Copper binding and protein aggregation: a journey from the brain to the human lens

Abstract

-induced non-amyloid aggregation of γ-crystallins, it is evident that, although the impact in aggregation - and the nature of the aggregate - may differ in each system, at the molecular level there is a competition between metal ion coordination and the stability of β-sheet structures. Considering the importance of the β-sheet fold in biology, it is fundamental to understand the energetics and molecular details behind such competition. This opinion article aims to highlight future research directions in the field that can help tackle the important question of how metal ion binding may impact protein folding and aggregation and how this relates to disease.

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