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In Silico Molecular Docking of Fisetin with the Amyloidogenic Peptides Human Amylin and Aβ42

Amylin is a 37‐residue polypeptide which is co‐secreted with insulin from pancreatic beta cells. In diabetics, this protein has been shown to misfold and form amyloids which cause pancreatic cell death. The exact mechanism by which hIAPP causes cell death remains unknown. However, it has been associated with an aggregation of the protein and an increase in the oxidative stress in the cell. Amylin has similarities with Aβ42, the main protein implicated in the pathogenesis of Alzheimer's disease. Fisetin, a naturally occurring substance which is found in strawberries, apples and cucumbers has been shown to slow down the rate of aggregation of Aβ42. Fisetin has also been proven to have antioxidant properties. Based on the structural and molecular similarities between Aβ42 and human IAPP, we have used molecular alignment and docking experiments to study and show the possibility that fisetin may also slow down the rate of aggregation of human IAPP by binding to single IAPP chains before they form aggregates. Using Autodock Vina, Autodock Tools and Discovery Studio Visualizer, the binding sites of fisetin to both proteins were determined. Binding energies and protein conformations were also determined and analyzed.