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Atomic‐Resolution Three‐Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation
Author(s) -
Schütz Anne K.,
Vagt Toni,
Huber Matthias,
Ovchinnikova Oxana Y.,
Cadalbert Riccardo,
Wall Joseph,
Güntert Peter,
Böckmann Anja,
Glockshuber Rudi,
Meier Beat H.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201408598
Subject(s) - fibril , amyloid fibril , resolution (logic) , mutation , amyloid (mycology) , peptide , chemistry , intermolecular force , crystallography , biophysics , high resolution , amyloid β , biochemistry , biology , molecule , disease , medicine , gene , pathology , inorganic chemistry , artificial intelligence , computer science , remote sensing , organic chemistry , geology
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.