Insulin fibrillation control by specific zinc binding sites

Herein, we present for the first time a study that identifies the morphology of full-length insulin fibrils in the absence and in the presence of Zn2+ ions. Different possible metal binding sites were probed within insulin fibrils at the molecular level. The effects of Zn2+ ions on the fibrillation of insulin are determined for each specific Zn2+-binding site on the characterization and stabilization of the fibrils. Our findings are expected to initiate future studies to investigate the functions of unique insulin fibrils that bind the Zn2+ ions.