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Protein Science (2004), 13:1417-1421. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

Transient formation of nano-crystalline structures during fibrillation of an A{beta}-like peptide

Daniel E. Otzen1 and Mikael Oliveberg2

1 Department of Life Sciences, Aalborg University, DK-9000 Aalborg, Denmark
2 Department of Biochemistry, Umeå University, S-90187 Umeå, Sweden

(RECEIVED December 9, 2003; FINAL REVISION February 4, 2004; ACCEPTED February 9, 2004)



Abstract

During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the A{beta}-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 {beta}-strand conformation.

Keywords: peptide aggregation; protein aggregation; amyloid fibrils; peptide crystal; electron microscopy

Reprint requests to: Mikael Oliveberg, Department of Biochemistry, Umeå University, S-90187 Umeå, Sweden; e-mail: mikael.oliveberg{at}chem.umu.se; fax: 46-90-786-7661.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03538904.


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