Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.
- Schütz AK Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093 Zurich (Switzerland).
- Vagt T
- Huber M
- Ovchinnikova OY
- Cadalbert R
- Wall J
- Güntert P
- Böckmann A
- Glockshuber R
- Meier BH
- 2014-11-15
Published in:
- Angewandte Chemie (International ed. in English). - 2015
Alzheimer's disease
amyloids
solid-state NMR spectroscopy
structure elucidation
Alzheimer Disease
Amino Acid Sequence
Amyloid beta-Peptides
Humans
Models, Molecular
Molecular Sequence Data
Mutation
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments
English
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.
- Language
-
- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1002/anie.201408598
- PMID 25395337
- Persistent URL
- https://sonar.ch/global/documents/180957
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