Transient formation of nano-crystalline structures during fibrillation of an A-like peptide
2004 (English)In: Protein Science, Vol. 13, 1417-21 p.Article in journal (Refereed) Published
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.
peptide aggregation, protein aggregation, amyloid fibrils, peptide crystal, electron microscopy
IdentifiersURN: urn:nbn:se:umu:diva-14791DOI: doi:10.1110/ps.03538904OAI: oai:DiVA.org:umu-14791DiVA: diva2:154463