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Atomic-resolution three-dimensional structure of amyloid ? fibrils bearing the Osaka mutation.

ABSTRACT: 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 A?1-40 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.

SUBMITTER: Schutz AK

PROVIDER: S-EPMC4502972 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature

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Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.

Schütz Anne K AK Vagt Toni T Huber Matthias M Ovchinnikova Oxana Y OY Cadalbert Riccardo R Wall Joseph J Güntert Peter P Böckmann Anja A Glockshuber Rudi R Meier Beat H BH

Angewandte Chemie (International ed. in English) 20141113 1

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 intermolecula ...[more]

PMID: 25395337

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