Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
Chinmay Dey, Madhuparna Roy, Somdatta Ghosh Dey
ACS Omega · 2022
doi:10.1021/acsomega.1c06056 (opens in a new tab)
We email you when a new notice or a question about this paper appears.
Abstract
High Resolution Image Download MS PowerPoint Slide Amyloid β (Aβ) peptides mutated at different positions using a cysteine moiety assemble on Au electrodes using the thiol functionality of cysteine. Self-assembled monolayers (SAMs) of Aβ on Au surfaces can act as abiological platforms that allow the mimicking of fibrils and oligomeric Aβ via the formation of controlled large and small peptide aggregates. These Aβ constructs bind with heme and Cu and exhibit different reactivities. These abiological platforms can also be used to investigate potential drugs that can interact with heme and Cu-Aβ. SAM formation of Aβ mutants allows the study of different morphology and structure as well as behavior changes on binding with different metals and cytochrome c (Cyt c ). This review provides a detailed insight into the structure and reactivities of various Aβ aggregated on Au electrodes mimicking the cell membrane.
Abstract licence: CC BY-NC-ND
References23
23 more references, whose wording the paper’s licence keeps private.
Reads
Read by people on this page
None yet.
Checked or read by AI through naulon
None yet.
A person counts once a day per paper. We keep no cookie and no address: a reader is a hash that changes every day. Any month under five reads shows no number.
Are you an author?
Is this your paper?
Claim it to add your note and be paid when agents cite it. Free.