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A Hexameric Peptide Barrel as Building Block of Amyloid-β Protofibrils
Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences (SLU).
Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences (SLU).
Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences (SLU).
Department of Physics, Warwick University, Coventry.
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2014 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 126, no 47, p. 12970-12974Article in journal (Refereed) Published
Abstract [en]

Oligomeric and protofibrillar aggregates formed by the amyloid-β peptide (Aβ) are believed to be involved in the pathology of Alzheimer’s disease. Central to Alzheimer pathology is also the fact that the longer Aβ42 peptide is more prone to aggregation than the more prevalent Aβ40. Detailed structural studies of Aβ oligomers and protofibrils have been impeded by aggregate heterogeneity and instability. We previously engineered a variant of Aβ 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 Aβ 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 Aβ, and hairpin loops extend from the core. The model accounts for why Aβ42 forms oligomers and protofibrils more easily than Aβ40.

Place, publisher, year, edition, pages
2014. Vol. 126, no 47, p. 12970-12974
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
Identifiers
URN: urn:nbn:se:ltu:diva-3054DOI: 10.1002/anie.201406357ISI: 000344793400011PubMedID: 25256598Scopus ID: s2.0-84911413890Local ID: 0d0c7b87-d61d-4b24-8f51-f079e15f4458OAI: oai:DiVA.org:ltu-3054DiVA: diva2:975910
Note

Validerad; 2014; 20140930 (andbra)

Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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CiteExportLink to record
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