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

Daniel E. Otzen, Mikael Oliveberg*

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

11 Citations (Scopus)


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


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


Dive into the research topics of 'Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide'. Together they form a unique fingerprint.

Cite this