Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation

被引：230

作者：

Schuetz, Anne K. ^{[1
]}

Vagt, Toni ^{[2
]}

Huber, Matthias ^{[1
]}

Ovchinnikova, Oxana Y. ^{[2
]}

Cadalbert, Riccardo ^{[1
]}

Wall, Joseph ^{[3
]}

Guentert, Peter ^{[4
,5
]}

Boeckmann, Anja ^{[6
]}

Glockshuber, Rudi ^{[2
]}

Meier, Beat H. ^{[1
]}

机构：

[1] ETH, CH-8093 Zurich, Switzerland

[2] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland

[3] Brookhaven Natl Lab, Upton, NY 11973 USA

[4] Goethe Univ Frankfurt, Inst Biophys Chem, Ctr Biomol Magnet Resonance, D-60054 Frankfurt, Germany

[5] Goethe Univ Frankfurt, Frankfurt Inst Adv Studies, D-60054 Frankfurt, Germany

[6] Univ Lyon, Inst Biol & Chim Prot Bases Mol & Struct Syst Inf, Labex Ecofect, UMR CNRS 5086, F-69367 Lyon, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2015年 / 54卷 / 01期

基金：

瑞士国家科学基金会;

关键词：

Alzheimer's disease; amyloids; solid-state NMR spectroscopy; structure elucidation; SOLID-STATE NMR; ALPHA-SYNUCLEIN STRAINS; ALZHEIMERS-DISEASE; EXPERIMENTAL CONSTRAINTS; MOLECULAR-STRUCTURE; ROTATING SOLIDS; SPECTROSCOPY; HYPOTHESIS; DYNAMICS; PROTEIN;

D O I：

10.1002/anie.201408598

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid -peptide (A) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the A1-40 peptide with the Osaka mutation (E22), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints.

引用

页码：331 / 335

页数：5

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