Stability of Aβ-fibril fragments in the presence of fatty acids

We consider the effect of lauric acid on the stability of various fibril-like assemblies of A{beta} peptides. For this purpose, we have performed molecular dynamics simulations of these assemblies either in complex with lauric acid or without presence of the ligand. While we do not observe a stabilizing effect on A{beta}40-fibrils we find that addition of lauric acid strengthen the stability of fibrils built from the more toxic triple-stranded S-shaped A{beta}42-peptides. Or results may help to understand how specifics of the brain-environment modulate amyloid formation and propagation.