Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs

[Image: see text] Aβ(1–40) peptide is mutated to introduce cysteine residue to allow formation of organized self-assembled monolayers (SAMs) on Au electrodes. Three mutants of this peptide are produced, which vary in the position of the inserted cysteine residue. Fourier transform infrared data on t...

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Autores principales: Sarkar, Ankita, Sengupta, Kushal, Chatterjee, Sudipta, Seal, Manas, Faller, Peter, Dey, Somdatta Ghosh, Dey, Abhishek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6644584/
https://www.ncbi.nlm.nih.gov/pubmed/31458095
http://dx.doi.org/10.1021/acsomega.8b01736
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author Sarkar, Ankita
Sengupta, Kushal
Chatterjee, Sudipta
Seal, Manas
Faller, Peter
Dey, Somdatta Ghosh
Dey, Abhishek
author_facet Sarkar, Ankita
Sengupta, Kushal
Chatterjee, Sudipta
Seal, Manas
Faller, Peter
Dey, Somdatta Ghosh
Dey, Abhishek
author_sort Sarkar, Ankita
collection PubMed
description [Image: see text] Aβ(1–40) peptide is mutated to introduce cysteine residue to allow formation of organized self-assembled monolayers (SAMs) on Au electrodes. Three mutants of this peptide are produced, which vary in the position of the inserted cysteine residue. Fourier transform infrared data on these peptide SAMs show the presence of both α helices and β sheet in these Aβ constructs. These peptide constructs interact with cytochrome c (Cytc), allowing electron transfer between Cytc and the electrode via the Aβ peptides. Binding of metals like Zn(2+) or Cu(2+) induces changes in the morphologies of these assemblies, making them fold, which inhibits their spontaneous interaction with Cytc.
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spelling pubmed-66445842019-08-27 Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs Sarkar, Ankita Sengupta, Kushal Chatterjee, Sudipta Seal, Manas Faller, Peter Dey, Somdatta Ghosh Dey, Abhishek ACS Omega [Image: see text] Aβ(1–40) peptide is mutated to introduce cysteine residue to allow formation of organized self-assembled monolayers (SAMs) on Au electrodes. Three mutants of this peptide are produced, which vary in the position of the inserted cysteine residue. Fourier transform infrared data on these peptide SAMs show the presence of both α helices and β sheet in these Aβ constructs. These peptide constructs interact with cytochrome c (Cytc), allowing electron transfer between Cytc and the electrode via the Aβ peptides. Binding of metals like Zn(2+) or Cu(2+) induces changes in the morphologies of these assemblies, making them fold, which inhibits their spontaneous interaction with Cytc. American Chemical Society 2018-10-25 /pmc/articles/PMC6644584/ /pubmed/31458095 http://dx.doi.org/10.1021/acsomega.8b01736 Text en Copyright © 2018 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Sarkar, Ankita
Sengupta, Kushal
Chatterjee, Sudipta
Seal, Manas
Faller, Peter
Dey, Somdatta Ghosh
Dey, Abhishek
Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
title Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
title_full Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
title_fullStr Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
title_full_unstemmed Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
title_short Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
title_sort metal binding to aβ peptides inhibits interaction with cytochrome c: insights from abiological constructs
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6644584/
https://www.ncbi.nlm.nih.gov/pubmed/31458095
http://dx.doi.org/10.1021/acsomega.8b01736
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