Molecular dynamics studies of the inhibitory mechanism of copper(Ⅱ) on aggregation of amyloid β-peptide

摘要

The inhibitory mechanism of copper(Ⅱ) on the aggregation of amyloid β-peptide (Aβ) was investigated by molecular dynamics simulations.The bindingmode ofcopper(Ⅱ) with Aβ is characterized by the imidazolenitrogenatom,Nπ, of the histidine residue H13,acting as the anchoring site, and the backbone's deprotoned amide nitrogen atoms as the main binding sites. Drove by the coordination bonds and their induced hydrogen bond net, the conformations of Aβ converted from β-sheet non-β-sheet conformations, which destabilized the aggregation of Aβ into fibrils.