Atomic‐Resolution Three‐Dimensional Structure of Amyloid β 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 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.

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Cited by papers we hold 6

• Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue · 2019
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• Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy · 2019
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• The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism · 2018
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• Envisaging the Structural Elevation in the Early Event of Oligomerization of Disordered Amyloid β Peptide · 2017
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• Monomer-dependent secondary nucleation in amyloid formation · 2017
  No notice
• Alternative salt bridge formation in Aβ – a hallmark of early-onset Alzheimer’s disease? · 2015
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