Amyloid fibrils: modulation of formation and structure by copper(ii)

Abstract

The role of Cu^II-complexation of amyloidogenic peptides on the formation and structure of aggregates were analyzed in order to obtain a general insight into modulation of peptide aggregation by metal ions. The results mimicked various facets of biological relevant peptides/protein-aggregation. Important mechanistic features are the ability of Cu^II to associate the peptides by bridging coordination, the structural changes induced by Cu^II binding and their effect on peptide–peptide interactions.