Structural basis and functional significance of food-derived inhibitors of islet amyloid polypeptide fibrillation toward antidiabetic effects

Several approaches are taken in type 2 diabetes (T2D) management to increase insulin effectiveness through the reduction of hepatic glucose production, release and reabsorption, and enzyme inhibition. These approaches are geared toward treating the downstream effects of (3-cell malfunction rather than minimizing the initial source of stress contributing to the loss of (3-cell mass. Islet amyloid polypeptide (IAPP), or amylin, causes a loss of (3-cell mass upon fibrillation, a common feature in T2D development. Thus, IAPP fibrillation is emerging as a physiological target in mitigating (3-cell cytotoxicity. This paper discusses recent advances in the inhibition of IAPP fibrillation by food-derived polyphenols, peptides, and polysaccharides. Structure-activity relationships suggest the importance of motifs such as catechol-containing groups of polyphenols in increasing anti-fibrillation activity.