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Transient formation of nano-crystalline structures during fibrillation of an A-like peptide
Umeå University, Faculty of Science and Technology, Chemistry.
2004 (English)In: Protein Science, Vol. 13, 1417-21 p.Article in journal (Refereed) Published
Abstract [en]

During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the A-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended -strand conformation.

Place, publisher, year, edition, pages
2004. Vol. 13, 1417-21 p.
Keyword [en]
peptide aggregation, protein aggregation, amyloid fibrils, peptide crystal, electron microscopy
Identifiers
URN: urn:nbn:se:umu:diva-14791DOI: doi:10.1110/ps.03538904OAI: oai:DiVA.org:umu-14791DiVA: diva2:154463
Available from: 2007-06-18 Created: 2007-06-18 Last updated: 2011-01-12Bibliographically approved

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