Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure |
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Authors: | Boucher Geneviève Mousseau Normand Derreumaux Philippe |
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Affiliation: | Département de Physique and Centre Robert-Cedergren en bioinformatique, Université de Montréal, C.P. 6128, Succursale Centre-ville Montréal, Québec H3C 3J7, Canada. |
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Abstract: | We present a detailed analysis of the structural properties of one monomer of Abeta(11-25) as well as of the aggregation mechanisms for four chains of Abeta(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 beta-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. |
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Keywords: | protein aggregation Alzheimer beta amyloid fibrils molecular dynamics activation‐relaxation technique simulation |
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