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 Zn^(2+)ions.Different possible metal binding sites were probed within in...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 Zn^(2+)ions.Different possible metal binding sites were probed within insulin fibrils at the molecular level.The effects of Zn^(2+)ions on the fibrillation of insulin are determined for each specific Zn^(2+)-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 Zn^(2+)ions.展开更多
基金supported by the Israel Science Foundation(grant 532/15).
文摘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 Zn^(2+)ions.Different possible metal binding sites were probed within insulin fibrils at the molecular level.The effects of Zn^(2+)ions on the fibrillation of insulin are determined for each specific Zn^(2+)-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 Zn^(2+)ions.
