Abstract
The role of CuII-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 CuII to associate the peptides by bridging coordination, the structural changes induced by CuII binding and their effect on peptide–peptide interactions.
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