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

Abstract

AbstractWe consider the effect of lauric acid on the stability of various fibril-like assemblies of Aβ 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 Aβ40-fibrils we find that addition of lauric acid strengthen the stability of fibrils built from the more toxic triple-stranded S-shaped Aβ42-peptides. Or results may help to understand how specifics of the brain-environment modulate amyloid formation and propagation.