Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling

被引：329

作者：

Török, M

Milton, S

Kayed, R

Wu, P

McIntire, T

Glabe, CG ^{[1
]}

Langen, R

机构：

[1] Univ Calif Irvine, Dept Biol Mol, Irvine, CA 92697 USA

[2] Univ Calif Irvine, Dept Biochem, Irvine, CA 92697 USA

[3] Univ Calif Irvine, Dept Chem, Irvine, CA 92697 USA

[4] Univ So Calif, Keck Sch Med, Neurogenet Inst, Dept Biochem & Mol Biol, Los Angeles, CA 90033 USA

[5] Univ So Calif, Keck Sch Med, Arnold & Mabel Beckman Macular Res Ctr, Los Angeles, CA 90033 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2002年 / 277卷 / 43期

关键词：

D O I：

10.1074/jbc.M205659200

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：

Electron paramagnetic resonance spectroscopy analysis of 19 spin-labeled derivatives of the Alzheimer's amyloid beta (Abeta) peptide was used to reveal structural features of amyloid fibril formation. In the fibril, extensive regions of the peptide show an in-register, parallel arrangement. Based on the parallel arrangement and side chain mobility analysis we find the amyloid structure to be mostly ordered and specific, but we also identify more dynamic regions (N and C termini) and likely turn or bend regions (around residues 23-26). Despite their different aggregation properties and roles in disease, the two peptides, Abeta40 and Abeta42, homogeneously co-mix in amyloid fibrils suggesting that they possess the same structural architecture.

引用

页码：40810 / 40815

页数：6

共 46 条

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