Effect of Zn(II) on pramlintide: structural kink, fibril formation, antifungal activity

Abstract

Abstract The antimicrobial properties of amylin, a polypeptide secreted by the pancreas, are far less known than its antidiabetic function. Among the studied amylin analogues, the coordination of zinc(II) enhances the antifungal properties of pramlintide, a non-fibrillating therapeutic analogue of amylin; binding at the N-terminal amino group and His18 imidazole, it induces a kink in the peptide structure, which, in turn, triggers a fibrillization process of the complex, resulting in an amyloid structure most likely responsible for the disruption of the fungal cell.