Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22Δ) fibrils
- Journal Article
Rights / licenseIn Copyright - Non-Commercial Use Permitted
Alzheimer’s disease (AD) is the most common form of dementia. Aggregation of amyloid β (Aβ), a peptide of 39−43 residues length, into insoluble fibrils is considered to initiate the disease. Determination of the molecular structure of Aβ fibrils is technically challenging and is a significant goal in AD research that may lead to design of effective therapeutical inhibitors of Aβ aggregation. Here, we present chemical-shift assignments for fibrils formed by highly pure recombinant Aβ1−40 with the Osaka E22Δ mutation that is found in familial AD. We show that that all regions of the peptide are rigid, including the N-terminal part often believed to be flexible in Aβ wt. Show more
Journal / seriesBiomolecular NMR Assignments
Pages / Article No.
SubjectAlzheimer’s disease; Solid-state NMR spectroscopy; Amyloid beta; Amyloid structures; Fibrils
Organisational unit03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
03412 - Glockshuber, Rudolf / Glockshuber, Rudolf
146757 - NMR studies in the Solid State (SNF)
NotesIt was possible to publish this article open access thanks to a Swiss National Licence with the publisher.
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