reported findings, tyrosinase inhibitors produced by microorganisms have been summarised. This review shows that diverse tyrosinase inhibitors isolated from plant sources and fungi are mostly phenolic compounds, steroids, and alkaloids structurally comparable with each other. In contrast, tyrosinase inhibitors from bacteria comprise a smaller group of alkaloids, macrolides, and polyphenols, which competitively inhibit the enzyme.

Simple phenols

22Phenolic compounds which are characterised by having at least one aromatic ring and one (or more) hydroxyl group can be classified based on the number and arrangement of their carbon atoms. These compounds are commonly found to be conjugated to sugars and organic acids. Phenolics range from simple to large and complex tannins and derived polyphenols due to their molecular-weight and number of aromatic-rings.

23The simple phenols such as hydroquinone, and its derivatives,, deoxyarbutin, and its derivatives, 4–(6-Hydroxy-2-naphthyl)-1,3-bezendiol, resorcinol (or resorcin) and 4-n-butylresorcinol, vanillin and its derivatives, have been reported in the scientific literature as possible phenolic inhibitors of the tyrosinase (Figure 4). Chen et al. have found the alkylhydroquinone 10'(Z)-heptadecenylhydroquinone, isolated from the sap of the lacquer tree Rhus succedanea, can inhibit the activity of tyrosinase and suppress melanin production in animal cells. The IC50 of this compound (37 µM) is less than hydroquinone (70 µM) as a known inhibitor of tyrosinase. They have suggested that the potent inhibitory effect of this derivative on tyrosinase activity is likely due to its heptadecenyl chain, which facilitates the oxidation of the hydroquinone ring,.

24Isotachioside, a methoxy-hydroquinone-1-O-beta-d-glucopyranoside isolated from Isotachis japonica and Protea neriifolia and its glycoside derivatives (glucoside, xyloside, cellobioside, and maltoside) are categorised as analogs of arbutin. However, isotachioside and arbutin could not be determined as potent inhibitor. But, glucoside, xyloside, cellobioside and maltoside derivatives, missing methyl and benzoyl groups, acted as tyrosinase inhibitors with IC50s of 417, 852, 623 and 657 µM, respectively. Among these novel inhibitors, glucoside derivative (IC50 = 417 µM) was the most potent, indicating that the structural combination of resorcinol and glucose was significant for inducing the inhibitory effect.

25Hydroquinone and some of its known derivatives, including α and β-arbutin, are described as both a tyrosinase inhibitor and a substrate,. Deoxyarbutin and its second-generation derivatives have been proposed as promising agents to ameliorate hyperpigmented lesions or lighten skin due to less toxicity at their effective inhibitory dose,.

26Monophenolic compounds such as l-tyrosine, l-α-methyl-tyrosine and tyramine are substrates of tyrosinase. o-Quinone evolves in the medium of reaction accumulating o-diphenol and this accumulation provokes that met-tyrosinase (Em) is transformed into oxy-tyrosinase (Eox), which is the active form of the tyrosinase for monophenols and o-diphenols. Therefore, tyrosinase is active with monophenols such as: umbelliferone, hydroquinone,p-hydroxybenzyl alcohol, 4-hexylresorcinol, oxyresveratrol, 4-n-butylresorcinol, resorcinols, α and β-arbutin and p-coumaric acid, when we add the following reagents to medium of reaction: hydrogen peroxide (transforms Em to Eox), an o-diphenol or a reducing agent such as ascorbic acid transforming Em to Ed which, with molecular oxygen, is transformed into Eox. A particular case is deoxyarbutin, which acts as a substrate of tyrosinase even if any reagent is not added to the medium of reaction. Taking into consideration all the previous comments, several methods have been developed to discriminate between true inhibitors and alternative substrates of the enzyme,.

Polyphenols

27Plants produce a large diverse class of polyphenols including phenolic acids, flavonoids, stillbenes and lignans,. A large number of these compounds have been reported as a weak or potent inhibitor of tyrosinase from natural and synthetic sources.

Flavonoids

28Among polyphenolic compounds, some of the flavonoid derivatives mostly found in herbal plants, fruits and synthetic sources have been raveled to be the potent inhibitors of tyrosinase,,. There is a significant correlation between the inhibitory potency of flavonoids on mushroom tyrosinase and melanin synthesis in melanocytes. In searching effective tyrosinase inhibitors from natural products, many flavonoid compounds have been isolated and evaluated for their inhibitory activity on mushroom tyrosinase from different natural sources such as Trifolium nigrescens Subsp. Petrisavi, mung bean (Vigna radiatae L.), calamondin peel, Morus yunnanensis, Bhagwa and Arakta cultivar, Tibouchina semidecandra L, Maackia faurie, Pleurotus ostreatus, Potentilla bifurca, Alpinia officinarum, roots of Morus lhou, Garcinia subelliptica, Artocapus altilis, Myrsine africana, Pulsatilla cernua, Salvia miltiorrhiza-Carthamus tinctorius (Danshen-Honghua, DH) herbal pair and other various medicinal plants.

29Generally, major flavonoids (Figure 5) are classified into several main classes: flavones, flavonols, isoflavones, flavanones, flavanoles and anthocyanidins. Minor flavonoids included: dihydroflavones, flavan-3,4-diols, coumarins, chalcones, dihydrochalcones and aurones. Also, prenylated and vinylated flavonoids, such as flavonoid Glycosides, are other subclasses of flavonoids. Some flavonoid glycosides such as myricetin 3-galactoside and quercetin 3-O-β-galactopyronaside from Limonium tetragonum and 3',5'-di-C-β glucopyranosylphloretin from unripe calamondin peel (IC50 = 0.87 mg/ml), have been investigated for their inhibitory activities on tyrosinase. Moreover, the inhibitory activities of some other prenylated and vinylated flavonoids, such as kuwanon C, papyriflavonol A, sanggenon D and sophoflavescenol, and sanggenon D (IC50 = 7.3 µM) against tyrosinase, have been approved by Lee et al.. However, according to their findings, the prenylation with isoprenyl group or the vinylation of some flavonoid molecules does not enhance their tyrosinase inhibitory activity. Interestingly, it has even demonstrated that deglycosylation of some flavonoid glycosides by far-infrared irradiation can be improved tyrosinase inhibitory activity. In a survey from reported findings (2008–2013), Orhan et al. reviewed many examples of tyrosinase inhibitors with flavonoid structure. In the following, some tyrosinase inhibitors from various flavonoid classes have been mentioned and discussed.

Flavones and dihydroflavones

30The most common flavones are luteolin, apigenin, baicalein, chrysin and their glycosides (e.g. apigetrin, vitexin, and baicalin). Furthermore, nobiletin and tangeretin are the polymethoxylated flavones. Nguyen et al. have investigated the presence of apigenin and nobiletin from the methanolic extract of the heartwood of Artocapus altilis with 11 other phenolic compounds for their inhibitory activities on tyrosinase. In another research, Shang et al. have found a derivative of flavone, namely 7,8,4´-trihydroxyflavone which inhibits diphenolase activity of tyrosinase with an IC50 value of 10.31 ± 0.41 µM and a noncompetitive manner with a Ki of 9.50 ± 0.40 µM. The quenching anlaysis of tyrosinase by this compound showed a static mechanism and a single binding site with a binding constant of 7.50 ± 1.20 × 104 M−1 at 298 K. Based on the thermodynamics parameters, the binding process involved hydrogen bonds and van der Waals forces. Also, docking simulation illustrated hydrogen bonds between this compound and the residues His244 and Met280 of active site.

31In addition, several hydroxyflavones including baicalein, 6-hydroxyapigenin, 6-hydroxygalangin and 6-hydroxy-kaempferol and tricin (5,7,4′-trihydroxy-3′,5′-dimethoxyflavone) have been demonstrated as inhibitors of diphenolase activity of tyrosinase. The mechanism of inhibition by baicalein (IC50 = 0.11 mM) indicated a mix-type (Ki of 0.17 mM, α = 0.56). A single binding site with a binding constant of 2.78 × 105 M − 1 was obtained from the quenching fluorescence analysis for this compound. Thermodynamic parameters suggested spontaneous binding through hydrogen bonding and van der Waals forces. Furthermore, circular dichroism spectra indicated a reduction in the content of α-helix from 32.67% to 29.00% due to this binding. Docking simulations also indicated that baicalein mainly bound tyrosinase via its Met280 residue. While, tricin was found as a noncompetitive inhibitor of tyrosinase with good efficacy compared to its control. Based on circular dichroism spectra, the interactions between tricin and tyrosinase did not change the secondary structure. Fluorescence quenching revealed that the interaction of tricin with residues in the hydrophobic pocket of tyrosinase is stabilised by hydrophobic interactions and hydrogen bonding. Also, docking results implied that the stereospecific effects of tricin on substrates or products and flexible conformation alterations of tyrosinase produced by weak interactions between tricin and this enzyme are the possible inhibitory mechanisms of this compound.

32Another flavone named morusone from the twigs of Morus alba L. (IC50 = 290.00 ± 7.90 µM), a new bioflavone 4''',5,5″,7,7″-pentahydroxy-3',3'''-dimethoxy-3-O-β-d-glucosyl-3″,4'-O-biflavone from Trifolium nigrescens Subsp. Petrisavi, along with apigenin, flavone glucoside vitexin (IC50 = 6.3 mg/ml) and a C-glycosylflavone isovitexin (IC50 = 5.6 mg/ml) from Vigna radiatae L. extracts exhibited significant tyrosinase inhibition activities. Also, inhibitory effects of five flavones including mormin (IC50 = 0.088 mM), cyclomorusin (IC50 = 0.092 mM), morusin (IC50 = 0.250 mM), kuwanon C (IC50 = 0.135 mM) and norartocarpetin (IC50 = 1.2 µM) isolated from the stem barks of Morus lhou (S.) Koidz, have been investigated by Ryu et al. The mechanism of inhibition indicated that mormin, cyclomorusin, kuwanon C and norartocarpetin inhibited tyrosinase competitively.

Flavonoles

33Myricetin, kaempferol, quercetin, morin, isorhamnetin, galangin and their glycosides (e.g. rutin, quercitrin, and astragalin) are the predominant flavonols most commonly found as O-glycosides. So far, several flavonols such as kaempferol from Hypericum laricifolium Juss and Crocus sativus L., quercetin from Olea europaea L., quercetin-4'-O-beta-d-glucoside from Potentilla bifurca, quercetin-3-O-(6-O-malonyl)-β-d-glucopyranoside and kaempferol-3-O-(6-O-malonyl)-β-d-glucopyranoside from mulberry leaves, galangin from Alpinia officinarum, morin and (±) 2,3-cis-dihydromorin (IC50 = 31.1 µM), 2,3-trans-dihydromorin (IC50 = 21.1 µM) from Cudrania cochinchinensis, were identified as tyrosinase inhibitors.

34Based on kinetics studies, morin reversibly inhibited tyrosinase through a multi-phase kinetic process and bind to tyrosinase at a single binding site mainly by hydrogen bonds and van der Waals forces. It inhibited tyrosinase reversibly in a competitive manner with Ki = 4.03 ± 0.26 mM and the binding of morin to tyrosinase-induced rearrangement and conformational changes of the enzyme. Furthermore, it was reported that three flavonols including galangin, kaempferol and quercetin inhibit the oxidation of L-DOPA catalysed by mushroom tyrosinase and presumably this inhibitory activity comes from their copper chelating ability. While their corresponding flavones, chrysin, apigenin and luteolin, are not identified as copper chelator, Kubo et al. believed that the chelation mechanism by flavonols may be attributed to the free 3-hydroxyl group. Interestingly, quercetin behaves as a cofactor and does not inhibit monophenolase activity. In contrast, galangin inhibits monophenolase activity and does not act as a cofactor, and kaempferol neither acts as a cofactor nor inhibits monophenolase activity. However, inhibiting of diphenolase activity by chelating copper in the enzyme is the common feature of these three flavonols.

35Recently, 8-prenylkaempferol as a competitive tyrosinase inhibitor along with Kushenol A (noncompetitive) isolated from Sophora flavescens, have been investigated with IC50 values less than 10 µM. Finally, based on the literature review, many flavonol inhibitors are usually competitive inhibitors due to the 3-hydroxy-4-keto moiety of the flavonol structure, which chelates the copper in the active site. Also, among all these compounds, quercetin-4'-O-beta-d-glucoside with a IC50 value of 1.9 µM is revealed stronger tyrosinase inhibition than their positive control, kojic acid. While the other flavonol inhibitors listed above are very weak inhibitors and have little potential as skin whitening or food antibrowning.

Isoflavones

36Isoflavones such as daidzein, genistein, glycitein, formononetin, and their glycosides (e.g. genistin, daidzin) mostly are detected in the medicinal herbs. Park et al. have investigated tyrosinase inhibition activities of some natural o-dihydroxyisoflavone derivatives with variable hydroxyl substituent at the aromatic ring of isoflavone isolated from five-year-old Korean fermented soybean paste. They have demonstrated that two derivatives 7,8,4'-trihydroxyisoflavone and 7,3',4'-trihydroxyisoflavone inhibit tyrosinase by IC50 value of 11.21 ± 0.8 µM and 5.23 ± 0.6 µM, respectively, whereas very low inhibition activity was obtained for 6,7,4'-trihydroxyisoflavone, daidzein, glycitein and genistein. Also, 6,7,4'-trihydroxyisoflavone was identified as a potent competitive inhibitor of monophenolase activity of tyrosinase by Chang et al., with an IC50 value of 9.2 µM, which is six times potent than kojic acid. But, its analogs, glycitein, daidzein, and genistein showed little anti-tyrosinase activity. Therefore, they have suggested that C-6 and C-7 hydroxyl groups of the isoflavone skeleton might play an important role in the tyrosinase inhibitory activity. Furthermore, two other isoflavone metabolites, 7,8,4'-trihydroxyisoflavone and 5,7,8,4'-tetrahydroxyisoflavone isolated from soygerm koji, were investigated by Chang et al.. These compounds inhibited both monophenolase and diphenolase activities with an irreversible inhibition manner. Interestingly, by using HPLC analysis and kinetic studies, they have found that 7,8,4'-trihydroxyisoflavone and 5,7,8,4'-tetrahydroxyisoflavone are potent suicide substrates of mushroom tyrosinase. It may be concluded that the hydroxyl groups at both the C7 and C8 positions could completely change the inhibitory mechanism of the isoflavones from the reversible competitive to the irreversible suicide form.

37Recently, a noncompetitive inhibitor, glabridin (IC50 = 0.43 µM), isolated from the root of Glycyrrhiza glabra Linn, has exhibited excellent inhibitory effects on tyrosinase. The quenching analysis of tyrosinase by glabridin showed a static mechanism. Notably, a drug delivery system by using glabridin microsponge-loaded gel as a new approach for hyperpigmentation disorders have been proposed by Deshmukh et al.. In another research, Jirawattanapong et al. have identified a synthetic glabridin, 3'',4''-dihydroglabridin, with higher activity than glabridin (IC50 = 11.40 µM) against tyrosinase. They have suggested the more effective interaction with the enzyme may be due to more conformational flexibly of this compound that has occurred by the 4-substituted resorcinol skeleton and the lacking of double bond between carbon atom 3'' and 4'' in its structure. Also, Nerya et al. have reported that another isoflavone, glabrene, in the licorice extract can inhibit both monophenolase and diphenolase tyrosinase activities. In the study reported by Heo et al., two new isoflavones desmodianone H and uncinanone B have been identified as novel tyrosinase inhibitors. However, uncinanone B has higher anti-tyrosinase rate than desmodianone H. Glyasperin C from Glycyrrhiza glabra is another kind of isoflavone identified as tyrosinase inhibitor. Furthermore, some other isoflavones, formononetin, genistein, daidzein, texasin, tectorigenin, odoratin and mirkoin isolated from the stems of Maackia fauriei, have been investigated by Kim et al. for their tyrosinase inhibition activity. Based on their results, among these falvonoids, mirkoin (IC50 = 5 µM) revealed stronger tyrosinase inhibition than the positive control, kojic acid and inhibited tyrosinase reversibly in a competitive mode. Recently, two isoflavonoids lupinalbin (IC50 = 39.7 ± 1.5 µM), and 2′-hydroxygenistein-7-O-gentibioside (IC50 = 50.0 ± 3.7 µM) from Apios americana were identified as competitive inhibitors, with Ki values of 10.3 ± 0.8 µM and 44.2 ± 1.7 µM, respectively.

Flavanones

38Flavanones such as naringenin, hesperetin, eriodictyol and their glycosides (e.g. naringin, hesperidin, and liquiritin) and flavanonols (taxifolin) are mainly found in citrus fruits and the medicinal herbs. A copper chelator flavanone named hesperetin inhibits tyrosinase reversibly and competitively. Based on the ANS-binding fluorescence analysis, hesperetin disrupted of tyrosinase structure by hydrophobic interactions. In addition, hesperetin chelates a copper ion coordinating with 3 histidine residues (HIS61, HIS85, and HIS259) within the active site pocket of the enzyme due to docking simulation results. In another study, Chiari et al. have illustrated tyrosinase inhibitory activity of a 6-isoprenoid-substituted flavanone isolated from Dalea elegans. Also, Steppogenin is a natural flavanone with a strong tyrosinase inhibitory activity (IC50 = 0.98 ± 0.01 µM), from Morus alba L. Recently, a new isoprenylated sanggenon-type flavanone, nigrasin K, along with some other analogs including sanggenon M, C and O, chalcomoracin, sorocein H and kuwanon J isolated from the twigs of Morus nigra have been identified as potent tyrosinase inhibitors by Hu et al.. Among these natural inhibitors, sanggenon D revealed stronger tyrosinase inhibition than the positive control, kojic acid or arbutin.

Flavanoles and flavan-3,4-diols

39Flavan-3-ols are the most complex subclass of flavonoids ranging from the simple monomers (+)-catechin and its isomer (−)-epicatechin to the oligomeric and polymeric proanthocyanidins, which are also known as condensed tannins. Flavanols, such as catechin, epicatechin, epi-gallocatechin, epicatechin gallate (ECG), epigallocatechin gallate (EGCG) and proanthocyanidins are widespread in the medicinal herbs and higher plants,. Alphitonia neocaledonica (Rhamnaceae) is an endemic tree of New Caledonia, which has been identified as an anti-tyrosinase source due to the presence of tannins and gallocatechin. Moreover, a catechin compound isolated from the ethanol extract of Distylium racemosum branches, with IC50 value of 30.2 µg/mL, showed higher tyrosinase inhibition activity than arbutin as a positive control. Also, a proanthocyanidins from Clausena lansium demonstrated potent mushroom tyrosinase inhibition in a mixed competitive manner and illustrated strong inhibition of the melanogenic activity of B16 cells. The IC50 values for the monophenolase and diphenolase activities were 23.6 ± 1.2 and 7.0 ± 0.2 µg/mL, respectively. Furthermore, from the inhibition mechanism of this compound, it can be concluded that a chelation between the hydroxyl group on the B ring of the proanthocyanidins and dicopper ions of the enzyme has been occurred.

40Another investigation revealed that procyanidin-type proanthocyanidins, purified from cherimoya (Annona squamosa) pericarp could powerfully inhibit the activities of monophenolase and diphenolase of tyrosinase, competitively. In addition, Kim et al. have demonstrated that (+)-catechin-aldehyde polycondensates inhibit the l-tyrosine hydroxylation and L-DOPA oxidation by chelation to the active site of tyrosinase. Recently, another tyrosinase inhibitor from this class, condensed tannins (mixtures of procyanidins, propelargonidins, prodelphinidins) and their acyl derivatives (galloyl and p-hydroxybenzoate) from Longan Bark indicated the reversible and mixed (competitive is dominant) inhibition of tyrosinase.

Anthocyanidins

41Anthocyanins, including anthocyanidins (e.g. cyanidin, delphinidin, malvidin, peonidin, pelargonidin, etc.) and their glycosides, are widely distributed in the medicinal herbs. It seems that there is a significant relationship between anthocyanin content with anti-human and anti-mushroom tyrosinase activities.

Curcuminoids

42Two phenolic compounds, namely curcumin and desmethoxycurcumin have been isolated from the methanolic extract of the heartwood of Artocapus altilis and showed more potent tyrosinase inhibitory activities than the positive control kojic acid. Also, a curcumin included in Chouji and Yakuchi extracts inhibited the enzyme competitively. In addition, some synthetic curcumin derivative compounds, and its analogs possessing m-diphenols and o-diphenols have been investigated as potent inhibitors of mushroom tyrosinase. Based on the results, 4-hydroxyl groups in curcumin analogs containing 4-hydroxyl-substituted phenolic rings with C-2/C-4- or C-3/C-4-dihydroxyl-substituted diphenolic rings make them more active than kojic acid.

Coumarins

43In search of tyrosinase inhibitors, the inhibitory effects of several coumarin derivatives (Figure 6) such as 3-aryl and 3-heteroarylcoumarins, esculetin, coumarinolignoid 8'-epi-cleomiscosin, umbelliferone and their analogs, phenyl coumarins, hydroxycoumarins,, thiophosphonic acid diamides, diazaphosphinanes coumarin derivatives, cardol-coumarin derivatives and coumarin-resveratrol hybrids, were evaluated on tyrosinase activity.

44Interestingly, among hydroxycoumarins, the 3-hydroxycoumarin and 7-hydroxycoumarin showed potent activity for the tyrosinase inhibition, while the 4-hydroxycoumarin is not an inhibitor. Also, 2-(1-(coumarin-3-yl)-ethylidene) hydrazinecarbothioamide and 2-(1-(6-chlorocoumarin-3-yl) ethylidene)-hydrazinecarbothioamide demonstrated an irreversible inhibition of tyrosinase. Recently, in the screening of natural products for the development of cosmetic ingredients, two major compounds, trans-N-coumaroyltyramine (IC50 = 40.6 µM) and cis-N-coumaroyltyramine (IC50 = 36.4 µM) from Humulus japonicus showed potent tyrosinase inhibition.

Chalcones and dihydrochalcones

45Chalcones (butein, phloretin, sappan-chalcone, carthamin, etc.), or 1,3-diphenyl-2-propen-1-ones, are one of the most important classes of flavonoids. Chalcone-containing plants have been used for a long time in traditional medicine. Based on the reports, some natural and synthetic chalcones and their derivatives are identified as new potent depigmentation agents and tyrosinase inhibitors (Figure 7). So far, natural chalcones isoliquiritigenin (2′,4′,4-trihydroxychalcone) and glabrene from licorice roots, 2,4,2',4'-hydroxycalcone and three of its analogs with 3'-substituted resorcinol moieties from Morus australis (Figure 6, 19–22), 2,4,2',4'-tetrahydroxy-3-(3-methyl-2-butenyl)-chalcone from Morus nigra, vulpinoideol B from Carex vulpinoidea seeds, dihydrochalcones from Flemingia philippinensis, 2,4,2′,4′-tetrahydroxychalcone (IC50 = 0.07 ± 0.02 µM) and morachalcone A (IC50 = 0.08 ± 0.02 µM) from Morus alba L. and bavachinin from Psoralea corylifolia have been presented as tyrosinase inhibitors.

46Also, tyrosinase inhibitory effects of several synthetic chalcones and their derivatives were evaluated by various researchers. Oxindole-based chalcones, 1-(2-cyclohexylmethoxy-6-hydroxy-phenyl)-3-(4-hydroxymethyl-phenyl) propenone derivative, isoxazole chalcone derivatives, some azachalcones and their oximes,, 2,4,2',4'-tetrahydroxychalcone and its two derivatives (1,3,5-tris-(2,4-dihydroxy-phenyl) pentane-1,5-dione and 7,2',4'-trihydroxyflavanone), 2',4',6'-trihydroxychalcones, naphthyl chalcones and chalcone thiosemicarbazide derivatives have been identified as a new class of tyrosinase inhibitors. Interestingly, the most important factors in the efficacy of a chalcone are the location of the hydroxyl groups on both aromatic rings and the number of these hydroxyls and the presence of a catechol moiety don't correlate with increasing tyrosinase inhibition potency.

Aurones

47Okombi et al. have identified Z-benzylidenebenzofuran-3(2H)-one and analogs as human tyrosinase inhibitors. However, they found that aurones are weak inhibitors, but their derivatives with two or three hydroxyl groups preferably at 4,6 and 4' positions make them significant tyrosinase inhibitors. For example, the most potent aurone, 4,6,4'-trihydroxyaurone induces 75% inhibition at 0.1 mM concentration and is highly effective compared to kojic acid. In addition to synthetic compounds, several natural compounds such as (2'R)-2',3'-dihydro-2'-(1-hydroxy-1-methylethyl)-2,6'-bibenzofuran-6,4'-diol and 2-arylbenzofurans isolated from Morus notabilis and Morus yunnanensis, benzofuran flavonoids such as mulberrofuran G (MG) and albanol B (AB) isolated from Morus sp and macrourins E isolated from Morus macroura (IC50 = 0.39 µM) are potent tyrosinase inhibitors among aurones.

Phenolic acids

48Phenolic acids are divided into hydroxybenzoates and hydoxycinnamates. The most common hydroxycinnamates are p-coumaric, caffeic and ferulic acids. So far, p-hydroxybenzoic acid, chlorogenic acid (the ester of caffeic acid), vanilic acid (4-hydroxy-3-methoxybenzoic acid) and protocatechuic acid (a dihydroxybenzoic acid) from Hypericum laricifolium Juss, protocatechualdehyde (IC50 = 0.40 µg/mL) from Phellinus linteus, benzoic acid propyl gallate, orsellinic acid (2,4-dihydroxy-6-methylbenzoic acid) and orsellinates (2,4-dihydroxy-6-methyl benzoates), p-coumaric acid from ginseng leaves, m-coumaric acid, p-coumarate and its derivatives from leaves of Breynia officinalis caffeic acid and its n-nonyl ester, ferulic acid from Spiranthes sinensis, 4-Hydroxy cinnamic acid, synthetic hydroxycinnamoyl phenylalanyl/prolyl hydroxamic acid derivatives, and seven hydroxycinnamoyl derivatives in green coffee beans have been investigated for their tyrosinase inhibition activity. Among these, propyl gallate is a reversible and mixed-type inhibitor on diphenolase activity of tyrosinase with KIS = 2.135 mM and Ki = 0.661 mM309. Furthermore, n-butyl, iso-propyl, sec-butyl, n-pentyl, n-hexyl and n-octyl orsellinates (uncompetitive, with an inhibition constant of 0.99 mM) behaved as inhibitors at 0.50 mM, whereas methyl, ethyl, n-propyl, tert-butyl, and n-cetyl orsellinates acted as tyrosinase activators. Thus, tyrosinase inhibition increased with chain elongation, suggesting that the enzyme site can accept an eight-carbon alkyl chain.

49In addition to these compounds, 3-phenylbenzoic acid (3-PBA) was revealed to be the most potent inhibitor against monophenolase (noncompetitive, IC50 = 6.97 µM) and diphenolase (mixed type inhibition, IC50 = 36.3 µM) activity of mushroom tyrosinase. Also, Oyama et al. have found that some modification such as esterification can abrogate this inhibitory activity of tyrosinase.

Stillbenes

50Resveratrol is the most common stilbene. Several stillbenes derivatives from natural and synthetic sources (Figure 8) have been investigated for their tyrosinase inhibition activity including: resveratrol from Morus alba, Pleurotus ferulae, vitis viniferae caulis, Carignan grape juiceArtocarpus gomezianus and Streptomyces avermitilis MA4680 and also, its derivatives from Dipterocarpaceae plants and synthetic sources, oxyresveratrol from Morus australis, Morus alba L (IC50 = 0.10 ± 0.01 µM) and Cudrania cochinchinensis (IC50 = 2.33 µM), azo-resveratrol and its derivatives such as (E)-2-((2,4-dihydroxyphenyl)diazenyl) phenyl 4 methylbenzenesulfonate and azo-oxyresveratrol, trans-resveratrol from Streptomyces avermitilis MA4680, a resveratrol dimer named gnetin C, from melinjo (Gnetum gnemon). Also, several hydroxystillbene compounds from synthetic and semisynthetic sources, and from the extract of Veratrum patulum, along with synthetic glycosides of resveratrol, pterostilbene, and pinostilbene, synthetic trans-stilbene derivatives, azastilbene analogs, a newly synthesised stillbene 5-(6-hydroxy-2-naphthyl)-1,2,3-benzenetriol, coumarin-resveratrol hybrids, synthetic polyphenolic deoxybenzoins, hydroxy substituted 2-phenyl-naphthalenes and 4-(6-hydroxy-2-naphthyl)-1,3-bezendiol have been studied for their inhibition activity against tyrosinase. However, based on the enzymatic assays, resveratrol did not inhibit the diphenolase activity of tyrosinase, but L-tyrosine oxidation by tyrosinase was suppressed in presence of 100 µM resveratrol. Interestingly, after the 30 min of preincubation of tyrosinase and resveratrol, both monophenolase and diphenolase activities of tyrosinase were significantly suppressed. Furthermore, this effect was reduced with the addition of l-cysteine, which indicated suicide inhibition mechanism of resveratrol. Also, oxyresveratrol is identified as a tyrosinase substrate like hydroquinone, arbutin, caffeic acid and some other inhibitors. In addition to these studies on resveratrol, Fachinetti et al., have demonstrated that the incorporation of resveratrol into nanostructured lipid carriers allowed an enhanced tyrosinase inhibitory activity.

Lignans

51Lignans are complex and diverse structures, which are formed from three primary precursors. So far, lignans and lignan glycosides isolated from exocarp of Castanea henryi, Marrubium velutinum and Marrubium cylleneum, Pinellia ternate and Crataegus pinnatifida have been evaluated for their tyrosinase inhibitory potentials. However, these compounds mostly displayed a moderate mushroom tyrosinase inhibitory activity.

Terpenoid derivatives

52Carvacrol is a monoterpenoid phenol. To date, some carvacrol derivatives from synthetic sources, bakuchiol, a terpene phenol from Psoralea corylifolia, iridoid glucosides (another type of monoterpenoids) from Wulfenia carinthiaca Jacq and two new bis-iridoids, namely 7-O-caffeoyl-sylvestroside I and 7-O-(p-coumaroyl)-sylvestroside I isolated from Scabiosa stellata have been investigated for their anti-tyrosinase activities. Among these terpenoid derivatives, Cheng et al. have demonstrated that bakuchiol is a potent inhibitor by applying capillary electrophoresis with reliable online immobilised enzyme microreactor. Also, carvacrol derivatives such as 2-[2-methyl-5-(propan-2-yl)phenoxy]-2-oxoethyl(2E)-3–(2,4-dihydroxyphenyl)prop-2-enoate showed excellent tyrosinase inhibitory activity by a noncompetitive manner with Ki value 0.05 µM and IC50 = 0.0167 µM.

Quinone derivatives

53The quinones are a class of small molecules that are mostly derived from aromatic compounds such as benzene or naphthalene. Among these compounds, Aloin, an anthraquinone-C-glycoside from Aloe vera, anthraquinones from Polygonum cuspidatum and tanshinone IIA (IC50 = 1214 µM) have been verified as tyrosinase inhibitors.

Phenyl derivatives

54Several biphenyl derivatives (Figure 9) such as 4,4'-dihydroxybiphenyl, biphenyl ester derivatives, biphenyl construction from flavan-3-ol substrates, hydroxylated biphenyls, functionalised bis-biphenyl substituted thiazolidinones, phenylbenzoic acid derivatives, phenylethylamide and phenylmethylamide derivatives, hydroxy substituted 2-phenyl-naphthalenes, 4-hydroxyphenyl beta-d-oligoxylosides, benzenethiol or phenylthiol, 2-((1Z)-(2–(2,4-dinitrophenyl)hydrazin-1-ylidene)methyl) phenol and 4-[(4-hydroxyphenyl)azo]-benzenesulfonamide, have been identified as tyrosinase inhibitors.

Pyridine, Piperidine, pyridinones and hydroxypyridinone derivatives

55Some hydroxypyridinone derivatives, 3-hydroxypyridine-4-one derivatives hydroxypyridinone-L-phenylalanine and pyridinones have been characterised for their antityrosinase activity (Figure 10). Among these inhibitors, one mixed-type inhibitor from hydroxypyridinone-l-phenylalanine conjugates named ((S)-(5-(benzyloxy)-1-octyl-4-oxo-1,4-dihydropyridin-2-yl) methyl 2-amino-3-phenylpropanoate) showed potent inhibitory effect with IC50 values of 12.6 and 4.0 µM for monophenolase and diphenolase activities, respectively.

Thiosemicarbazones, Thiosemicarbazide and other Thio derivatives

56Several kinds of thiosemicarbazone derivatives,, has been investigated as possible tyrosinase inhibitors (Figure 11). Furthermore, some benzaldehyde derivatives of thiosemicarbazone such as chlorobenzaldehyde thiosemicarbazones, p-hydroxy and p-methoxy benzaldehyde thiosemicarbazone along with p-methoxybenzaldehyde thiosemicarbazone and 4-dimethylaminobenzaldehyde-thiosemicarbazone and 4-dimethylaminobenzaldehyde-N-phenyl-thiosemicarbazone were evaluated for their inhibitory activities on mushroom tyrosinase.

57Based on the findings, the appropriate functionalisation of thiosemicarbazone may be improved the inhibitory activity of these inhibitors. Dong et al. believe that the sterically bulky group at the C-4 position of the thiophene ring contributes to this activity. For example, the 4-functionalisation thiophene-2-carbaldehyde thiosemicarbazone with a methoxyacetyl group or introducing benzene ring to the 4-functionalised ester group enhanced inhibitory activity of thiophene-2-carbaldehyde thiosemicarbazone. However, 5-functionalisation decreased its inhibitory activity. Also, Soares et al., have demonstrated thiosemicarbazones Thio-1, Thio-2, Thio-3 and Thio-4 substituted with oxygenate moieties, displayed better inhibitory activity (IC50 0.42, 0.35, 0.36 and 0.44 mM, respectively) than Thio-5, Thio-6, Thio-7 and Thio-8.

58In addition to thiosemicarbazone derivatives, thiosemicarbazide and its derivatives, 5-benzylidene(thio)barbiturate-beta-d-glycosides, n-alkyl, p-phenylene-bis, phenyl, benzyl, p-xylidine-bis and p-pyridine dithiocarbamate sodium salts, diethyldithiocarbamate, phenylthiourea3 and other thiourea derivatives (Figure 12) such as methimazole, thiouracil, methylthiouracil, propylthiouracil, ambazone, and thioacetazone have been identified as tyrosinase inhibitors.

Azole and thiazolidine derivatives

59So far, several azole derivatives (Figure 13) have been studied for their tyrosinase inhibitory activity. The discovered new types of inhibitors included DL-3(5-benzazolyl) alanines and alpha-methyldopa analogs, aryl pyrazoles, heterocyclic hybrids based on pyrazole and thiazolidinone scaffolds, 3,5-diaryl-4,5-dihydro-1H and 3,5-diaryl pyrazole derivatives, pyrazolo[4,3-e][1,2,4]triazine sulfonamides and sildenafil, 1,3-oxazine-tetrazole, indole-spliced thiadiazole, benzimidazole-1,2,3-triazole hybrids, 1,2,3-triazole-linked coumarinopyrazole conjugates, isoxazolone derivatives 5(4H)-oxazolone derivative, imidazolium ionic liquids, thiazolyl resorcinols have demonstrated the inhibitory effect on tyrosinase. Furthermore, some thiazolidine derivatives have been evaluated for their tyrosinase inhibitory activity including azo-hydrazone tautomeric dyes substituted by thiazolidinone moiety, (Z)-5-(2,4-dihydroxybenzylidene) thiazolidine-2,4-dione, 5-(substituted benzylidene) thiazolidine-2,4-dione derivatives, (2RS,4R)-2-(2,4-dihydroxyphenyl)thiazolidine-4-carboxylic acid, 2-(substituted phenyl) thiazolidine-4-carboxylic acid derivatives and (Z)-5-(3-hydroxy-4-methoxybenzylidene)-2-iminothiazolidin-4-one.

Kojic acid analogs

60Kojic acid is a well-known tyrosinase inhibitor. When DL-DOPA, norepinephrine and dopamine are oxidised by tyrosinase, Kojic acid inhibits effectively the rate of formation of pigmented product(s) and of oxygen uptake. Furthermore, several of its derivatives have demonstrated a potent tyrosinase inhibitory activity,. Noh et al. have modified kojic acid with amino acids and screened their tyrosinase inhibitory activity. Among them, kojic acid-phenylalanine amide showed a strong noncompetitive inhibition. Interestingly, some kojic acid derivatives despite their depigmenting activities did not display tyrosinase inhibitory activitiy.

61Recently, Xie et al. have reported a kojic acid analog namely 5-phenyl-3-[5-hydroxy-4-pyrone-2-yl-methylmercapto]-4-(2,4-dihydroxylbenzylamino)-1,2,4-triazol as a potent competitive tyrosinase inhibitor with an IC50 value of 1.35 ± 2.15 µM. Tyrosinase inhibitory activity of some kojic acid derivatives is shown in Figure 14.

Benzaldehyde derivatives

62Benzaldehyde and its derivatives, hydroxy- or methoxy-substituted benzaldoximes and benzaldehyde-O-alkyloximes, piperonal or 4-(methylenedioxy) benzaldehyde mesoionic derivatives, 4-hydroxybenzaldehyde derivatives, anisaldehyde have been investigated for their inhibitory activities against tyrosinase (Figure 15).

63Among these derivatives, 3,4-dihydroxybenzaldehyde-O-ethyloxime (IC50 = 0.3 ± 0.1 µM) is of the same magnitude as one of the best tyrosinase known inhibitors tropolone (IC50 = 0.13 ± 0.08 µM). However, in benzaldehyde derivatives, the presence of the aldehyde group and the terminal methoxy group in C4 was found to play an important role in its inhibitory effect. But, due to their lower activity levels or serious side effects, unfortunately, most 4-substituted benzaldehyde derivatives cannot be considered for practical use.

Carboxylic acids

64Inhibitory effects of pyruvic acid, acrylic acid, propanoic acid, 2-oxo-butanoic acid, and 2-oxo-octanoic acid, (S)- and (R)-6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acids have been investigated on tyrosinase activity.

65Based on the findings investigated by Gheibi et al., aliphatic carboxylic acids have dual effects on the monophenolase and diphenolase activities of mushroom tyrosinase. They have found that optimal diphenolase activity of tyrosinase takes place in the presence of n-alkyl acids (pyruvic acid, acrylic acid, propanoic acid, 2-oxo-butanoic acid, and 2-oxo-octanoic acid). While, the monophenolase activity is inhibited by all types of n-alkyl acids. They have believed that there is a physical difference in the docking of mono- and o-diphenols to the tyrosinase active site. On the other hand, the binding of acids occurs through their carboxylate group with one copper ion of the binuclear site. So these carboxylic acid compounds completely block the monophenolase reaction, by preventing monophenol binding to the oxyform of the enzyme.

Xanthate derivative

66The inhibitory effect of some synthesised xanthates including C3H7OCS2Na, C4H9OCS2Na, C5H11OCS2Na, C2H5OCS2Na, and C6H13OCS2Na have been examined for inhibition of both monophenolase and diphenolase activities of mushroom tyrosinase. Based on the reports, C3H7OCS2Na and C4H9OCS2Na showed a mixed inhibition pattern on monophenolase activity but C5H11OCS2Na and C6H13OCS2Na showed a competitive and C2H5OCS2Na showed uncompetitive inhibition pattern. For diphenolase activity, C3H7OCS2Na and C2H5OCS2Na showed mixed inhibition but C4H9OCS2Na and C5H11OCS2Na and C6H13OCS2Na showed competitive inhibition. According to their results, it seems that the lengthening of the hydrophobic tail of the xanthates leads to a decrease of the Ki values for monophenolase inhibition and an increase of the Ki values for diphenolase inhibition.

Other tyrosinase inhibitors

67Except the inhibitors listed above, other compounds have also been registered for their tyrosinase inhibitory activity by different researchers such as: two Keggin-type polyoxometalates containing glycine as potent inorganic reversible inhibitors, cadmium ions with an IC50 of 2.92 ± 0.16 mM and rifampicin with an IC50 = 90 ± 0.6 µM as reversible and noncompetitive inhibitors, ammonium tetrathiotungstate, amoxicillin (IC50 = 9.0 ± 1.8 mM), mallotophilippen A and B α-naphthol and β-naphthol, red koji extracts (IC50 of 5.57 mg/mL) and alpha-hydrazinophloretic acid as competitive inhibitors and rottlerin as a mixed inhibitor. Furthermore, n-alkyl sulfates, sericin extracted from tasar silk fiber waste, 2-hydroxy-3-methylcyclopent-2-enone (IC50 = 721.91 µg mL−1) isolated from ribose-histidine Maillard reaction products, three natural compounds from safflower and mimosine and ethylenediamine are other kinds of tyrosinase inhibitors.

Synergistic effects of tyrosinase inhibitors

68Synergistic strategy for tyrosinase inhibitors is a useful strategy for the improvement of their inhibitory activities. Based on the findings, the mixtures of glabridin:resveratrol, glabridin:oxyresveratrol, resveratrol:oxyresveratrol, phenylethylresorcinol:resveratrol, oxyresveratrol:dioscin, aloesin:arbutin, 4-methyl catechol: catechol, 3-(2,4-dihydroxyphenyl)propionic acid:l-ascorbic acid, dihydromyricetin:vitamin D3, linderanolide B combined with arbutin, 1-phenyl-2-thiourea or kojic acid, have shown synergistic effect on tyrosinase. These studies may provide a scientific strategy for screening effective tyrosinase inhibitors.

Conclusion

69Due to the vital role of tyrosinase in the enzymatic browning of food and depigmentation disorders in humans, its inhibitors have been considered by researchers, extensively. As mentioned above, natural sources such as plants and microorganisms and their effective compounds have wonderful potential as organic anti-tyrosinase sources.

70However, the majority of the compounds identified from natural sources were isolated from plants but, recently, microorganisms are considered as potential sources of tyrosinase inhibitors. It is interesting that despite the diversity of natural inhibitors, a large number of tyrosinase inhibitors are phenolic-based structures. Many researchers have designed appropriate scaffold inspired by the structure of natural compounds and developed novel synthetic inhibitors. In this paper, many natural, semi-synthetic and synthetic inhibitors have been summarised and the inhibitory effects of these compounds on the tyrosinase activity are discussed.

71Based on the results, phenolic compounds (simple phenols and polyphenols) and their derivatives and several compounds including terpenoid, phenyl, pyridine, piperidine, pyridinone, hydroxypyridinone, thiosemicarbazone, thiosemicarbazide, azole, thiazolidine, kojic acid, benzaldehyde and xanthate derivatives were characterised as potent tyrosinase inhibitors. The appropriate functionalisation of these inhibitors such as C-6 and C-7 hydroxyl groups of the isoflavone skeleton, 4-functionalisation thiophene-2-carbaldehyde thiosemicarbazone with a methoxyacetyl group and the aldehyde group and methoxy group in C4 of benzaldehyde derivatives may be improved the inhibitory activity of these inhibitors. Furthermore, in cholcone derivatives, the location of the hydroxyl groups on both aromatic rings and the number of hydroxyls is an important factor in the efficacy of a chalcone. In contrast, some modifications such as the prenylation or the vinylation of some flavonoid molecules do not enhance their tyrosinase inhibitory activity while deglycosylation of some flavonoid glycosides by far-infrared irradiation can be improved tyrosinase inhibitory activity. Interestingly, among different inhibitors, some compounds, especially hydroquinone and its known derivatives (α and β-arbutin), are described as both a tyrosinase inhibitor and a substrate.

72Actually, the main objective of this review is to provide a useful source of effective tyrosinase inhibitors. However, despite the existence of a wide range of tyrosinase inhibitors from natural and synthetic sources, only a few of them, in addition to being effective, are known as safe compounds. Therefore, it is recommended to examine the efficacy and safety of inhibitors by in vivo models, along with in vitro and docking experiments, especially for the application of such materials in food and medicinal products. Finally, we hope that the information provided in this study, which is the result of numerous researchers’ efforts, could serve as leads in the search for effective anti-tyrosinase agents from natural and synthetic sources with increased efficiency and safety in the food and cosmetics industries.

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Haghbeen K, Saboury AA, Karbassi F Substrate share in the suicide inactivation of mushroom tyrosinase. Biochim Biophys Acta2004;1675:139–46.
Not in our library10.1016/j.bbagen.2004.08.017
101.
Saboury AA, Karbassi F, Haghbeen K, et al.Stability, structural and suicide inactivation changes of mushroom tyrosinase after acetylation by n-acetylimidazole. Int J Biol Macromol2004;34:257–62.
Not in our library10.1016/j.ijbiomac.2004.06.003
102.
Munoz-Munoz JL, Garcia-Molina F, Garcia-Ruiz PA, et al.Phenolic substrates and suicide inactivation of tyrosinase: kinetics and mechanism. Biochem J2008;416:431–40.
Not in our library10.1042/bj20080892
103.
Munoz-Munoz JL, Garcia-Molina F, Garcia-Ruiz PA, et al.Stereospecific inactivation of tyrosinase by L- and D-ascorbic acid. Biochim Biophys Acta2009;1794:244–53.
Not in our library10.1016/j.bbapap.2008.10.002
104.
Munoz-Munoz JL, Acosta-Motos JR, Garcia-Molina F, et al.Tyrosinase inactivation in its action on dopa. Biochim Biophys Acta2010;1804:1467–75.
Not in our library10.1016/j.bbapap.2010.02.015
105.
Munoz-Munoz JL, Garcia-Molina F, Berna J, et al.Kinetic characterisation of o-aminophenols and aromatic o-diamines as suicide substrates of tyrosinase. Biochim Biophys Acta2012;1824:647–55.
Not in our library10.1016/j.bbapap.2012.02.001
106.
Muñoz-Muñoz JL, Berna J, Garcia-Molina F, et al.Unravelling the suicide inactivation of tyrosinase: a discrimination between mechanisms. J Mol Catal B Enzym2012;75:11–9.
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107.
Munoz-Munoz JL, Garcia-Molina Mdel M, Garcia-Molina F, et al.Indirect inactivation of tyrosinase in its action on 4-tert-butylphenol. J Enzyme Inhib Med Chem2014;29:344–52.
Not in our library10.3109/14756366.2013.782298
108.
Munoz-Munoz JL, Garcia-Molina F, Acosta-Motos JR, et al.Indirect inactivation of tyrosinase in its action on tyrosine. Acta Biochim Pol2011;58:477–88.
Not in our library
109.
del Mar Garcia-Molina M, Munoz-Munoz JL, Berna J, et al.Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone. IUBMB Life2014;66:122–7.
Not in our library10.1002/iub.1250
110.
Munoz-Munoz JL, Garcia-Molina F, Arribas E, et al.Suicide inactivation of tyrosinase in its action on tetrahydropterines. J Enzyme Inhib Med Chem2011;26:728–33.
Not in our library10.3109/14756366.2010.548811
111.
Garcia-Molina F, Munoz-Munoz JL, Martinez-Ortiz F, et al.Tetrahydrofolic acid is a potent suicide substrate of mushroom tyrosinase. J Agric Food Chem2011;59:1383–91.
Not in our library10.1021/jf1035433
112.
Garcia-Molina F, Munoz-Munoz JL, Garcia-Molina M, et al.Melanogenesis inhibition due to NADH. Biosci Biotechnol Biochem2010;74:1777–87.
Not in our library10.1271/bbb.90965
113.
Park J, Jung H, Kim K, et al.D-tyrosine negatively regulates melanin synthesis by competitively inhibiting tyrosinase activity. Pigment Cell Melanoma Res2018;31:374–83.
Not in our library10.1111/pcmr.12668
114.
Hassani S, Gharechaei B, Nikfard S, et al.New insight into the allosteric effect of l-tyrosine on mushroom tyrosinase during l-dopa production. Int J Biol Macromol2018;114:821–9.
Not in our library10.1016/j.ijbiomac.2018.03.185
115.
Zhao DY, Zhang MX, Dong XW, et al.Design and synthesis of novel hydroxypyridinone derivatives as potential tyrosinase inhibitors. Bioorg Med Chem Lett2016;26:3103–8.
Not in our library10.1016/j.bmcl.2016.05.006
116.
Yin SJ, Si YX, Qian GY Inhibitory effect of phthalic acid on tyrosinase: the mixed-type inhibition and docking simulations. Enzyme Res2011;2011:1. doi:.
Not in our library10.4061/2011/294724
117.
Yin SJ, Si YX, Chen YF, et al.Mixed-type inhibition of tyrosinase from Agaricus bisporus by terephthalic acid: computational simulations and kinetics. Protein J2011;30:273–80.
Not in our library10.1007/s10930-011-9329-x
118.
Liu HJ, Ji S, Fan YQ, et al.The effect of D-(−)-arabinose on tyrosinase: an integrated study using computational simulation and inhibition kinetics. Enzyme Res2012;2012:731427. doi:.
Not in our library10.1155/2012/731427
119.
Hridya H, Amrita A, Sankari M, et al.Inhibitory effect of brazilein on tyrosinase and melanin synthesis: kinetics and in silico approach. Int J Biol Macromol2015;81:228–34.
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120.
Ashraf Z, Rafiq M, Seo SY, et al.Kinetic and in silico studies of novel hydroxy-based thymol analogues as inhibitors of mushroom tyrosinase. Eur J Med Chem2015;98:203–11.
Not in our library10.1016/j.ejmech.2015.05.031
121.
Karbassi F, Saboury AA, Khan MT, et al.Mushroom tyrosinase inhibition by two potent uncompetitive inhibitors. J Enzyme Inhib Med Chem2004;19:349–53.
Not in our library10.1080/14756360409162449
122.
Seo B, Yun J, Lee S, et al.Barbarin as a new tyrosinase inhibitor from Barbarea orthocerus. Planta Med1999;65:683–6.
Not in our library10.1055/s-1999-14092
123.
Hu YH, Liu X, Jia YL, et al.Inhibitory kinetics of chlorocinnamic acids on mushroom tyrosinase. J Biosci Bioeng2014;117:142–6.
Not in our library10.1016/j.jbiosc.2013.07.002
124.
Gheibi N, Saboury AA, Haghbeen K, et al.Dual effects of aliphatic carboxylic acids on cresolase and catecholase reactions of mushroom tyrosinase. J Enzyme Inhib Med Chem2009;24:1076–81.
Not in our library10.1080/14756360802632658
125.
Shiino M, Watanabe Y, Umezawa K Synthesis and tyrosinase inhibitory activity of novel N-hydroxybenzyl-N-nitrosohydroxylamines. Bioorg Chem2003;31:129–35.
Not in our library10.1016/s0045-2068(03)00026-9
126.
Chen QX, Song KK, Wang Q, Huang H Inhibitory effects on mushroom tyrosinase by some alkylbenzaldehydes. J Enzyme Inhib Med Chem2003;18:491–6.
Not in our library10.1080/14756360310001613094
127.
Saeed A, Mahesar PA, Channar PA, et al.Synthesis, molecular docking studies of coumarinyl-pyrazolinyl substituted thiazoles as non-competitive inhibitors of mushroom tyrosinase. Bioorg Chem2017;74:187–96.
Not in our library10.1016/j.bioorg.2017.08.002
128.
Mann T, Gerwat W, Batzer J, et al.Inhibition of human tyrosinase requires molecular motifs distinctively different from mushroom tyrosinase. J Invest Dermatol2018; 138:1601–8.
Not in our library10.1016/j.jid.2018.01.019
129.
Hamed SH, Sriwiriyanont P, deLong MA, et al.Comparative efficacy and safety of deoxyarbutin, a new tyrosinase-inhibiting agent. J Cosmet Sci2006;57:291–308.
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130.
Sugimoto K, Nishimura T, Nomura K, et al.Syntheses of arbutin-alpha-glycosides and a comparison of their inhibitory effects with those of alpha-arbutin and arbutin on human tyrosinase. Chem Pharm Bull (Tokyo)2003;51:798–801.
Not in our library10.1248/cpb.51.798
131.
Di Petrillo A, Gonzalez-Paramas AM, Era B, et al.Tyrosinase inhibition and antioxidant properties of Asphodelus microcarpus extracts. BMC Complement Altern Med2016;16:453.
Not in our library10.1186/s12906-016-1442-0
132.
Koyu H, Kazan A, Demir S, et al.Optimization of microwave assisted extraction of Morus nigra L. Fruits maximizing tyrosinase inhibitory activity with isolation of bioactive constituents. Food Chem2018;248:183–91.
Not in our library10.1016/j.foodchem.2017.12.049
133.
Anti-Melanogenic Effects of Flavonoid Glycosides from Limonium tetragonum (Thunb.) Bullock via Inhibition of Tyrosinase and Tyrosinase-Related Proteins · 2017
Not checked
134.
Matsuo K, Kobayashi M, Takuno Y, et al.Anti-tyrosinase activity constituents of Arctostaphylos uva-ursi. Yakugaku Zasshi1997;117:1028–32.
Not in our library10.1248/yakushi1947.117.12_1028
135.
Alam N, Yoon KN, Lee JS, et al.Consequence of the antioxidant activities and tyrosinase inhibitory effects of various extracts from the fruiting bodies of Pleurotus ferulae. Saudi J Biol Sci2012;19:111–18.
Not in our library10.1016/j.sjbs.2011.11.004
136.
Kim NY, Kwon HS, Lee HY Effect of inhibition on tyrosinase and melanogenesis of Agastache rugosa Kuntze by lactic acid bacteria fermentation. J Cosmet Dermatol2017;16:407–15.
Not in our library10.1111/jocd.12264
137.
Taherkhani M Chemical constituents, total phenolic content, antimicrobial, antioxidant and radical scavenging properties, chelating ability, tyrosinase inhibition and in vitro cytotoxic effects of Artemisia aucheri herbs. Pharm Chem J2017;50:736–45.
Not in our library
138.
Lee GY, Cho BO, Shin JY, et al.Tyrosinase inhibitory components from the seeds of Cassia tora. Arch Pharm Res2018;41:490–6.
Not in our library10.1007/s12272-018-1032-4
139.
Senol FS, Orhan I, Yilmaz G, et al.Acetylcholinesterase, butyrylcholinesterase, and tyrosinase inhibition studies and antioxidant activities of 33 Scutellaria L. taxa from Turkey. Food Chem Toxicol2010;48:781–8.
Not in our library10.1016/j.fct.2009.12.004
140.
Ya W, Chun-Meng Z, Tao G, et al.Preliminary screening of 44 plant extracts for anti-tyrosinase and antioxidant activities. Pak J Pharm Sci2015;28:1737–44.
Not in our library
141.
Nithitanakool S, Pithayanukul P, Bavovada R, Saparpakorn P Molecular docking studies and anti-tyrosinase activity of Thai mango seed kernel extract. Molecules2009;14:257–65.
Not in our library10.3390/molecules14010257
142.
Abdillahi HS, Finnie JF, Van Staden J Anti-inflammatory, antioxidant, anti-tyrosinase and phenolic contents of four Podocarpus species used in traditional medicine in South Africa. J Ethnopharmacol2011;136:496–503.
Not in our library10.1016/j.jep.2010.07.019
143.
Saeio K, Yotsawimonwat S, Anuchapreeda S, Okonogi S Development of microemulsion of a potent anti-tyrosinase essential oil of an edible plant. Drug Discov Ther2011;5:246–52.
Not in our library10.5582/ddt.2011.v5.5.246
144.
Mapunya MB, Hussein AA, Rodriguez B, Lall N Tyrosinase activity of Greyia flanaganii (Bolus) constituents. Phytomedicine2011;18:1006–12.
Not in our library10.1016/j.phymed.2011.03.013
145.
Lin YS, Chen HJ, Huang JP, et al.Kinetics of tyrosinase inhibitory activity using Vitis vinifera leaf extracts. Biomed Res Int2017;2017:5232680. doi:.
Not in our library10.1155/2017/5232680
146.
Huang MH, Tai HM, Wang BS, Chang LW Inhibitory effects of water extract of Flos Inulae on mutation and tyrosinase. Food Chem2013;139:1015–20.
Not in our library10.1016/j.foodchem.2013.01.066
147.
Chiari ME, Joray MB, Ruiz G, et al.Tyrosinase inhibitory activity of native plants from central argentina: isolation of an active principle from Lithrea molleoides. Food Chem2010;120:10–4.
Not in our library
148.
Burlando B, Clericuzio M, Cornara L Moraceae plants with tyrosinase inhibitory activity: A review. Mini Rev Med Chem2017;17:108–21.
Not in our library10.2174/1389557516666160609071854
149.
Chatatikun M, Chiabchalard A Thai plants with high antioxidant levels, free radical scavenging activity, anti-tyrosinase and anti-collagenase activity. BMC Complement Altern Med2017;17:487.
Not in our library10.1186/s12906-017-1994-7
150.
Issa RA, Afifi FU, Amro BI Studying the anti-tyrosinase effect of Arbutus andrachne L. extracts. Int J Cosmet Sci2008;30:271–6.
Not in our library10.1111/j.1468-2494.2008.00439.x
151.
Hameed A, Akhtar N Comparative chemical investigation and evaluation of antioxidant and tyrosinase inhibitory effects of Withania somnifera (L.) Dunal and Solanum nigrum (L.) berries. Acta Pharm2018;68:47–60.
Not in our library10.2478/acph-2018-0007
152.
Neagu E, Radu GL, Albu C, Paun G Antioxidant activity, acetylcholinesterase and tyrosinase inhibitory potential of Pulmonaria officinalis and Centarium umbellatum extracts. Saudi J Biol Sci2018;25:578–85.
Not in our library10.1016/j.sjbs.2016.02.016
153.
Panda P, Dash P, Ghosh G Chemometric profile, antioxidant and tyrosinase inhibitory activity of Camel's foot creeper leaves (Bauhinia vahlii). Nat Prod Res2018;32:596–9.
Not in our library10.1080/14786419.2017.1326487
154.
Quispe YN, Hwang SH, Wang Z, Lim SS Screening of peruvian medicinal plants for tyrosinase inhibitory properties: identification of tyrosinase inhibitors in Hypericum laricifolium Juss. Molecules2017;22:doi:.
Not in our library10.3390/molecules22030402
155.
Suh SS, Hwang J, Park M, et al.Phenol content, antioxidant and tyrosinase inhibitory activity of mangrove plants in Micronesia. Asian Pac J Trop Med2014;7:531–5.
Not in our library10.1016/s1995-7645(14)60089-4
156.
Hun Son K, Young Heo M Inhibitory effects of Korean indigenous plants on tyrosinase and melanogenesis. J Cosmet Sci2013;64:145–58.
Not in our library
157.
Souza PM, Elias ST, Simeoni LA, et al.Plants from Brazilian cerrado with potent tyrosinase inhibitory activity. PLoS One2012;7:e48589.
Not in our library10.1371/journal.pone.0048589
158.
Khazaeli P, Goldoozian R, Sharififar F An evaluation of extracts of five traditional medicinal plants from Iran on the inhibition of mushroom tyrosinase activity and scavenging of free radicals. Int J Cosmet Sci2009;31:375–81.
Not in our library10.1111/j.1468-2494.2009.00503.x
159.
Masuda T, Fujita N, Odaka Y, et al.Tyrosinase inhibitory activity of ethanol extracts from medicinal and edible plants cultivated in Okinawa and identification of a water-soluble inhibitor from the leaves of Nandina domestica. Biosci Biotechnol Biochem2007;71:2316–20.
Not in our library10.1271/bbb.70249
160.
Masuda T, Yamashita D, Takeda Y, Yonemori S Screening for tyrosinase inhibitors among extracts of seashore plants and identification of potent inhibitors from Garcinia subelliptica. Biosci Biotechnol Biochem2005;69:197–201.
Not in our library10.1271/bbb.69.197
161.
Baurin N, Arnoult E, Scior T, et al.Preliminary screening of some tropical plants for anti-tyrosinase activity. J Ethnopharmacol2002;82:155–8.
Not in our library10.1016/s0378-8741(02)00174-5
162.
Kubo I, Yokokawa Y, Kinst-Hori I Tyrosinase inhibitors from Bolivian medicinal plants. J Nat Prod1995;58:739–43.
Not in our library10.1021/np50119a013
163.
Bonesi M, Xiao J, Tundis R, et al.Advances in the tyrosinase inhibitors from plant source. Curr Med Chem2018;25:1. doi:.
Not in our library10.2174/0929867325666180522091311
164.
Vasantha KY, Murugesh CS, Sattur AP A tyrosinase inhibitor from Aspergillus niger. J Food Sci Technol2014;51:2877–80.
Not in our library10.1007/s13197-014-1395-6
165.
Tsuchiya T, Yamada K, Minoura K, et al.Purification and determination of the chemical structure of the tyrosinase inhibitor produced by Trichoderma viride strain H1-7 from a marine environment. Biol Pharm Bull2008;31:1618–20.
Not in our library10.1248/bpb.31.1618
166.
Lu R, Liu X, Gao S, et al.New tyrosinase inhibitors from Paecilomyces gunnii. J Agric Food Chem2014;62:11917–23.
Not in our library10.1021/jf504128c
167.
Kang HS, Choi JH, Cho WK, et al.A sphingolipid and tyrosinase inhibitors from the fruiting body of Phellinus linteus. Arch Pharm Res2004;27:742–50.
Not in our library10.1007/bf02980143
168.
Morimura K, Yamazaki C, Hattori Y, et al.A tyrosinase inhibitor, daedalin a, from mycelial culture of Daedalea dickinsii. Biosci Biotechnol Biochem2007;71:2837–40.
Not in our library10.1271/bbb.70266
169.
Sharma VK, Choi J, Sharma N, et al.In vitro anti-tyrosinase activity of 5-(hydroxymethyl)-2-furfural isolated from Dictyophora indusiata. Phytother Res2004;18:841–4.
Not in our library10.1002/ptr.1428
170.
Ishihara A, Ide Y, Bito T, et al.Novel tyrosinase inhibitors from liquid culture of Neolentinus lepideus. Biosci Biotechnol Biochem2018;82:22–30.
Not in our library10.1080/09168451.2017.1415125
171.
Li X, Kim MK, Lee U, et al.Myrothenones A and B, cyclopentenone derivatives with tyrosinase inhibitory activity from the marine-derived fungus Myrothecium sp. Chem Pharm Bull (Tokyo)2005;53:453–5.
Not in our library10.1248/cpb.53.453
172.
Two Novel Tyrosinase Inhibitory Sesquiterpenes Induced by CuCl2 from a Marine-Derived Fungus Pestalotiopsis sp. Z233 · 2013
Not checked
173.
Chang TS, Tseng M, Ding HY, Shou-Ku Tai S Isolation and characterization of Streptomyces hiroshimensis strain TI-C3 with anti-tyrosinase activity. J Cosmet Sci2008;59:33–40.
Not in our library
174.
le Roes-Hill M, Prins A, Meyers PR Streptomyces swartbergensis sp. Nov., a novel tyrosinase and antibiotic producing actinobacterium. Antonie Van Leeuwenhoek2018;111:589–600.
Not in our library10.1007/s10482-017-0979-3
175.
Nakashima T, Anzai K, Kuwahara N, et al.Physicochemical characters of a tyrosinase inhibitor produced by Streptomyces roseolilacinus NBRC 12815. Biol Pharm Bull2009;32:832–6.
Not in our library10.1248/bpb.32.832
176.
Deering RW, Chen J, Sun J, et al.N-acyl dehydrotyrosines, tyrosinase inhibitors from the marine bacterium Thalassotalea sp. PP2-459. J Nat Prod2016;79:447–50.
Not in our library10.1021/acs.jnatprod.5b00972
177.
Sano T, Kaya K Oscillapeptin G, a tyrosinase inhibitor from toxic Oscillatoria agardhii. J Nat Prod1996;59:90–2.
Not in our library10.1021/np9600210
178.
Ji K, Cho YS, Kim YT Tyrosinase inhibitory and anti-oxidative effects of lactic acid bacteria isolated from dairy cow feces. Probiotics Antimicrob Proteins2018;10:43–55.
Not in our library10.1007/s12602-017-9274-x
179.
Wang GH, Chen CY, Tsai TH, et al.Evaluation of tyrosinase inhibitory and antioxidant activities of Angelica dahurica root extracts for four different probiotic bacteria fermentations. J Biosci Bioeng2017;123:679–84.
Not in our library10.1016/j.jbiosc.2017.01.003
180.
Crozier A, Jaganath IB, Clifford MN Phenols, polyphenols and tannins: an overview. Plant Secondary Metabolites2007;1–24..
Not in our library10.1002/9780470988558.ch1
181.
Sakuma K, Ogawa M, Sugibayashi K, et al.Relationship between tyrosinase inhibitory action and oxidation-reduction potential of cosmetic whitening ingredients and phenol derivatives. Arch Pharm Res1999;22:335–9.
Not in our library10.1007/bf02979054
182.
Hashimoto A, Ichihashi M, Mishima Y The mechanism of depigmentation by hydroquinone: a study on suppression and recovery processes of tyrosinase activity in the pigment cells in vivo and in vitro. Nihon Hifuka Gakkai Zasshi1984;94:797–804.
Not in our library
183.
Chen YR, Y-Y R, Lin TY, et al.Identification of an alkylhydroquinone from Rhus succedanea as an inhibitor of tyrosinase and melanogenesis. J Agric Food Chem2009;57:2200–5.
Not in our library10.1021/jf802617a
184.
Sasaki A, Yamano Y, Sugimoto S, et al.Phenolic compounds from the leaves of Breynia officinalis and their tyrosinase and melanogenesis inhibitory activities. J Nat Med2018;72:381–9.
Not in our library10.1007/s11418-017-1148-8
185.
Chawla S, deLong MA, Visscher MO, et al.Mechanism of tyrosinase inhibition by deoxyarbutin and its second-generation derivatives. Br J Dermatol2008;159:1267–74.
Not in our library10.1111/j.1365-2133.2008.08864.x
186.
Boissy RE, Visscher M, DeLong MA Deoxyarbutin: a novel reversible tyrosinase inhibitor with effective in vivo skin lightening potency. Exp Dermatol2005;14:601–8.
Not in our library10.1111/j.0906-6705.2005.00337.x
187.
Chawla S, Kvalnes K, deLong MA, et al.Deoxyarbutin and its derivatives inhibit tyrosinase activity and melanin synthesis without inducing reactive oxygen species or apoptosis. J Drugs Dermatol2012;11:e28–34.
Not in our library
188.
Tasaka K, Kamei C, Nakano S, et al.Effects of certain resorcinol derivatives on the tyrosinase activity and the growth of melanoma cells. Methods Find Exp Clin Pharmacol1998;20:99–109.
Not in our library10.1358/mf.1998.20.2.485637
189.
Kolbe L, Mann T, Gerwat W, et al.4-n-Butylresorcinol, a highly effective tyrosinase inhibitor for the topical treatment of hyperpigmentation. J Eur Acad Dermatol Venereol2013;27:19–23.
Not in our library10.1111/jdv.12051
190.
Nguyen MH, Nguyen HX, Nguyen MT, Nguyen NT Phenolic constituents from the heartwood of Artocapus altilis and their tyrosinase inhibitory activity. Nat Prod Commun2012;7:185–6.
Not in our library
191.
Ashraf Z, Rafiq M, Seo SY, et al.Synthesis, kinetic mechanism and docking studies of vanillin derivatives as inhibitors of mushroom tyrosinase. Bioorg Med Chem2015;23:5870–80.
Not in our library10.1016/j.bmc.2015.06.068
192.
Shirota S, Miyazaki K, Aiyama R, et al.Tyrosinase inhibitors from crude drugs. Biol Pharm Bull1994;17:266–9.
Not in our library10.1248/bpb.17.266
193.
Matsumoto T, Nakajima T, Iwadate T, Nihei KI Chemical synthesis and tyrosinase-inhibitory activity of isotachioside and its related glycosides. Carbohydr Res2018;465:22–8.
Not in our library10.1016/j.carres.2018.06.004
194.
The unravelling of the complex pattern of tyrosinase inhibition · 2016
No notice
195.
Garcia-Jimenez A, Teruel-Puche JA, Berna J, et al.Action of tyrosinase on alpha and beta-arbutin: a kinetic study. PLoS One2017;12:e0177330.
Not in our library10.1371/journal.pone.0177330
196.
Garcia-Molina MO, Munoz-Munoz JL, Garcia-Molina F, et al.Study of umbelliferone hydroxylation to esculetin catalyzed by polyphenol oxidase. Biol Pharm Bull2013;36:1140–5.
Not in our library10.1248/bpb.b13-00119
197.
Maria Del Mar Garcia-Molina JB, Muñoz-Muñoz JL, García-Ruiz PA, Moreno MG, Martinez JR, Garcia-Canovas F Action of tyrosinase on hydroquinone in the presence of catalytic amounts of o-diphenol. A kinetic study. React Kinet Mech Cat2014;112:305–20.
Not in our library
198.
Garcia-Molina Mdel M, Munoz Munoz JL, Martinez-Ortiz F, et al.Tyrosinase-catalyzed hydroxylation of hydroquinone, a depigmenting agent, to hydroxyhydroquinone: a kinetic study. Bioorg Med Chem2014;22:3360–9.
Not in our library10.1016/j.bmc.2014.04.048
199.
Ortiz-Ruiz CV, Berna J, Garcia-Molina Mdel M, et al.Identification of p-hydroxybenzyl alcohol, tyrosol, phloretin and its derivate phloridzin as tyrosinase substrates. Bioorg Med Chem2015;23:3738–46.
Not in our library10.1016/j.bmc.2015.04.016
200.
Ortiz-Ruiz CV, Berna J, Rodriguez-Lopez JN, et al.Tyrosinase-catalyzed hydroxylation of 4-hexylresorcinol, an antibrowning and depigmenting agent: A kinetic study. J Agric Food Chem2015;63:7032–40.
Not in our library10.1021/acs.jafc.5b02523
201.
Ortiz-Ruiz CV, Ballesta de Los Santos M, Berna J, et al.Kinetic characterization of oxyresveratrol as a tyrosinase substrate. IUBMB Life2015;67:828–36.
Not in our library10.1002/iub.1439
202.
Garcia-Jimenez A, Teruel-Puche JA, Ortiz-Ruiz CV, et al.4-n-Butylresorcinol, a depigmenting agent used in cosmetics, reacts with tyrosinase. IUBMB Life2016;68:663–72.
Not in our library10.1002/iub.1528
203.
Garcia-Jimenez A, Teruel-Puche JA, Berna J, et al.Characterization of the action of tyrosinase on resorcinols. Bioorg Med Chem2016;24:4434–43.
Not in our library10.1016/j.bmc.2016.07.048
204.
Garcia-Jimenez A, Munoz-Munoz JL, Garcia-Molina F, et al.Spectrophotometric characterization of the action of tyrosinase on p-coumaric and caffeic acids: characteristics of o-caffeoquinone. J Agric Food Chem2017;65:3378–86.
Not in our library10.1021/acs.jafc.7b00446
205.
Garcia-Jimenez A, Garcia-Molina F, Teruel-Puche JA, et al.Catalysis and inhibition of tyrosinase in the presence of cinnamic acid and some of its derivatives. Int J Biol Macromol2018;119:548–54.
Not in our library10.1016/j.ijbiomac.2018.07.173
206.
Garcia-Jimenez A, Teruel-Puche JA, Garcia-Ruiz PA, et al.Structural and kinetic considerations on the catalysis of deoxyarbutin by tyrosinase. PLoS One2017;12:e0187845.
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An Overview of Plant Phenolic Compounds and Their Importance in Human Nutrition and Management of Type 2 Diabetes · 2016
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209.
Huang WY, Cai YZ, Zhang Y Natural phenolic compounds from medicinal herbs and dietary plants: potential use for cancer prevention. Nutr Cancer2010;62:1–20.
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210.
Wang Y, Curtis-Long MJ, Lee BW, et al.Inhibition of tyrosinase activity by polyphenol compounds from Flemingia philippinensis roots. Bioorg Med Chem2014;22:1115–20.
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Xue YL, Miyakawa T, Hayashi Y, et al.Isolation and tyrosinase inhibitory effects of polyphenols from the leaves of persimmon, Diospyros kaki. J Agric Food Chem2011;59:6011–7.
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Sirat HM, Rezali MF, Ujang Z Isolation and identification of radical scavenging and tyrosinase inhibition of polyphenols from Tibouchina semidecandra L. J Agric Food Chem2010;58:10404–9.
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Orhan IE, Khan MT Flavonoid derivatives as potent tyrosinase inhibitors – a survey of recent findings between 2008–2013. Curr Top Med Chem2014;14:1486–93.
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Jegal J, Park SA, Chung K, et al.Tyrosinase inhibitory flavonoid from Juniperus communis fruits. Biosci Biotechnol Biochem2016;80:2311–7.
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Muhammad D, Hubert J, Lalun N, et al.Isolation of flavonoids and triterpenoids from the fruits of Alphitonia neocaledonica and evaluation of their anti-oxidant, anti-tyrosinase and cytotoxic activities. Phytochem Anal2015;26:137–44.
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Erdogan Orhan I, Senol FS, Aslan Erdem S, et al.Tyrosinase and cholinesterase inhibitory potential and flavonoid characterization of Viola odorata L. (Sweet Violet). Phytother Res2015;29:1304–10.
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Demirkiran O, Sabudak T, Ozturk M, Topcu G Antioxidant and tyrosinase inhibitory activities of flavonoids from Trifolium nigrescens Subsp. petrisavi. J Agric Food Chem2013;61:12598–603.
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Yao Y, Cheng X, Wang L, et al.Mushroom tyrosinase inhibitors from mung bean (Vigna radiatae L.) extracts. Int J Food Sci Nutr2012;63:358–61.
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Lou SN, Yu MW, Ho CT Tyrosinase inhibitory components of immature calamondin peel. Food Chem2012;135:1091–6.
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Hu X, Wu JW, Wang M, et al.2-Arylbenzofuran, flavonoid, and tyrosinase inhibitory constituents of Morus yunnanensis. J Nat Prod2012;75:82–7.
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Antibacterial, antioxidant and tyrosinase-inhibition activities of pomegranate fruit peel methanolic extract · 2012
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232.
Kim JM, Ko RK, Jung DS, et al.Tyrosinase inhibitory constituents from the stems of Maackia fauriei. Phytother Res2010;24:70–5.
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Alam N, Yoon KN, Lee KR, et al.Antioxidant activities and tyrosinase inhibitory effects of different extracts from Pleurotus ostreatus fruiting bodies. Mycobiology2010;38:295–301.
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Piao X, Tian Y, Mi X, Cui J tyrosinase inhibition of Potentilla bifurca. Zhongguo Zhong Yao Za Zhi2009;34:1952–4.
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Lu YH, Lin T, Wang ZT, et al.Mechanism and inhibitory effect of galangin and its flavonoid mixture from Alpinia officinarum on mushroom tyrosinase and B16 murine melanoma cells. J Enzyme Inhib Med Chem2007;22:433–8.
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236.
Jeong SH, Ryu YB, Curtis-Long MJ, et al.Tyrosinase inhibitory polyphenols from roots of Morus lhou. J Agric Food Chem2009;57:1195–203.
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Lee HS Tyrosinase inhibitors of Pulsatilla cernua root-derived materials. J Agric Food Chem2002;50:1400–3.
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Wang YL, Hu G, Zhang Q, et al.Screening and characterizing tyrosinase inhibitors from Salvia miltiorrhiza and Carthamus tinctorius by spectrum-effect relationship analysis and molecular docking. J Anal Methods Chem2018;2018:1.
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Azizuddin, Khan AM, Choudhary MI Tyrosinase inhibitory potential of natural products isolated from various medicinal plants. Nat Prod Res2011;25:750–3.
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Flavonoids: biosynthesis, biological functions, and biotechnological applications · 2012
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242.
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Manthey JA, Cesar TB, Jackson E, Mertens-Talcott S Pharmacokinetic study of nobiletin and tangeretin in rat serum by high-performance liquid chromatography-electrospray ionization-mass spectrometry. J Agric Food Chem2011;59:145–51.
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Mu Y, Li L, Hu SQ Molecular inhibitory mechanism of tricin on tyrosinase. Spectrochim Acta A Mol Biomol Spectrosc2013;107:235–40.
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Zhang L, Tao G, Chen J, Zheng ZP, Characterization of a new flavone and tyrosinase inhibition constituents from the Twigs of Morus alba L. Molecules2016;21(9):1130
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Ryu YB, Ha TJ, Curtis-Long MJ, et al Inhibitory effects on mushroom tyrosinase by flavones from the stem barks of Morus lhou (S.) Koidz. J Enzyme Inhib Med Chem2008;23:922–30.
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Kubo I, Kinst-Hori I Flavonols from saffron flower: tyrosinase inhibitory activity and inhibition mechanism. J Agric Food Chem1999;47:4121–5.
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Omar SH, Scott CJ, Hamlin AS, Obied HK Biophenols: enzymes (β-secretase, cholinesterases, histone deacetylase and tyrosinase) inhibitors from olive (Olea europaea L.)). Fitoterapia2018;128:118–29.
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Yang Z, Zhang Y, Sun L, et al.An ultrafiltration high-performance liquid chromatography coupled with diode array detector and mass spectrometry approach for screening and characterising tyrosinase inhibitors from mulberry leaves. Anal Chim Acta2012;719:87–95.
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254.
Wang Y, Zhang G, Yan J, Gong D Inhibitory effect of morin on tyrosinase: insights from spectroscopic and molecular docking studies. Food Chem2014;163:226–33.
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Zheng ZP, Zhu Q, Fan CL, et al.Phenolic tyrosinase inhibitors from the stems of Cudrania cochinchinensis. Food Funct2011;2:259–64.
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Kim JH, Cho IS, So YK, et al.Kushenol a and 8-prenylkaempferol, tyrosinase inhibitors, derived from Sophora flavescens. J Enzyme Inhib Med Chem2018;33:1048–54.
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257.
Park JS, Kim DH, Lee JK, et al.Natural ortho-dihydroxyisoflavone derivatives from aged Korean fermented soybean paste as potent tyrosinase and melanin formation inhibitors. Bioorg Med Chem Lett2010;20:1162–4.
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Chang TS, Ding HY, Lin HC Identifying 6,7,4'-trihydroxyisoflavone as a potent tyrosinase inhibitor. Biosci Biotechnol Biochem2005;69:1999–2001.
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Chang TS Two potent suicide substrates of mushroom tyrosinase: 7,8,4'-trihydroxyisoflavone and 5,7,8,4'-tetrahydroxyisoflavone. J Agric Food Chem2007;55:2010–5.
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Chen J, Yu X, Huang Y Inhibitory mechanisms of glabridin on tyrosinase. Spectrochim Acta A Mol Biomol Spectrosc2016;168:111–7.
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261.
Deshmukh K, Poddar SS Tyrosinase inhibitor-loaded microsponge drug delivery system: new approach for hyperpigmentation disorders. J Microencapsul2012;29:559–68.
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Jirawattanapong W, Saifah E, Patarapanich C Synthesis of glabridin derivatives as tyrosinase inhibitors. Arch Pharm Res2009;32:647–54.
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Nerya O, Vaya J, Musa R, et al.Glabrene and isoliquiritigenin as tyrosinase inhibitors from licorice roots. J Agric Food Chem2003;51:1201–7.
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Heo do Y, Kim YM, Lee J, et al.Desmodianone H and uncinanone B, potential tyrosinase inhibitors obtained from Lespedeza maximowiczii by using bioactivity-guided isolation. Biosci Biotechnol Biochem2014;78:943–5.
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265.
Kim HJ, Seo SH, Lee BG, Lee YS Identification of tyrosinase inhibitors from Glycyrrhiza uralensis. Planta Med2005;71:785–7.
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Kim JH, Kim HY, Kang SY, et al.Chemical constituents from Apios americana and their inhibitory activity on tyrosinase. Molecules2018;23:232. doi:.
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Si YX, Wang ZJ, Park D, et al.Effect of hesperetin on tyrosinase: inhibition kinetics integrated computational simulation study. Int J Biol Macromol2012;50:257–62.
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268.
Chiari ME, Vera DM, Palacios SM, Carpinella MC Tyrosinase inhibitory activity of a 6-isoprenoid-substituted flavanone isolated from Dalea elegans. Bioorg Med Chem2011;19:3474–82.
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269.
Hu X, Yu MH, Yan GR, et al.Isoprenylated phenolic compounds with tyrosinase inhibition from Morus nigra. J Asian Nat Prod Res2018;20:488–93.
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270.
Kim SS, Hyun CG, Choi YH, Lee NH Tyrosinase inhibitory activities of the compounds isolated from Neolitsea aciculata (Blume) Koidz. J Enzyme Inhib Med Chem2013;28:685–9.
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271.
Ko RK, Kim GO, Hyun CG, et al.Compounds with tyrosinase inhibition, elastase inhibition and DPPH radical scavenging activities from the branches of Distylium racemosum Sieb. et Zucc. Phytother Res2011;25:1451–6.
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Chai WM, Lin MZ, Wang YX, et al.Inhibition of tyrosinase by cherimoya pericarp proanthocyanidins: structural characterization, inhibitory activity and mechanism. Food Res Int2017;100:731–9.
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273.
Kim YJ, Chung JE, Kurisawa M, et al.New tyrosinase inhibitors, (+)-catechin-aldehyde polycondensates. Biomacromolecules2004;5:474–9.
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Chai WM, Huang Q, Lin MZ, et al.Condensed tannins from longan bark as inhibitor of tyrosinase: structure, activity, and mechanism. J Agric Food Chem2018;66:908–17.
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275.
Jhan JK, Chung YC, Chen GH, et al.Anthocyanin contents in the seed coat of black soya bean and their anti-human tyrosinase activity and antioxidative activity. Int J Cosmet Sci2016;38:319–24.
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Bukhari SN, Jantan I, Unsal Tan O, et al Biological activity and molecular docking studies of curcumin-related α,β-unsaturated carbonyl-based synthetic compounds as anticancer agents and mushroom tyrosinase inhibitors. J Agric Food Chem2014;62:5538–47.
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Liu J, Wu F, Chen L, et al.Biological evaluation of coumarin derivatives as mushroom tyrosinase inhibitors. Food Chem2012;135:2872–8.
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Le-Thi-Thu H, Casanola-Martin GM, Marrero-Ponce Y, et al.Novel coumarin-based tyrosinase inhibitors discovered by OECD principles-validated QSAR approach from an enlarged, balanced database. Mol Divers2011;15:507–20.
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279.
Hassan M, Ashraf Z, Abbas Q, et al.Exploration of novel human tyrosinase inhibitors by molecular modeling, docking and simulation studies. Interdiscip Sci2018;10:68–80.
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Pintus F, Matos MJ, Vilar S, et al.New insights into highly potent tyrosinase inhibitors based on 3-heteroarylcoumarins: anti-melanogenesis and antioxidant activities, and computational molecular modeling studies. Bioorg Med Chem2017;25:1687–95.
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281.
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Ahmad VU, Ullah F, Hussain J, et al.Tyrosinase inhibitors from Rhododendron collettianum and their structure–activity relationship (SAR) studies. Chem Pharm Bull (Tokyo)2004;52:1458–61.
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Ashraf Z, Rafiq M, Seo SY, et al.Design, synthesis and bioevaluation of novel umbelliferone analogues as potential mushroom tyrosinase inhibitors. J Enzyme Inhib Med Chem2015;30:874–83.
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284.
Matos MJ, Santana L, Uriarte E, et al.New halogenated phenylcoumarins as tyrosinase inhibitors. Bioorg Med Chem Lett2011;21:3342–5.
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Ueno T, Fukami H, Ohkishi H, et al.Synthesis of 3,4-dihydro-3-amino-7-hydroxycoumarin from s-methyl-l-cysteine and resorcinol by crystalline-beta-tyrosinase. Biochim Biophys Acta1970;206:476–9.
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286.
Asthana S, Zucca P, Vargiu AV, et al.Structure–activity relationship study of hydroxycoumarins and mushroom tyrosinase. J Agric Food Chem2015;63:7236–44.
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Gardelly M, Trimech B, Belkacem MA, et al.Synthesis of novel diazaphosphinanes coumarin derivatives with promoted cytotoxic and anti-tyrosinase activities. Bioorg Med Chem Lett2016;26:2450–4.
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288.
Tocco G, Fais A, Meli G, et al.PEG-immobilization of cardol and soluble polymer-supported synthesis of some cardol-coumarin derivatives: preliminary evaluation of their inhibitory activity on mushroom tyrosinase. Bioorg Med Chem Lett2009;19:36–9.
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289.
Fais A, Corda M, Era B, et al.Tyrosinase inhibitor activity of coumarin-resveratrol hybrids. Molecules2009;14:2514–20.
Not in our library10.3390/molecules14072514
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Yang HH, Oh KE, Jo YH, et al.Characterization of tyrosinase inhibitory constituents from the aerial parts of Humulus japonicus using LC-MS/MS coupled online assay. Bioorg Med Chem2018;26:509–15.
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291.
Takahashi M, Takara K, Toyozato T, Wada K A novel bioactive chalcone of Morus australis inhibits tyrosinase activity and melanin biosynthesis in B16 melanoma cells. J Oleo Sci2012;61:585–92.
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292.
Zhang X, Hu X, Hou A, Wang H Inhibitory effect of 2,4,2',4'-tetrahydroxy-3-(3-methyl-2-butenyl)-chalcone on tyrosinase activity and melanin biosynthesis. Biol Pharm Bull2009;32:86–90.
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293.
Niesen DB, Ma H, Yuan T, et al.Phenolic constituents of Carex vulpinoidea seeds and their tyrosinase inhibitory activities. Nat Prod Commun2015;10:491–3.
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294.
Suthar SK, Bansal S, Narkhede N, et al.Design, synthesis and biological evaluation of oxindole-based chalcones as small-molecule inhibitors of melanogenic tyrosinase. Chem Pharm Bull (Tokyo)2017;65:833–9.
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295.
Kim BH, Park KC, Park JH, et al.Inhibition of tyrosinase activity and melanin production by the chalcone derivative 1-(2-cyclohexylmethoxy-6-hydroxy-phenyl)-3-(4-hydroxymethyl-phenyl)-propenone. Biochem Biophys Res Commun2016;480:648–54.
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296.
Niu C, Yin L, Nie LF, et al.Synthesis and bioactivity of novel isoxazole chalcone derivatives on tyrosinase and melanin synthesis in murine B16 cells for the treatment of vitiligo. Bioorg Med Chem2016;24:5440–8.
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297.
Radhakrishnan SK, Shimmon RG, Conn C, Baker AT Evaluation of novel chalcone oximes as inhibitors of tyrosinase and melanin formation in B16 cells. Arch Pharm (Weinheim)2016;349:20–9.
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298.
Radhakrishnan SK, Shimmon RG, Conn C, Baker AT Inhibitory kinetics of azachalcones and their oximes on mushroom tyrosinase: a facile solid-state synthesis. Chem Biodivers2016;13:531–8.
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299.
Dong X, Zhang Y, He JL, et al.Preparation of tyrosinase inhibitors and antibrowning agents using green technology. Food Chem2016;197:589–96.
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300.
Jun N, Hong G, Jun K Synthesis and evaluation of 2',4',6'-trihydroxychalcones as a new class of tyrosinase inhibitors. Bioorg Med Chem2007;15:2396–402.
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301.
Radhakrishnan S, Shimmon R, Conn C, Baker A Integrated kinetic studies and computational analysis on naphthyl chalcones as mushroom tyrosinase inhibitors. Bioorg Med Chem Lett2015;25:4085–91.
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302.
Liu J, Chen C, Wu F, Zhao L Microwave-assisted synthesis and tyrosinase inhibitory activity of chalcone derivatives. Chem Biol Drug Des2013;82:39–47.
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303.
Nerya O, Musa R, Khatib S, et al.Chalcones as potent tyrosinase inhibitors: the effect of hydroxyl positions and numbers. Phytochemistry2004;65:1389–95.
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304.
Okombi S, Rival D, Bonnet S, et al.Discovery of benzylidenebenzofuran-3(2H)-one (aurones) as inhibitors of tyrosinase derived from human melanocytes. J Med Chem2006;49:329–33.
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Zhu JJ, Yan GR, Xu ZJ, et al.Inhibitory effects of (2'R)-2',3'-dihydro-2'-(1-hydroxy-1-methylethyl)-2,6'-bibenzofuran-6,4'-diol on mushroom tyrosinase and melanogenesis in B16-F10 melanoma cells. Phytother Res2015;29:1040–5.
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306.
Hu X, Wang M, Yan GR, et al.2-Arylbenzofuran and tyrosinase inhibitory constituents of Morus notabilis. J Asian Nat Prod Res2012;14:1103–8.
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307.
Koirala P, Seong SH, Zhou Y, et al.Structure(−)activity relationship of the tyrosinase inhibitors kuwanon G, mulberrofuran G, and albanol B from Morus species: a kinetics and molecular docking study. Molecules2018;23:1413. doi:.
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308.
Wang Y, Xu L, Gao W, et al.Isoprenylated phenolic compounds from Morus macroura as potent tyrosinase inhibitors. Planta Med2018;84:336–43.
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309.
Lin YF, Hu YH, Lin HT, et al.Inhibitory effects of propyl gallate on tyrosinase and its application in controlling pericarp browning of harvested longan fruits. J Agric Food Chem2013;61:2889–95.
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310.
Lopes TIB, Coelho RG, Honda NK Inhibition of mushroom tyrosinase activity by orsellinates. Chem Pharm Bull (Tokyo)2018;66:61–4.
Not in our library10.1248/cpb.c17-00502
311.
Lim JY, Ishiguro K, Kubo I Tyrosinase inhibitory p-coumaric acid from ginseng leaves. Phytother Res1999;13:371–5.
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312.
Cabanes J, Garcia-Carmona F, Garcia-Canovas F, et al.Kinetic study on the slow inhibition of epidermis tyrosinase by m-coumaric acid. Biochim Biophys Acta1984;790:101–7.
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313.
An SM, Koh JS, Boo YC p-Coumaric acid not only inhibits human tyrosinase activity in vitro but also melanogenesis in cells exposed to UVB. Phytother Res2010;24:1175–80.
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Hu YH, Chen QX, Cui Y, et al.4-Hydroxy cinnamic acid as mushroom preservation: anti-tyrosinase activity kinetics and application. Int J Biol Macromol2016;86:489–95.
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Kwak SY, Yang JK, Choi HR, et al.Synthesis and dual biological effects of hydroxycinnamoyl phenylalanyl/prolyl hydroxamic acid derivatives as tyrosinase inhibitor and antioxidant. Bioorg Med Chem Lett2013;23:1136–42.
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Bernard P, Berthon JY Resveratrol: an original mechanism on tyrosinase inhibition. Int J Cosmet Sci2000;22:219–26.
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Park J, Boo YC Isolation of resveratrol from Vitis Viniferae caulis and its potent inhibition of human tyrosinase. Evid Based Complement Alternat Med2013;2013:645257.
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Gilly R, Mara D, Oded S, Zohar K Resveratrol and a novel tyrosinase in carignan grape juice. J Agric Food Chem2001;49:1479–85.
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Lee N, Kim EJ, Kim BG Regioselective hydroxylation of trans-resveratrol via inhibition of tyrosinase from Streptomyces avermitilis MA4680. ACS Chem Biol2012;7:1687–92.
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Inhibitory Effects of Resveratrol Analogs on Mushroom Tyrosinase Activity · 2012
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Shin NH, Ryu SY, Choi EJ, et al.Oxyresveratrol as the potent inhibitor on DOPA oxidase activity of mushroom tyrosinase. Biochem Biophys Res Commun1998;243:801–3.
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Zheng ZP, Tan HY, Wang M Tyrosinase inhibition constituents from the roots of Morus australis. Fitoterapia2012;83:1008–13.
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Bae SJ, Ha YM, Kim JA, et al.A novel synthesized tyrosinase inhibitor: (E)-2-((2,4-dihydroxyphenyl) diazenyl) phenyl 4-methylbenzenesulfonate as an azo-resveratrol analog. Biosci Biotechnol Biochem2013;77:65–72.
Not in our library10.1271/bbb.120547
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Song YM, Ha YM, Kim JA, et al.Synthesis of novel azo-resveratrol, azo-oxyresveratrol and their derivatives as potent tyrosinase inhibitors. Bioorg Med Chem Lett2012;22:7451–5.
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Yanagihara M, Yoshimatsu M, Inoue A, et al.Inhibitory effect of gnetin c, a resveratrol dimer from melinjo (Gnetum gnemon), on tyrosinase activity and melanin biosynthesis. Biol Pharm Bull2012;35:993–6.
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Kim YM, Yun J, Lee CK, et al.Oxyresveratrol and hydroxystilbene compounds. Inhibitory effect on tyrosinase and mechanism of action. J Biol Chem2002;277:16340–4.
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Ohguchi K, Tanaka T, Kido T, et al.Effects of hydroxystilbene derivatives on tyrosinase activity. Biochem Biophys Res Commun2003;307:861–3.
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Kim DH, Kim JH, Baek SH, et al.Enhancement of tyrosinase inhibition of the extract of Veratrum patulum using cellulase. Biotechnol Bioeng2004;87:849–54.
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Ismail T, Shafi S, Srinivas J, et al.Synthesis and tyrosinase inhibition activity of trans-stilbene derivatives. Bioorg Chem2016;64:97–102.
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Lima LL, Lima RM, da Silva AF, et al.Azastilbene analogs as tyrosinase inhibitors: new molecules with depigmenting potential. Scientific World Journal2013;2013:274643. doi: 10.1155/2013/274643.
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Choi J, Bae SJ, Ha YM, et al.A newly synthesized, potent tyrosinase inhibitor: 5-(6-hydroxy-2-naphthyl)-1,2,3-benzenetriol. Bioorg Med Chem Lett2010;20:4882–4.
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Song S, Lee H, Jin Y, et al.Syntheses of hydroxy substituted 2-phenyl-naphthalenes as inhibitors of tyrosinase. Bioorg Med Chem Lett2007;17:461–4.
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Ha YM, Chung SW, Song S, et al.4-(6-Hydroxy-2-naphthyl)-1,3-bezendiol: a potent, new tyrosinase inhibitor. Biol Pharm Bull2007;30:1711–5.
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Satooka H, Kubo I Resveratrol as a kcat type inhibitor for tyrosinase: potentiated melanogenesis inhibitor. Bioorg Med Chem2012;20:1090–9.
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Fachinetti N, Rigon RB, Eloy JO, et al.Comparative study of glyceryl behenate or polyoxyethylene 40 stearate-based lipid carriers for trans-resveratrol delivery: development, characterization and evaluation of the in vitro tyrosinase inhibition. AAPS PharmSciTech2018;19:1401–9.
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Wu B, Zhang X, Wu X New lignan glucosides with tyrosinase inhibitory activities from exocarp of Castanea henryi. Carbohydr Res2012;355:45–9.
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Karioti A, Protopappa A, Megoulas N, Skaltsa H Identification of tyrosinase inhibitors from Marrubium velutinum and Marrubium cylleneum. Bioorg Med Chem2007;15:2708–14.
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Wu YY, Huang XX, Wu J, et al.A new cyclolignan glycoside from the tubers of Pinellia ternata. J Asian Nat Prod Res2015;17:1097–103.
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Huang XX, Liu QB, Wu J, et al.Antioxidant and tyrosinase inhibitory effects of neolignan glycosides from Crataegus pinnatifida seeds. Planta Med2014;80:1732–8.
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Ashraf Z, Rafiq M, Nadeem H, et al.Carvacrol derivatives as mushroom tyrosinase inhibitors; synthesis, kinetics mechanism and molecular docking studies. PLoS One2017; 12:e0178069.
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Mutschlechner B, Rainer B, Schwaiger S, Stuppner H Tyrosinase inhibitors from the aerial parts of Wulfenia carinthiaca Jacq. Chem Biodivers2018;15:e1800014
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Tan C, Zhu W, Lu Y Aloin, cinnamic acid and sophorcarpidine are potent inhibitors of tyrosinase. Chin Med J (Engl)2002;115:1859–62.
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Leu YL, Hwang TL, Hu JW, Fang JY Anthraquinones from Polygonum cuspidatum as tyrosinase inhibitors for dermal use. Phytother Res2008;22:552–6.
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Kim YJ, No JK, Lee JH, Chung HY 4,4'-Dihydroxybiphenyl as a new potent tyrosinase inhibitor. Biol Pharm Bull2005;28:323–7.
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van Rensburg WJ, Ferreira D, Malan E, Steenkamp JA Tyrosinase catalysed biphenyl construction from flavan-3-ol substrates. Phytochemistry2000;53:285–92.
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Oyama T, Yoshimori A, Takahashi S, et al.Structural insight into the active site of mushroom tyrosinase using phenylbenzoic acid derivatives. Bioorg Med Chem Lett2017;27:2868–72.
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Le Mellay-Hamon V, Criton M Phenylethylamide and phenylmethylamide derivatives as new tyrosinase inhibitors. Biol Pharm Bull2009;32:301–3.
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Chiku K, Dohi H, Saito A, et al.Enzymatic synthesis of 4-hydroxyphenyl beta-D-oligoxylosides and their notable tyrosinase inhibitory activity. Biosci Biotechnol Biochem2009;73:1123–8.
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Saboury AA, Zolghadri S, Haghbeen K, Moosavi-Movahedi AA The inhibitory effect of benzenethiol on the cresolase and catecholase activities of mushroom tyrosinase. J Enzyme Inhib Med Chem2006;21:711–7.
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Shareefi Borojerdi S, Haghbeen K, Asghar Karkhane A, et al.Successful resonance Raman study of cresolase activity of mushroom tyrosinase. Biochem Biophys Res Commun2004;314:925–30.
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361.
Saghaie L, Pourfarzam M, Fassihi A, Sartippour B Synthesis and tyrosinase inhibitory properties of some novel derivatives of kojic acid. Res Pharm Sci2013;8:233–42.
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362.
Li DF, Hu PP, Liu MS, et al.Design and synthesis of hydroxypyridinone-l-phenylalanine conjugates as potential tyrosinase inhibitors. J Agric Food Chem2013;61:6597–603.
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Dong H, Liu J, Liu X, et al.Molecular docking and QSAR analyses of aromatic heterocycle thiosemicarbazone analogues for finding novel tyrosinase inhibitors. Bioorg Chem2017;75:106–17.
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Song S, You A, Chen Z, et al.Study on the design, synthesis and structure-activity relationships of new thiosemicarbazone compounds as tyrosinase inhibitors. Eur J Med Chem2017;139:815–25.
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Xie J, Dong H, Yu Y, Cao S Inhibitory effect of synthetic aromatic heterocycle thiosemicarbazone derivatives on mushroom tyrosinase: insights from fluorescence, (1)H-NMR titration and molecular docking studies. Food Chem2016;190:709–16.
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Zhu TH, Cao SW, Yu YY Synthesis, characterization and biological evaluation of paeonol thiosemicarbazone analogues as mushroom tyrosinase inhibitors. Int J Biol Macromol2013;62:589–95.
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Xu J, Liu J, Zhu X, et al.Novel inhibitors of tyrosinase produced by the 4-substitution of TCT. Food Chem2017;221:1530–8.
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Chen LH, Hu YH, Song W, et al.Synthesis and antityrosinase mechanism of benzaldehyde thiosemicarbazones: novel tyrosinase inhibitors. J Agric Food Chem2012;60:1542–7.
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Li ZC, Chen LH, Yu XJ, et al.Inhibition kinetics of chlorobenzaldehyde thiosemicarbazones on mushroom tyrosinase. J Agric Food Chem2010;58:12537–40.
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El-Sadek MM, Hassan SY, Abdelwahab HE, Yacout GA Synthesis of new 1,3,4-thiadiazole and 1,2,3,4-oxathiadiazole derivatives from carbohydrate precursors and study of their effect on tyrosinase enzyme. Molecules2012;17:8378–96.
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Yi W, Dubois C, Yahiaoui S, et al.Refinement of arylthiosemicarbazone pharmacophore in inhibition of mushroom tyrosinase. Eur J Med Chem2011;46:4330–5.
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Yang MH, Chen CM, Hu YH, et al.Inhibitory kinetics of DABT and DABPT as novel tyrosinase inhibitors. J Biosci Bioeng2013;115:514–7.
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Liu J, Wu F, Chen C Design and synthesis of aloe-emodin derivatives as potent anti-tyrosinase, antibacterial and anti-inflammatory agents. Bioorg Med Chem Lett2015;25:5142–6.
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You A, Zhou J, Song S, et al.Structure-based modification of 3-/4-aminoacetophenones giving a profound change of activity on tyrosinase: from potent activators to highly efficient inhibitors. Eur J Med Chem2015;93:255–62.
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Yi W, Cao R, Wen H, et al.Discovery of 4-functionalized phenyl-o-beta-d-glycosides as a new class of mushroom tyrosinase inhibitors. Bioorg Med Chem Lett2009;19:6157–60.
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Liu J, Yi W, Wan Y, et al.1-(1-Arylethylidene)thiosemicarbazide derivatives: a new class of tyrosinase inhibitors. Bioorg Med Chem2008;16:1096–102.
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Yan Q, Cao R, Yi W, et al.Synthesis and evaluation of 5-benzylidene(thio)barbiturate-beta-d-glycosides as mushroom tyrosinase inhibitors. Bioorg Med Chem Lett2009;19:4055–8.
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Gheibi N, Saboury AA, Mansuri-Torshizi H, et al.The inhibition effect of some n-alkyl dithiocarbamates on mushroom tyrosinase. J Enzyme Inhib Med Chem2005;20:393–9.
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Amin E, Saboury AA, Mansouri-Torshizi H, et al.Evaluation of p-phenylene-bis and phenyl dithiocarbamate sodium salts as inhibitors of mushroom tyrosinase. Acta Biochim Pol2010;57:277–83.
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Amin E, Saboury AA, Mansuri-Torshizi H, Moosavi-Movahedi AA Potent inhibitory effects of benzyl and p-xylidine-bis dithiocarbamate sodium salts on activities of mushroom tyrosinase. J Enzyme Inhib Med Chem2010;25:272–81.
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Zarivi O, Bonfigli A, Cesare P, et al.Truffle thio-flavours reversibly inhibit truffle tyrosinase. FEMS Microbiol Lett2003;220:81–8.
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Choi J, Jee JG Repositioning of thiourea-containing drugs as tyrosinase inhibitors. Int J Mol Sci2015;16:28534–48.
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Loriga M, Paglietti G, Sparatore F, et al.Synthesis of substituted DL-3(5-benzazolyl)alanines as dopa and alpha-methyldopa analogs and their effects on dopamine beta-hydroxylase, tyrosinase and diphenoloxidase. Farmaco1992;47:439–48.
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Channar PA, Saeed A, Larik FA, et al.Synthesis of aryl pyrazole via suzuki coupling reaction, in vitro mushroom tyrosinase enzyme inhibition assay and in silico comparative molecular docking analysis with kojic acid. Bioorg Chem2018;79:293–300.
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Gawande SS, Warangkar SC, Bandgar BP, Khobragade CN Synthesis of new heterocyclic hybrids based on pyrazole and thiazolidinone scaffolds as potent inhibitors of tyrosinase. Bioorg Med Chem2013;21:2772–7.
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Zhou Z, Zhuo J, Yan S, Ma L Design and synthesis of 3,5-diaryl-4,5-dihydro-1H-pyrazoles as new tyrosinase inhibitors. Bioorg Med Chem2013;21:2156–62.
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393.
Bandgar BP, Totre JV, Gawande SS, et al.Synthesis of novel 3,5-diaryl pyrazole derivatives using combinatorial chemistry as inhibitors of tyrosinase as well as potent anticancer, anti-inflammatory agents. Bioorg Med Chem2010;18:6149–55.
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Khan KM, Maharvi GM, Khan MT, et al.A facile and improved synthesis of sildenafil (viagra) analogs through solid support microwave irradiation possessing tyrosinase inhibitory potential, their conformational analysis and molecular dynamics simulation studies. Mol Divers2005;9:15–26.
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Mojzych M, Tarasiuk P, Kotwica-Mojzych K, et al.Synthesis of chiral pyrazolo[4,3-e][1,2,4]triazine sulfonamides with tyrosinase and urease inhibitory activity. J Enzyme Inhib Med Chem2017;32:99–105.
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Mojzych M, Dolashki A, Voelter W Synthesis of pyrazolo[4,3-e][1,2,4]triazine sulfonamides, novel sildenafil analogs with tyrosinase inhibitory activity. Bioorg Med Chem2014;22:6616–24.
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Qamar R, Saeed A, Larik FA, et al.Novel 1,3-oxazine-tetrazole hybrids as mushroom tyrosinase inhibitors and free radical scavengers: synthesis, kinetic mechanism and molecular docking studies. Chem Biol Drug Des2018; doi:.
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Nikalje APG, Gawhane P, Tiwari S, et al.Ultrasound promoted green synthesis, docking study of indole spliced thiadiazole, alpha-amino phosphonates as anticancer agents and anti-tyrosinase agents. Anticancer Agents Med Chem2018;18:1. doi:.
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Mahdavi M, Ashtari A, Khoshneviszadeh M, et al.Synthesis of new benzimidazole-1,2,3-triazole hybrids as tyrosinase inhibitors. Chem Biodivers2018; 15:e1800120.
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Chekir S, Debbabi M, Regazzetti A, et al.Design, synthesis and biological evaluation of novel 1,2,3-triazole linked coumarinopyrazole conjugates as potent anticholinesterase, anti-5-lipoxygenase, anti-tyrosinase and anti-cancer agents. Bioorg Chem2018;80:189–94.
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Kim SJ, Yang J, Lee S, et al.The tyrosinase inhibitory effects of isoxazolone derivatives with a (z)-beta-phenyl-alpha, beta-unsaturated carbonyl scaffold. Bioorg Med Chem2018; doi:.
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Hamidian H, Tagizadeh R, Fozooni S, et al.Synthesis of novel azo compounds containing 5(4h)-oxazolone ring as potent tyrosinase inhibitors. Bioorg Med Chem2013;21:2088–92.
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Heitz MP, Rupp JW Determining mushroom tyrosinase inhibition by imidazolium ionic liquids: a spectroscopic and molecular docking study. Int J Biol Macromol2018;107:1971–81.
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Mann T, Scherner C, Rohm KH, Kolbe L Structure–activity relationships of thiazolyl resorcinols, potent and selective inhibitors of human tyrosinase. Int J Mol Sci2018;19:690. doi:.
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Rezaei M, Mohammadi HT, Mahdavi A, et al.Evaluation of thiazolidinone derivatives as a new class of mushroom tyrosinase inhibitors. Int J Biol Macromol2018;108:205–13.
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Kim SH, Ha YM, Moon KM, et al.Anti-melanogenic effect of (z)-5-(2,4-dihydroxybenzylidene) thiazolidine-2,4-dione, a novel tyrosinase inhibitor. Arch Pharm Res2013;36:1189–97.
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Ha YM, Park YJ, Kim JA, et al.Design and synthesis of 5-(substituted benzylidene)thiazolidine-2,4-dione derivatives as novel tyrosinase inhibitors. Eur J Med Chem2012;49:245–52.
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Han YK, Park YJ, Ha YM, et al.Characterization of a novel tyrosinase inhibitor, (2RS,4R)-2-(2,4-dihydroxyphenyl)thiazolidine-4-carboxylic acid (MHY384). Biochim Biophys Acta2012;1820:542–9.
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Ha YM, Park YJ, Lee JY, et al.Design, synthesis and biological evaluation of 2-(substituted phenyl)thiazolidine-4-carboxylic acid derivatives as novel tyrosinase inhibitors. Biochimie2012;94:533–40.
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Jung HJ, Lee MJ, Park YJ, et al.A novel synthetic compound, (z)-5-(3-hydroxy-4-methoxybenzylidene)-2-iminothiazolidin-4-one (mhy773) inhibits mushroom tyrosinase. Biosci Biotechnol Biochem2018;82:759–67. doi:.
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Kahn V Effect of kojic acid on the oxidation of DL-dopa, norepinephrine, and dopamine by mushroom tyrosinase. Pigment Cell Res1995;8:234–40.
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Xie W, Zhang H, He J, et al.Synthesis and biological evaluation of novel hydroxybenzaldehyde-based kojic acid analogues as inhibitors of mushroom tyrosinase. Bioorg Med Chem Lett2017;27:530–2.
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Chen MJ, Hung CC, Chen YR, et al.Novel synthetic kojic acid-methimazole derivatives inhibit mushroom tyrosinase and melanogenesis. J Biosci Bioeng2016;122:666–72.
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Asadzadeh A, Sirous H, Pourfarzam M, et al.In vitro and in silico studies of the inhibitory effects of some novel kojic acid derivatives on tyrosinase enzyme. Iran J Basic Med Sci2016;19:132–44.
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Xie W, Zhang J, Ma X, et al.Synthesis and biological evaluation of kojic acid derivatives containing 1,2,4-triazole as potent tyrosinase inhibitors. Chem Biol Drug Des2015;86:1087–92.
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416.
Lima CR, Silva JR, de Tassia Carvalho Cardoso E, et al.Combined kinetic studies and computational analysis on kojic acid analogous as tyrosinase inhibitors. Molecules2014;19:9591–605.
Not in our library10.3390/molecules19079591
417.
Noh JM, Kwak SY, Seo HS, et al.Kojic acid-amino acid conjugates as tyrosinase inhibitors. Bioorg Med Chem Lett2009;19:5586–9.
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418.
Lee YS, Park JH, Kim MH, et al.Synthesis of tyrosinase inhibitory kojic acid derivative. Arch Pharm (Weinheim)2006;339:111–4.
Not in our library10.1002/ardp.200500213
419.
Cho JC, Rho HS, Joo YH, et al.Depigmenting activities of kojic acid derivatives without tyrosinase inhibitory activities. Bioorg Med Chem Lett2012;22:4159–62.
Not in our library10.1016/j.bmcl.2012.04.046
420.
Nihei KI, Kubo I Substituent effect of benzaldehydes on tyrosinase inhibition. Plant Physiol Biochem2017;112:278–82.
Not in our library10.1016/j.plaphy.2017.01.009
421.
Rafiee M, Javaheri M A theoretical study of benzaldehyde derivatives as tyrosinase inhibitors using ab initio calculated NQCC parameters. Mol Biol Res Commun2015;4:151–9.
Not in our library
422.
Ley JP, Bertram HJ Hydroxy- or methoxy-substituted benzaldoximes and benzaldehyde-o-alkyloximes as tyrosinase inhibitors. Bioorg Med Chem2001;9:1879–85.
Not in our library10.1016/s0968-0896(01)00084-0
423.
Lopes ND, Chaves OA, de Oliveira MCC, et al.Novel piperonal 1,3,4-thiadiazolium-2-phenylamines mesoionic derivatives: synthesis, tyrosinase inhibition evaluation and HSA binding study. Int J Biol Macromol2018;112:1062–72.
Not in our library10.1016/j.ijbiomac.2018.02.050
424.
Yi W, Cao R, Peng W, et al.Synthesis and biological evaluation of novel 4-hydroxybenzaldehyde derivatives as tyrosinase inhibitors. Eur J Med Chem2010;45:639–46.
Not in our library10.1016/j.ejmech.2009.11.007
425.
Ha TJ, Tamura S, Kubo I Effects of mushroom tyrosinase on anisaldehyde. J Agric Food Chem2005;53:7024–8.
Not in our library10.1021/jf047943q
426.
Yu L Inhibitory effects of (s)- and (r)-6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acids on tyrosinase activity. J Agric Food Chem2003;51:2344–7.
Not in our library10.1021/jf0208379
427.
Alijanianzadeh M, Saboury AA, Mansuri-Torshizi H, et al.The inhibitory effect of some new synthesized xanthates on mushroom tyrosinase activities. J Enzyme Inhib Med Chem2007;22:239–46.
Not in our library10.1080/14756360601114536
428.
Saboury AA, Alijanianzadeh M, Mansoori-Torshizi H The role of alkyl chain length in the inhibitory effect n-alkyl xanthates on mushroom tyrosinase activities. Acta Biochim Pol2007;54:183–91.
Not in our library
429.
Xing R, Wang F, Zheng A, et al.Biological evaluation of two Keggin-type polyoxometalates containing glycine as mushroom tyrosinase inhibitors. Biotechnol Appl Biochem2016;63:746–50.
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430.
Park KH, Lee JR, Hahn HS, et al.Inhibitory effect of ammonium tetrathiotungstate on tyrosinase and its kinetic mechanism. Chem Pharm Bull (Tokyo)2006;54:1266–70.
Not in our library10.1248/cpb.54.1266
431.
Chen XX, Zhang J, Chai WM, et al.Reversible and competitive inhibitory kinetics of amoxicillin on mushroom tyrosinase. Int J Biol Macromol2013;62:726–33.
Not in our library10.1016/j.ijbiomac.2013.09.052
432.
Hemachandran H, Jain F, Mohan S, et al.Glandular hair constituents of Mallotus philippinensis muell. Fruit act as tyrosinase inhibitors: insights from enzyme kinetics and simulation study. Int J Biol Macromol2018;107:1675–82.
Not in our library10.1016/j.ijbiomac.2017.10.036
433.
Lin YF, Hu YH, Jia YL, et al.Inhibitory effects of naphthols on the activity of mushroom tyrosinase. Int J Biol Macromol2012;51:32–6.
Not in our library10.1016/j.ijbiomac.2012.04.026
434.
Wu LC, Chen YC, Ho JA, Yang CS Inhibitory effect of red koji extracts on mushroom tyrosinase. J Agric Food Chem2003;51:4240–6.
Not in our library10.1021/jf034064f
435.
Fourche J, Jensen H, Neuzil E, Bellegarde B [Alpha-hydrazinophloretic acid, competitive inhibitor of fungal tyrosinase]. CR Hebd Seances Acad Sci Ser D1977;284:2163–6.
Not in our library
436.
Gheibi N, Saboury AA, Haghbeen K, Moosavi-Movahedi AA Activity and structural changes of mushroom tyrosinase induced by n-alkyl sulfates. Colloids Surf B Biointerfaces2005;45:104–7.
Not in our library10.1016/j.colsurfb.2005.08.001
437.
Jena K, Pandey JP, Kumari R, et al.Tasar silk fiber waste sericin: new source for anti-elastase, anti-tyrosinase and anti-oxidant compounds. Int J Biol Macromol2018;114:1102–8.
Not in our library10.1016/j.ijbiomac.2018.03.058
438.
Hwang SH, Wang Z, Suh HW, Lim SS Antioxidant activity and inhibitory effects of 2-hydroxy-3-methylcyclopent-2-enone isolated from ribose-histidine maillard reaction products on aldose reductase and tyrosinase. Food Funct2018;9:1790–9.
Not in our library10.1039/c7fo01438d
439.
Huang XX, Yan ZY, Liu S, et al.Investigation of chemical constituents of safflower and their tyrosinase inhibitory activity. J Asian Nat Prod Res2018; 1–9. doi: 10.1080/10286020.2018.1430775.
Not in our library10.1080/10286020.2018.1430775
440.
Alijanianzadeh M, Saboury AA, Ganjali MR, et al.The inhibitory effect of ethylenediamine on mushroom tyrosinase. Int J Biol Macromol2012;50:573–7.
Not in our library10.1016/j.ijbiomac.2012.01.030
441.
Wang Y, Hao MM, Sun Y, et al.Synergistic promotion on tyrosinase inhibition by antioxidants. Molecules2018;23:106. doi:.
Not in our library10.3390/molecules23010106
442.
Liang C, Lim JH, Kim SH, Kim DS Dioscin: a synergistic tyrosinase inhibitor from the roots of Smilax china. Food Chem2012;134:1146–8.
Not in our library10.1016/j.foodchem.2012.03.003
443.
Jin YH, Lee SJ, Chung MH, et al.Aloesin and arbutin inhibit tyrosinase activity in a synergistic manner via a different action mechanism. Arch Pharm Res1999;22:232–6.
Not in our library10.1007/bf02976355
444.
Schved F, Kahn V Synergism exerted by 4-methyl catechol, catechol, and their respective quinones on the rate of DL-dopa oxidation by mushroom tyrosinase. Pigment Cell Res1992;5:41–8.
Not in our library10.1111/j.1600-0749.1992.tb00781.x
445.
Chen X, Haniu A, Kashiwagi T, et al.The evaluation of the synergistic effect of 3-(2,4-dihydroxyphenyl)propionic acid and L-ascorbic acid on tyrosinase inhibition. Z Naturforsch C2017;72:119–21.
Not in our library10.1515/znc-2016-0095
446.
Hseu YC, Cheng KC, Lin YC, et al.Synergistic effects of linderanolide B combined with arbutin, PTU or kojic acid on tyrosinase inhibition. Curr Pharm Biotechnol2015;16:1120–6.
Not in our library10.2174/1389201016666150907112819

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