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

Autor(es)

dos Santos, Nathalia Villa ^[1] ; Silva, Adriana F. ^[1] ; Oliveira, Jr., Vani Xavier ^[1] ; Homem-de-Mello, Paula ^[1] ; Cerchiaro, Giselle ^[1]

Afiliação do(s) autor(es)

^[1] Fed Univ ABC, UFABC, Ctr Nat Sci & Humanities, BR-09210170 Santo Andre, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Inorganic Biochemistry; v. 114, p. 1-7, SEP 2012.
• Citações Web of Science: 2

Resumo

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)

• Processo FAPESP: 07/05370-0 - Estudo químico-quântico de corantes e de complexos de metais de transição
• Beneficiário: Paula Homem-de-Mello
• Linha de fomento: Auxílio à Pesquisa - Apoio a Jovens Pesquisadores
• Processo FAPESP: 07/50765-2 - Estudo de processos oxidativos e radicalares envolvendo o cobre no meio biológico: uma investigação de mecanismos moleculares da atividade oxidante de complexos e proteínas contendo cobre
• Beneficiário: Giselle Cerchiaro
• Linha de fomento: Auxílio à Pesquisa - Apoio a Jovens Pesquisadores