No retraction, correction or concern found when last checked on Oct 21, 2026.

The SARS‐CoV‐2 main protease (M pro ): Structure, function, and emerging therapies for COVID‐19

Qing Hu, Yuan Xiong, Guang‐Hao Zhu and 4 more

MedComm · 2022 · Review · CC BY

Abstract

The main proteases (M pro ), also termed 3‐chymotrypsin‐like proteases (3CL pro ), are a class of highly conserved cysteine hydrolases in β‐coronaviruses. Increasing evidence has demonstrated that 3CL pro s play an indispensable role in viral replication and have been recognized as key targets for preventing and treating coronavirus‐caused infectious diseases, including COVID‐19. This review is focused on the structural features and biological function of the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) main protease M pro (also known as 3CL pro ), as well as recent advances in discovering and developing SARS‐CoV‐2 3CL pro inhibitors. To better understand the characteristics of SARS‐CoV‐2 3CL pro inhibitors, the inhibition activities, inhibitory mechanisms, and key structural features of various 3CL pro inhibitors (including marketed drugs, peptidomimetic, and non‐peptidomimetic synthetic compounds, as well as natural compounds and their derivatives) are summarized comprehensively. Meanwhile, the challenges in this field are highlighted, while future directions for designing and developing efficacious 3CL pro inhibitors as novel anti‐coronavirus therapies are also proposed. Collectively, all information and knowledge presented here are very helpful for understanding the structural features and inhibitory mechanisms of SARS‐CoV‐2 3CL pro inhibitors, which offers new insights or inspiration to medicinal chemists for designing and developing more efficacious 3CL pro inhibitors as novel anti‐coronavirus agents.

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Ma C, Sacco MD, Hurst B, et al. Boceprevir, GC‐376, and calpain inhibitors II, XII inhibit SARS‐CoV‐2 viral replication by targeting the viral main protease. Cell Res. 2020;30(8):678‐692.
Not in our library10.1038/s41422-020-0356-z
113.
Milligan JC, Zeisner TU, Papageorgiou G, et al. Identifying SARS‐CoV‐2 antiviral compounds by screening for small molecule inhibitors of Nsp5 main protease. Biochem J. 2021;478(13):2499‐2515.
Not in our library10.1042/bcj20210197
114.
Wang Y, Xu B, Ma S, et al. Discovery of SARS‐CoV‐2 3CL(Pro) peptidomimetic inhibitors through the catalytic dyad histidine‐specific protein–ligand interactions. Int J Mol Sci. 2022;23(4):2392.
Not in our library10.3390/ijms23042392
115.
Elseginy SA, Fayed B, Hamdy R, et al. Promising anti‐SARS‐CoV‐2 drugs by effective dual targeting against the viral and host proteases. Bioorg Med Chem Lett. 2021;43:128099.
Not in our library10.1016/j.bmcl.2021.128099
116.
Ge R, Shen Z, Yin J, et al. Discovery of SARS‐CoV‐2 main protease covalent inhibitors from a DNA‐encoded library selection. SLAS Discov. 2022;27(2):79‐85.
Not in our library10.1016/j.slasd.2022.01.001
117.
A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication · 2021
No notice
118.
Konno S, Kobayashi K, Senda M, et al. 3CL protease inhibitors with an electrophilic arylketone moiety as anti‐SARS‐CoV‐2 agents. J Med Chem. 2022;65(4):2926‐2939.
Not in our library10.1021/acs.jmedchem.1c00665
119.
Kitamura N, Sacco MD, Ma C, et al. Expedited approach toward the rational design of noncovalent SARS‐CoV‐2 main protease inhibitors. J Med Chem. 2022;65(4):2848‐2865.
Not in our library10.1021/acs.jmedchem.1c00509
120.
Bai B, Arutyunova E, Khan MB, et al. Peptidomimetic nitrile warheads as SARS‐CoV‐2 3CL protease inhibitors. RSC Med Chem. 2021;12(10):1722‐1730.
Not in our library10.1039/d1md00247c
121.
Lee JY, Kuo CJ, Shin JS, et al. Identification of non‐covalent 3C‐like protease inhibitors against severe acute respiratory syndrome coronavirus‐2 via virtual screening of a Korean compound library. Bioorg Med Chem Lett. 2021;42:128067.
Not in our library10.1016/j.bmcl.2021.128067
122.
Simmons G, Gosalia DN, Rennekamp AJ, et al. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc Natl Acad Sci U S A. 2005;102(33):11876‐11881.
Not in our library10.1073/pnas.0505577102
123.
Cathepsin L in COVID-19: From Pharmacological Evidences to Genetics · 2020
No notice
124.
Cell entry mechanisms of SARS-CoV-2 · 2020
No notice
125.
Costanzi E, Kuzikov M, Esposito F, et al. Structural and biochemical analysis of the dual inhibition of MG‐132 against SARS‐CoV‐2 main protease (Mpro/3CLpro) and human cathepsin‐L. Int J Mol Sci. 2021;22(21):11779.
Not in our library10.3390/ijms222111779
126.
Li L, Chenna BC, Yang KS, et al. Self‐masked aldehyde inhibitors: a novel strategy for inhibiting cysteine proteases. J Med Chem. 2021;64(15):11267‐11287.
Not in our library10.1021/acs.jmedchem.1c00628
127.
Al‐Wahaibi LH, Mostafa A, Mostafa YA, et al. Discovery of novel oxazole‐based macrocycles as anti‐coronaviral agents targeting SARS‐CoV‐2 main protease. Bioorg Chem. 2021;116:105363.
Not in our library10.1016/j.bioorg.2021.105363
128.
Johansen‐Leete J, Ullrich S, Fry SE, et al. Antiviral cyclic peptides targeting the main protease of SARS‐CoV‐2. Chem Sci. 2022;13(13):3826‐3836.
Not in our library10.1039/d1sc06750h
129.
Di Sarno V, Lauro G, Musella S, et al. Identification of a dual acting SARS‐CoV‐2 proteases inhibitor through in silico design and step‐by‐step biological characterization. Eur J Med Chem. 2021;226:113863.
Not in our library10.1016/j.ejmech.2021.113863
130.
Stille JK, Tjutrins J, Wang G, et al. Design, synthesis and in vitro evaluation of novel SARS‐CoV‐2 3CL(pro) covalent inhibitors. Eur J Med Chem. 2022;229:114046.
Not in our library10.1016/j.ejmech.2021.114046
131.
Breidenbach J, Lemke C, Pillaiyar T, et al. Targeting the main protease of SARS‐CoV‐2: from the establishment of high throughput screening to the design of tailored inhibitors. Angew Chem Int Ed Engl. 2021;60(18):10423‐10429.
Not in our library10.1002/anie.202016961
132.
Bispecific repurposed medicines targeting the viral and immunological arms of COVID-19 · 2021
Not checked
133.
Yang KS, Ma XR, Ma Y, et al. A quick route to multiple highly potent SARS‐CoV‐2 main protease inhibitors. ChemMedChem. 2021;16(6):942‐948.
Not in our library10.1002/cmdc.202000924
134.
Ma XR, Alugubelli YR, Ma Y, et al. MPI8 is potent against SARS‐CoV‐2 by inhibiting dually and selectively the SARS‐CoV‐2 main protease and the host cathepsin L. ChemMedChem. 2022;17(1):e202100456.
Not in our library10.1002/cmdc.202100456
135.
Yamane D, Onitsuka S, Re S, et al. Selective covalent targeting of SARS‐CoV‐2 main protease by enantiopure chlorofluoroacetamide. Chem Sci. 2022;13(10):3027‐3034.
Not in our library10.1039/d1sc06596c
136.
Yang J, Lin X, Xing N, et al. Structure‐based discovery of novel nonpeptide inhibitors targeting SARS‐CoV‐2 M(pro). J Chem Inf Model. 2021;61(8):3917‐3926.
Not in our library10.1021/acs.jcim.1c00355
137.
Glaser J, Sedova A, Galanie S, et al. Hit expansion of a noncovalent SARS‐CoV‐2 main protease inhibitor. ACS Pharmacol Transl Sci. 2022;5(4):255‐265.
Not in our library10.1021/acsptsci.2c00026
138.
Chen CC, Yu X, Kuo CJ, et al. Overview of antiviral drug candidates targeting coronaviral 3C‐like main proteases. FEBS J. 2021;288(17):5089‐5121.
Not in our library10.1111/febs.15696
139.
Turlington M, Chun A, Tomar S, et al. Discovery of N‐(benzo[1,2,3]triazol‐1‐yl)‐N‐(benzyl)acetamido)phenyl) carboxamides as severe acute respiratory syndrome coronavirus (SARS‐CoV) 3CLpro inhibitors: identification of ML300 and noncovalent nanomolar inhibitors with an induced‐fit binding. Bioorg Med Chem Lett. 2013;23(22):6172‐6177.
Not in our library10.1016/j.bmcl.2013.08.112
140.
Han SH, Goins CM, Arya T, et al. Structure‐based optimization of ML300‐derived, noncovalent inhibitors targeting the severe acute respiratory syndrome coronavirus 3CL protease (SARS‐CoV‐2 3CL(pro)). J Med Chem. 2022;65(4):2880‐2904.
Not in our library10.1021/acs.jmedchem.1c00598
141.
Ghahremanpour MM, Tirado‐Rives J, Deshmukh M, et al. Identification of 14 known drugs as inhibitors of the main protease of SARS‐CoV‐2. ACS Med Chem Lett. 2020;11(12):2526‐2533.
Not in our library10.1021/acsmedchemlett.0c00521
142.
Zhang CH, Stone EA, Deshmukh M, et al. Potent noncovalent inhibitors of the main protease of SARS‐CoV‐2 from molecular sculpting of the drug perampanel guided by free energy perturbation calculations. ACS Cent Sci. 2021;7(3):467‐475.
Not in our library10.1021/acscentsci.1c00039
143.
Deshmukh MG, Ippolito JA, Zhang CH, et al. Structure‐guided design of a perampanel‐derived pharmacophore targeting the SARS‐CoV‐2 main protease. Structure. 2021;29(8):823‐833.e5.
Not in our library10.1016/j.str.2021.06.002
144.
Zhang CH, Spasov KA, Reilly RA, et al. Optimization of triarylpyridinone inhibitors of the main protease of SARS‐CoV‐2 to low‐nanomolar antiviral potency. ACS Med Chem Lett. 2021;12(8):1325‐1332.
Not in our library10.1021/acsmedchemlett.1c00326
145.
Ultralarge Virtual Screening Identifies SARS-CoV-2 Main Protease Inhibitors with Broad-Spectrum Activity against Coronaviruses · 2022
No notice
146.
Ramos‐Guzman CA, Ruiz‐Pernia JJ, Tunon I. Inhibition mechanism of SARS‐CoV‐2 main protease with ketone‐based inhibitors unveiled by multiscale simulations: insights for improved designs. Angew Chem Int Ed Engl. 2021;60(49):25933‐25941.
Not in our library10.1002/anie.202110027
147.
GRL-0920, an Indole Chloropyridinyl Ester, Completely Blocks SARS-CoV-2 Infection · 2020
Not checked
148.
Ghosh AK, Gong G, Grum‐Tokars V, et al. Design, synthesis and antiviral efficacy of a series of potent chloropyridyl ester‐derived SARS‐CoV 3CLpro inhibitors. Bioorg Med Chem Lett. 2008;18(20):5684‐5688.
Not in our library10.1016/j.bmcl.2008.08.082
149.
Ma C, Hu Y, Townsend JA, et al. Ebselen, disulfiram, carmofur, PX‐12, tideglusib, and shikonin are nonspecific promiscuous SARS‐CoV‐2 main protease inhibitors. ACS Pharmacol Transl Sci. 2020;3(6):1265‐1277.
Not in our library10.1021/acsptsci.0c00130
150.
Qiao Z, Wei N, Jin L, et al. The Mpro structure‐based modifications of ebselen derivatives for improved antiviral activity against SARS‐CoV‐2 virus. Bioorg Chem. 2021;117:105455.
Not in our library10.1016/j.bioorg.2021.105455
151.
Sun LY, Chen C, Su J, et al. Ebsulfur and Ebselen as highly potent scaffolds for the development of potential SARS‐CoV‐2 antivirals. Bioorg Chem. 2021;112:104889.
Not in our library10.1016/j.bioorg.2021.104889
152.
Ghosh AK, Raghavaiah J, Shahabi D, et al. Indole chloropyridinyl ester‐derived SARS‐CoV‐2 3CLpro inhibitors: enzyme inhibition, antiviral efficacy, structure–activity relationship, and X‐ray structural studies. J Med Chem. 2021;64(19):14702‐14714.
Not in our library10.1021/acs.jmedchem.1c01214
153.
Ghosh AK, Shahabi D, Yadav M, et al. Chloropyridinyl esters of nonsteroidal anti‐inflammatory agents and related derivatives as potent SARS‐CoV‐2 3CL protease inhibitors. Molecules. 2021;26(19):5782.
Not in our library10.3390/molecules26195782
154.
Chen W, Feng B, Han S, et al. Discovery of highly potent SARS‐CoV‐2 M(pro) inhibitors based on benzoisothiazolone scaffold. Bioorg Med Chem Lett. 2022;58:128526.
Not in our library10.1016/j.bmcl.2022.128526
155.
Petrou A, Zagaliotis P, Theodoroula NF, et al. Thiazole/thiadiazole/benzothiazole based thiazolidin‐4‐one derivatives as potential inhibitors of main protease of SARS‐CoV‐2. Molecules. 2022;27(7):2180.
Not in our library10.3390/molecules27072180
156.
El Khoury L, Jing Z, Cuzzolin A, et al. Computationally driven discovery of SARS‐CoV‐2 M(pro) inhibitors: from design to experimental validation. Chem Sci. 2022;13(13):3674‐3687.
Not in our library10.1039/d1sc05892d
157.
Guo S, Xie H, Lei Y, et al. Discovery of novel inhibitors against main protease (Mpro) of SARS‐CoV‐2 via virtual screening and biochemical evaluation. Bioorg Chem. 2021;110:104767.
Not in our library10.1016/j.bioorg.2021.104767
158.
Fricker SP, Mosi RM, Cameron BR, et al. Metal compounds for the treatment of parasitic diseases. J Inorg Biochem. 2008;102(10):1839‐1845.
Not in our library10.1016/j.jinorgbio.2008.05.010
159.
Fricker SP. Cysteine proteases as targets for metal‐based drugs. Metallomics. 2010;2(6):366‐377.
Not in our library10.1039/b924677k
160.
Karges J, Cohen SM. Metal complexes as antiviral agents for SARS‐CoV‐2. ChemBioChem. 2021;22(16):2600‐2607.
Not in our library10.1002/cbic.202100186
161.
Discovery and Characterization of the Naturally Occurring Inhibitors Against Human Pancreatic Lipase in Ampelopsis grossedentata · 2022
Not checked
162.
Huo PC, Hu Q, Shu S, et al. Design, synthesis and biological evaluation of novel chalcone‐like compounds as potent and reversible pancreatic lipase inhibitors. Bioorg Med Chem. 2021;29:115853.
Not in our library10.1016/j.bmc.2020.115853
163.
Li C‐Y, Wang H‐N, Zhu G‐H, et al. Discovery and characterization of naturally occurring chalcones as potent inhibitors of bile salt hydrolases. Acta Mater Med. 2022;1(2).
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164.
Hou XD, Guan XQ, Cao YF, et al. Inhibition of pancreatic lipase by the constituents in St. John's Wort: in vitro and in silico investigations. Int J Biol Macromol. 2020;145:620‐633.
Not in our library10.1016/j.ijbiomac.2019.12.231
165.
Song YQ, Guan XQ, Weng ZM, et al. Discovery of a highly specific and efficacious inhibitor of human carboxylesterase 2 by large‐scale screening. Int J Biol Macromol. 2019;137:261‐269.
Not in our library10.1016/j.ijbiomac.2019.06.235
166.
Xiong Y, Zhu GH, Wang HN, et al. Discovery of naturally occurring inhibitors against SARS‐CoV‐2 3CL(pro) from Ginkgo biloba leaves via large‐scale screening. Fitoterapia. 2021;152:104909.
Not in our library10.1016/j.fitote.2021.104909
167.
Shen N, Wang T, Gan Q, et al. Plant flavonoids: classification, distribution, biosynthesis, and antioxidant activity. Food Chem. 2022;383:132531.
Not in our library10.1016/j.foodchem.2022.132531
168.
Ververidis F, Trantas E, Douglas C, et al. Biotechnology of flavonoids and other phenylpropanoid‐derived natural products. Part I: chemical diversity, impacts on plant biology and human health. Biotechnol J. 2007;2(10):1214‐1234.
Not in our library10.1002/biot.200700084
169.
D'Arcy MS. A review of biologically active flavonoids as inducers of autophagy and apoptosis in neoplastic cells and as cytoprotective agents in non‐neoplastic cells. Cell Biol Int. 2022.
Not in our library10.1002/cbin.11813
170.
Fraga CG, Croft KD, Kennedy DO, et al. The effects of polyphenols and other bioactives on human health. Food Funct. 2019;10(2):514‐528.
Not in our library10.1039/c8fo01997e
171.
Zaragoza C, Villaescusa L, Monserrat J, et al. Potential therapeutic anti‐inflammatory and immunomodulatory effects of dihydroflavones, flavones, and flavonols. Molecules. 2020;25(4):1107.
Not in our library10.3390/molecules25041017
172.
Herbal Medicine for Cardiovascular Diseases: Efficacy, Mechanisms, and Safety · 2020
No notice
173.
Mouffouk C, Mouffouk S, Mouffouk S, et al. Flavonols as potential antiviral drugs targeting SARS‐CoV‐2 proteases (3CL(pro) and PL(pro)), spike protein, RNA‐dependent RNA polymerase (RdRp) and angiotensin‐converting enzyme II receptor (ACE2). Eur J Pharmacol. 2021;891:173759.
Not in our library10.1016/j.ejphar.2020.173759
174.
Liskova A, Samec M, Koklesova L, et al. Flavonoids against the SARS‐CoV‐2 induced inflammatory storm. Biomed Pharmacother. 2021;138:111430.
Not in our library10.1016/j.biopha.2021.111430
175.
Song JW, Long JY, Xie L, et al. Applications, phytochemistry, pharmacological effects, pharmacokinetics, toxicity of Scutellaria baicalensis Georgi. and its probably potential therapeutic effects on COVID‐19: a review. Chin Med. 2020;15:102.
Not in our library10.1186/s13020-020-00384-0
176.
Li K, Liang Y, Cheng A, et al. Antiviral properties of Baicalin: a concise review. Rev Bras Farmacogn. 2021;31(4):408‐419.
Not in our library10.1007/s43450-021-00182-1
177.
Scutellaria baicalensis extract and baicalein inhibit replication of SARS-CoV-2 and its 3C-like protease in vitro · 2021
Not checked
178.
Bolton JL, Dunlap TL, Dietz BM. Formation and biological targets of botanical o‐quinones. Food Chem Toxicol. 2018;120:700‐707.
Not in our library10.1016/j.fct.2018.07.050
179.
Wu Q, Yan S, Wang Y, et al. Discovery of 4'‐O‐methylscutellarein as a potent SARS‐CoV‐2 main protease inhibitor. Biochem Biophys Res Commun. 2022;604:76‐82.
Not in our library10.1016/j.bbrc.2022.03.052
180.
Identification of pyrogallol as a warhead in design of covalent inhibitors for the SARS-CoV-2 3CL protease · 2021
No notice
181.
Su HX, Yao S, Zhao WF, et al. Anti‐SARS‐CoV‐2 activities in vitro of Shuanghuanglian preparations and bioactive ingredients. Acta Pharmacol Sin. 2020;41(9):1167‐1177.
Not in our library10.1038/s41401-020-0483-6
182.
Ugonin J Acts as a SARS-CoV-2 3C-like Protease Inhibitor and Exhibits Anti-inflammatory Properties · 2021
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183.
Evaluation of polyphenols from Broussonetia papyrifera as coronavirus protease inhibitors · 2017
No notice
184.
Ryu YB, Jeong HJ, Kim JH, et al. Biflavonoids from Torreya nucifera displaying SARS‐CoV 3CL(pro) inhibition. Bioorg Med Chem. 2010;18(22):7940‐7947.
Not in our library10.1016/j.bmc.2010.09.035
185.
Abian O, Ortega‐Alarcon D, Jimenez‐Alesanco A, et al. Structural stability of SARS‐CoV‐2 3CLpro and identification of quercetin as an inhibitor by experimental screening. Int J Biol Macromol. 2020;164:1693‐1703.
Not in our library10.1016/j.ijbiomac.2020.07.235
186.
Saakre M, Mathew D, Ravisankar V. Perspectives on plant flavonoid quercetin‐based drugs for novel SARS‐CoV‐2. Beni Suef Univ J Basic Appl Sci. 2021;10(1):21.
Not in our library10.1186/s43088-021-00107-w
187.
Mangiavacchi F, Botwina P, Menichetti E, et al. Seleno‐functionalization of quercetin improves the non‐covalent inhibition of M(pro) and its antiviral activity in cells against SARS‐CoV‐2. Int J Mol Sci. 2021;22(13):7048.
Not in our library10.3390/ijms22137048
188.
Chiou WC, Chen JC, Chen YT, et al. The inhibitory effects of PGG and EGCG against the SARS‐CoV‐2 3C‐like protease. Biochem Biophys Res Commun. 2022;591:130‐136.
Not in our library10.1016/j.bbrc.2020.12.106
189.
Du A, Zheng R, Disoma C, et al. Epigallocatechin‐3‐gallate, an active ingredient of Traditional Chinese Medicines, inhibits the 3CLpro activity of SARS‐CoV‐2. Int J Biol Macromol. 2021;176:1‐12.
Not in our library10.1016/j.ijbiomac.2021.02.012
190.
Nguyen TT, Woo HJ, Kang HK, et al. Flavonoid‐mediated inhibition of SARS coronavirus 3C‐like protease expressed in Pichia pastoris. Biotechnol Lett. 2012;34(5):831‐838.
Not in our library10.1007/s10529-011-0845-8
191.
Liu SY, Wang W, Ke JP, et al. Discovery of Camellia sinensis catechins as SARS‐CoV‐2 3CL protease inhibitors through molecular docking, intra and extra cellular assays. Phytomedicine. 2022;96:153853.
Not in our library10.1016/j.phymed.2021.153853
192.
Park J, Park R, Jang M, et al. Therapeutic potential of EGCG, a green tea polyphenol, for treatment of coronavirus diseases. Life. 2021;11(3):197.
Not in our library10.3390/life11030197
193.
Cianciosi D, Forbes‐Hernandez TY, Regolo L, et al. The reciprocal interaction between polyphenols and other dietary compounds: impact on bioavailability, antioxidant capacity and other physico‐chemical and nutritional parameters. Food Chem. 2022;375:131904.
Not in our library10.1016/j.foodchem.2021.131904
194.
Glycosylation Is a Major Regulator of Phenylpropanoid Availability and Biological Activity in Plants · 2016
No notice
195.
Plaza M, Pozzo T, Liu J, et al. Substituent effects on in vitro antioxidizing properties, stability, and solubility in flavonoids. J Agric Food Chem. 2014;62(15):3321‐3333.
Not in our library10.1021/jf405570u
196.
Biochemical and molecular characterization of a flavonoid 3-O-glycosyltransferase responsible for anthocyanins and flavonols biosynthesis in Freesia hybrida · 2016
Not checked
197.
Cherrak SA, Merzouk H, Mokhtari‐Soulimane N. Potential bioactive glycosylated flavonoids as SARS‐CoV‐2 main protease inhibitors: a molecular docking and simulation studies. PLoS One. 2020;15(10):e0240653.
Not in our library10.1371/journal.pone.0240653
198.
Jo S, Kim S, Shin DH, et al. Inhibition of SARS‐CoV 3CL protease by flavonoids. J Enzyme Inhib Med Chem. 2020;35(1):145‐151.
Not in our library10.1080/14756366.2019.1690480
199.
da Silva FMA, da Silva KPA, de Oliveira LPM, et al. Flavonoid glycosides and their putative human metabolites as potential inhibitors of the SARS‐CoV‐2 main protease (Mpro) and RNA‐dependent RNA polymerase (RdRp). Mem Inst Oswaldo Cruz. 2020;115:e200207.
Not in our library10.1590/0074-02760200207
200.
Godinho PIC, Soengas RG, Silva VLM. Therapeutic potential of glycosyl flavonoids as anti‐coronaviral agents. Pharmaceuticals. 2021;14(6):546.
Not in our library10.3390/ph14060546
201.
Refaat H, Mady FM, Sarhan HA, et al. Optimization and evaluation of propolis liposomes as a promising therapeutic approach for COVID‐19. Int J Pharm. 2021;592:120028.
Not in our library10.1016/j.ijpharm.2020.120028
202.
Rizzuti B, Grande F, Conforti F, et al. Rutin is a low micromolar inhibitor of SARS‐CoV‐2 main protease 3CLpro: implications for drug design of quercetin analogs. Biomedicines. 2021;9(4):375.
Not in our library10.3390/biomedicines9040375
203.
An integrated method for optimized identification of effective natural inhibitors against SARS-CoV-2 3CLpro · 2021
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204.
Chen L, Li J, Luo C, et al. Binding interaction of quercetin‐3‐beta‐galactoside and its synthetic derivatives with SARS‐CoV 3CL(pro): structure–activity relationship studies reveal salient pharmacophore features. Bioorg Med Chem. 2006;14(24):8295‐8306.
Not in our library10.1016/j.bmc.2006.09.014
205.
Menezes J, Campos VR. Natural biflavonoids as potential therapeutic agents against microbial diseases. Sci Total Environ. 2021;769:145168.
Not in our library10.1016/j.scitotenv.2021.145168
206.
Heleno SA, Martins A, Queiroz MJ, et al. Bioactivity of phenolic acids: metabolites versus parent compounds: a review. Food Chem. 2015;173:501‐513.
Not in our library10.1016/j.foodchem.2014.10.057
207.
Phenolic acids: Natural versatile molecules with promising therapeutic applications · 2019
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208.
Chen Z, Cui Q, Cooper L, et al. Ginkgolic acid and anacardic acid are specific covalent inhibitors of SARS‐CoV‐2 cysteine proteases. Cell Biosci. 2021;11(1):45.
Not in our library10.1186/s13578-021-00564-x
209.
Yao Q‐Q, Li L, Xu M‐C, et al. The metabolism and hepatotoxicity of ginkgolic acid (17:1) in vitro. Chin J Natural Med. 2018;16(11):829‐837.
Not in our library10.1016/s1875-5364(18)30124-9
210.
Borenstein R, Hanson BA, Markosyan RM, et al. Ginkgolic acid inhibits fusion of enveloped viruses. Sci Rep. 2020;10(1):4746.
Not in our library10.1038/s41598-020-61700-0
211.
Lu JM, Yan S, Jamaluddin S, et al. Ginkgolic acid inhibits HIV protease activity and HIV infection in vitro. Med Sci Monit. 2012;18(8):BR293‐BR298.
Not in our library10.12659/msm.883261
212.
Nguyen TTH, Jung JH, Kim MK, et al. The inhibitory effects of plant derivate polyphenols on the main protease of SARS coronavirus 2 and their structure–activity relationship. Molecules. 2021;26(7):1924.
Not in our library10.3390/molecules26071924
213.
Wang S‐C, Chen Y, Wang Y‐C, et al. Tannic acid suppresses SARS‐CoV‐2 as a dual inhibitor of the viral main protease and the cellular TMPRSS2 protease. Am J Cancer Res. 2020;10(12):4538‐4546.
Not in our library
214.
Tea Polyphenols EGCG and Theaflavin Inhibit the Activity of SARS‐CoV‐2 3CL‐Protease In Vitro · 2020
No notice
215.
Inhibition of SARS‐CoV 3C‐like Protease Activity by Theaflavin‐3,3′‐digallate (TF3) · 2005
No notice
216.
Torres‐León C, Ventura‐Sobrevilla J, Serna‐Cock L, et al. Pentagalloylglucose (PGG): a valuable phenolic compound with functional properties. J Funct Foods. 2017;37:176‐189.
Not in our library
217.
Park JY, Kim JH, Kwon JM, et al. Dieckol, a SARS‐CoV 3CL(pro) inhibitor, isolated from the edible brown algae Ecklonia cava. Bioorg Med Chem. 2013;21(13):3730‐3737.
Not in our library10.1016/j.bmc.2013.04.026
218.
Yan G, Li D, Lin Y, et al. Development of a simple and miniaturized sandwich‐like fluorescence polarization assay for rapid screening of SARS‐CoV‐2 main protease inhibitors. Cell Biosci. 2021;11(1):199.
Not in our library10.1186/s13578-021-00720-3
219.
Du R, Cooper L, Chen Z, et al. Discovery of chebulagic acid and punicalagin as novel allosteric inhibitors of SARS‐CoV‐2 3CL(pro). Antiviral Res. 2021;190:105075.
Not in our library10.1016/j.antiviral.2021.105075
220.
Monks TJ, Jones DC. The metabolism and toxicity of quinones, quinonimines, quinone methides, and quinone‐thioethers. Curr Drug Metab. 2002;3(4):425‐438.
Not in our library10.2174/1389200023337388
221.
Ali K, Mishra P, Kumar A, et al. Reactivity vs. selectivity of quinone methides: synthesis of pharmaceutically important molecules, toxicity and biological applications. Chem Commun. 2022;58(42):6160‐6175.
Not in our library10.1039/d2cc00838f
222.
Park JY, Kim JH, Kim YM, et al. Tanshinones as selective and slow‐binding inhibitors for SARS‐CoV cysteine proteases. Bioorg Med Chem. 2012;20(19):5928‐5935.
Not in our library10.1016/j.bmc.2012.07.038
223.
High-throughput screening identifies established drugs as SARS-CoV-2 PLpro inhibitors · 2021
No notice
224.
Ma C, Wang J. Validation and invalidation of SARS‐CoV‐2 papain‐like protease inhibitors. ACS Pharmacol Transl Sci. 2022;5(2):102‐109.
Not in our library10.1021/acsptsci.1c00240
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