The aggregated state of amyloid-β peptide in vitro depends on Cu2+ ion concentration

被引：47

作者：

Jun, Sangmi ^{[1
]}

Saxena, Sunil ^{[1
]}

机构：

[1] Univ Pittsburgh, Dept Chem, Pittsburgh, PA 15260 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 21期

关键词：

amyloid morphology; copper; EPR spectroscopy; peptide folding; peptides;

D O I：

10.1002/anie.200700318

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Hold them or fold them: The morphology of aggregated amyloid-β depends on the concentration of Cu2+ ions, as shown in the TEM images. Distinct differences in the coordination of Cu2+ ions to amyloid-β are observed by electron spin resonance as the metal concentration increases. The results suggest a correlation between specific Cu2+ ion coordination and the overall morphology of aggregates. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：3959 / 3961

页数：3

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