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Updated: Jan 20, 2026

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Metal Binding to Aβ Peptides Inhibits Interaction with Cytochrome c: Insights from Abiological Constructs
Ankita Sarkar1, Kushal Sengupta1, Sudipta Chatterjee1
1Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, 2A & 2B Raja S.C. Mullick Road, Kolkata 700032, India.
Abstract:
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 Zn2+ or Cu2+ induces changes in the morphologies of these assemblies, making them fold, which inhibits their spontaneous interaction with Cytc.
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