Copper(II) complexation to 1-octarepeat peptide from a prion protein: insights from theoretical and experimental UV-visible studies.
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.
Center for Natural Sciences and Humanities, Federal University of ABC, UFABC, Avenida dos Estados, 5001, Bloco B, 09210-170, Santo André, SP, Brazil.
Nathalia Villa
NV
dos Santos
Adriana F
AF
Silva
Vani Xavier
VX
Oliveira
Paula
P
Homem-de-Mello
Giselle
G
Cerchiaro
D001665:Binding Sites; D002413:Cations, Divalent; D056831:Coordination Complexes / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000737:chemistry; D018621:PrPC Proteins / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid; D013057:Spectrum Analysis; D055672:Static Electricity
D002413:Cations, Divalent; D056831:Coordination Complexes; D010446:Peptide Fragments; D018621:PrPC Proteins; D003300:Copper