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Updated: May 21, 2026
Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
Published on: April 5, 2022
Copper(II) complexation to 1-octarepeat peptide from a prion protein: insights from theoretical and experimental
Nathalia Villa dos Santos1, Adriana F Silva, Vani Xavier Oliveira
1Center for Natural Sciences and Humanities, Federal University of ABC, UFABC, Avenida dos Estados, 5001, Bloco B, 09210-170, Santo André, SP, Brazil.
Abstract:
The octarepeat domain in cellular prion protein (PrP(C)) has attracted much attention over the last 10 years because of its importance in the complexation of copper with PrP(C). The aim of this research was to study the UV-vis spectra of a peptide similar to the 1-repeat of the octarepeat region in PrP(C) using experimental and theoretical approaches and to gain insight into the complexation of the PrP(C) octarepeat domain with copper(II) ions in solution. We found that the copper atom was responsible for the peptide conformation, which allows for charge transfers between its two terminal residues.
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