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Aggregating the amyloid Aβ 11–25 peptide into a four‐stranded β‐sheet structure
Author(s) -
Boucher Geneviève,
Mousseau Normand,
Derreumaux Philippe
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21134
Subject(s) - antiparallel (mathematics) , reptation , monomer , globular protein , chemistry , biophysics , beta sheet , amyloid fibril , peptide , crystallography , physics , biochemistry , biology , amyloid β , polymer , medicine , disease , organic chemistry , pathology , quantum mechanics , magnetic field
We present a detailed analysis of the structural properties of one monomer of Aβ 11–25 as well as of the aggregation mechanisms for four chains of Aβ 11–25 using the activation–relaxation technique coupled with a generic energy potential. Starting from a random distribution of these four chains, we find that the system assembles rapidly into a random globular state that evolves into three‐ and four‐stranded antiparallel β‐sheets. The aggregation process is considerably accelerated by the presence of preformed dimers. We also find that the reptation mechanism already identified in shorter peptides plays a significant role here in allowing the structure to reorganize without having to fully dissociate. Proteins 2006. © 2006 Wiley‐Liss, Inc.