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  • Title: Probing amyloid fibril formation of the NFGAIL peptide by computer simulations.
    Author: Melquiond A, Gelly JC, Mousseau N, Derreumaux P.
    Journal: J Chem Phys; 2007 Feb 14; 126(6):065101. PubMed ID: 17313247.
    Abstract:
    Amyloid fibril formation, as observed in Alzheimer's disease and type II diabetes, is currently described by a nucleation-condensation mechanism, but the details of the process preceding the formation of the nucleus are still lacking. In this study, using an activation-relaxation technique coupled to a generic energy model, we explore the aggregation pathways of 12 chains of the hexapeptide NFGAIL. The simulations show, starting from a preformed parallel dimer and ten disordered chains, that the peptides form essentially amorphous oligomers or more rarely ordered beta-sheet structures where the peptides adopt a parallel orientation within the sheets. Comparison between the simulations indicates that a dimer is not a sufficient seed for avoiding amorphous aggregates and that there is a critical threshold in the number of connections between the chains above which exploration of amorphous aggregates is preferred.
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