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Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces

[Image: see text] 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 oligome...

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Autores principales: Dey, Chinmay, Roy, Madhuparna, Dey, Somdatta Ghosh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8973063/
https://www.ncbi.nlm.nih.gov/pubmed/35382274
http://dx.doi.org/10.1021/acsomega.1c06056
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author Dey, Chinmay
Roy, Madhuparna
Dey, Somdatta Ghosh
author_facet Dey, Chinmay
Roy, Madhuparna
Dey, Somdatta Ghosh
author_sort Dey, Chinmay
collection PubMed
description [Image: see text] 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.
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spelling pubmed-89730632022-04-04 Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces Dey, Chinmay Roy, Madhuparna Dey, Somdatta Ghosh ACS Omega [Image: see text] 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. American Chemical Society 2022-03-15 /pmc/articles/PMC8973063/ /pubmed/35382274 http://dx.doi.org/10.1021/acsomega.1c06056 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Dey, Chinmay
Roy, Madhuparna
Dey, Somdatta Ghosh
Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
title Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
title_full Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
title_fullStr Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
title_full_unstemmed Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
title_short Insights from Self-Assembled Aggregates of Amyloid β Peptides on Gold Surfaces
title_sort insights from self-assembled aggregates of amyloid β peptides on gold surfaces
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8973063/
https://www.ncbi.nlm.nih.gov/pubmed/35382274
http://dx.doi.org/10.1021/acsomega.1c06056
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