Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy

被引：47

作者：

Yamaguchi, Takahiro ^{[1
]}

Matsuzaki, Katsumi ^{[1
]}

Hoshino, Masaru ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan

来源：

FEBS LETTERS | 2011年 / 585卷 / 07期

关键词：

NMR; Amyloid fibril formation; Conformational change; Chemical exchange; ALZHEIMERS-DISEASE; EXPERIMENTAL CONSTRAINTS; FIBRIL FORMATION; NMR; STABILIZATION; SENSITIVITY; NUCLEATION; MECHANISM; OLIGOMERS; SCRAPIE;

D O I：

10.1016/j.febslet.2011.03.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A detailed analysis of the NMR spectra of amyloid-beta (A beta) peptide revealed a decrease in signal intensity at higher temperature, due to a reversible conformational change of the molecule. Although peak intensity did not depend on peptide concentrations, the intensity in the region from D23 to A30 depended significantly on temperature. During the early stages of A beta aggregation, each molecule might adopt transiently a turn conformation at around D23-A30, which converts mutually with a random coil. Stabilization of a turn by further conformational change and/or molecular association would lead to the formation of a "nucleus'' for amyloid fibrils. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1097 / 1102

页数：6

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