Aggregating the amyloid Aβ11-25 peptide into a four-stranded β-sheet structure

We present a detailed analysis of the structural properties of one monomer of A beta(11-25) as well as of the aggregation mechanisms for four chains of A beta(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.