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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Copper(II) complexation to 1-octarepeat peptide from a prion protein: Insights from theoretical and experimental UV-visible studies

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dos Santos, Nathalia Villa [1] ; Silva, Adriana F. [1] ; Oliveira, Jr., Vani Xavier [1] ; Homem-de-Mello, Paula [1] ; Cerchiaro, Giselle [1]
Total Authors: 5
[1] Fed Univ ABC, UFABC, Ctr Nat Sci & Humanities, BR-09210170 Santo Andre, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: Journal of Inorganic Biochemistry; v. 114, p. 1-7, SEP 2012.
Web of Science Citations: 2

The octarepeat domain in cellular prion protein (PrPc) has attracted much attention over the last 10 years because of its importance in the complexation of copper with PrPc. 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 PrPc using experimental and theoretical approaches and to gain insight into the complexation of the PrPc 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. (C) 2012 Elsevier Inc. All rights reserved. (AU)