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Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide

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During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-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 β-strand conformation.

Original languageEnglish
JournalProtein Science
Pages (from-to)1417-1421
Number of pages5
Publication statusPublished - 1 May 2004

    Research areas

  • Amyloid fibrils, Electron microscopy, Peptide aggregation, Peptide crystal, Protein aggregation

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