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Protein Sci. 2004 May;13(5):1417-21.

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

Author information

1
Department of Life Sciences, Aalborg University, Aalborg, Denmark.

Abstract

During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Abeta-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 A) 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 A to 120 A 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 beta-strand conformation.

PMID:
15096642
PMCID:
PMC2286749
DOI:
10.1110/ps.03538904
[Indexed for MEDLINE]
Free PMC Article

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