Center for Natural Sciences and Humanities, Federal University of ABC, UFABC, Avenida dos Estados, 5001, Bloco B, 09210-170, Santo André, SP, Brazil.
J Inorg Biochem. 2012 Sep;114:1-7. doi: 10.1016/j.jinorgbio.2012.04.008. Epub 2012 Apr 27.
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.
过去 10 年来，细胞朊蛋白（PrP(C)）中的八重复结构域因其在铜与 PrP(C)的络合中的重要性而备受关注。本研究旨在通过实验和理论方法研究与 PrP(C)中八重复区域的 1 重复相似的肽的紫外可见光谱，并深入了解铜(II)离子在溶液中与 PrP(C)八重复结构域的络合情况。我们发现，铜原子负责肽的构象，这使得其两个末端残基之间能够发生电荷转移。
