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

Authors :
Schütz, Anne K.
Vagt, Toni
Huber, Matthias
Ovchinnikova, Oxana Y.
Cadalbert, Riccardo
Wall, Joseph
Güntert, Peter
Böckmann, Anja
Glockshuber, Rudi
Meier, Beat H.
Source :
Angewandte Chemie International Edition. Jan2015, Vol. 54 Issue 1, p331-335. 5p.
Publication Year :
2015

Abstract

Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ1-40 peptide with the Osaka mutation (E22Δ), 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
14337851
Volume :
54
Issue :
1
Database :
Academic Search Index
Journal :
Angewandte Chemie International Edition
Publication Type :
Academic Journal
Accession number :
100178209
Full Text :
https://doi.org/10.1002/anie.201408598