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

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Sch眉tz AK, Vagt T, Huber M, Ovchinnikova OY, Cadalbert R, Wall J, G眉ntert P, B枚ckmann A, Glockshuber R, Meier BH
OpenAccess logo Angew Chem Int Ed Engl 54 331-5 (2015)
Cited: 149 times
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Abstract

Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid 尾-peptide (A尾) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the A尾1-40 peptide with the Osaka mutation (E22螖), 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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