Transient formation of nano-crystalline structures during fibrillation of an Abeta-like peptide.
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.
Otzen
Daniel E
DE
Department of Life Sciences, Aalborg University, Aalborg, Denmark.
Oliveberg
Mikael
M
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D003460:Crystallization; D046529:Microscopy, Electron, Transmission; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D010455:Peptides; C493516:Tet-p peptide; C493515:amyloid beta-protein (25-38)