Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance
2009 (English)In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 385, no 2, 374-376 p.Article in journal (Refereed) Published
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.
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:umu:diva-18743DOI: 10.1016/j.ab.2008.10.034PubMedID: 19027706OAI: oai:DiVA.org:umu-18743DiVA: diva2:174678