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A hexameric peptide barrel as building block of amyloid-β protofibrils.
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2014 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 53, p. 12756-12760Article in journal (Refereed) Published
Abstract [en]

Oligomeric and protofibrillar aggregates formed by the amyloid-A beta peptide (A beta) are believed to be involved in the pathology of Alzheimer's disease. Central to Alzheimer pathology is also the fact that the longer A beta(42) peptide is more prone to aggregation than the more prevalent A beta(40). Detailed structural studies of A beta oligomers and protofibrils have been impeded by aggregate heterogeneity and instability. We previously engineered a variant of A beta that forms stable protofibrils and here we use solid-state NMR spectroscopy and molecular modeling to derive a structural model of these. NMR data are consistent with packing of residues 16 to 42 of A beta protomers into hexameric barrel-like oligomers within the protofibril. The core of the oligomers consists of all residues of the central and C-terminal hydrophobic regions of A beta, and hairpin loops extend from the core. The model accounts for why A beta(42) forms oligomers and protofibrils more easily than A beta(40).

Place, publisher, year, edition, pages
John Wiley & Sons, 2014. Vol. 53, p. 12756-12760
Keywords [en]
Alzheimer's disease; amyloid beta-peptides; neurotoxicity; oligomers; protein structures
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:kth:diva-206097DOI: 10.1002/anie.201406357ISI: 000344793400011Scopus ID: 2-s2.0-84911413890OAI: oai:DiVA.org:kth-206097DiVA, id: diva2:1091164
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QC 20170502

Available from: 2017-04-26 Created: 2017-04-26 Last updated: 2017-05-02Bibliographically approved

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