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Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP).
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP).
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP).
2009 (English)In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 385, no 2, 374-376 p.Article in journal (Refereed) Published
Abstract [en]

A general method to explore the dynamic nature of amyloid fibrils is described, combining hydrogen/deuterium exchange and nuclear magnetic resonance spectroscopy to determine the exchange rates of individual amide protons within an amyloid fibril. Our method was applied to fibrils formed by the amyloid-beta(1-40) peptide, the major protein component of amyloid plaques in Alzheimer's disease. The fastest exchange rates were detected among the first 14 residues of the peptide, a stretch known to be poorly structured within the fibril. Considerably slower exchange rates were observed in the remainder of the peptide within the beta-strand-turn-beta-strand motif that constitutes the fibrillar core.

Place, publisher, year, edition, pages
Elsevier, 2009. Vol. 385, no 2, 374-376 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:umu:diva-18743DOI: 10.1016/j.ab.2008.10.034PubMedID: 19027706OAI: oai:DiVA.org:umu-18743DiVA: diva2:174678
Available from: 2009-02-24 Created: 2009-02-24 Last updated: 2017-12-13Bibliographically approved

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Olofsson, AndersSauer-Eriksson, A ElisabethÖhman, Anders
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