Exploration of the inhibitory mechanisms of trans-polydatin/resveratrol on α-glucosidase by multi-spectroscopic analysis, in silico docking and molecular dynamics simulation.

Plant-derived phenolics as natural α-glucosidase (α-GLU) inhibitors have attached great attention in the treatment of type-II diabetes mellitus currently. In this study, trans-polydatin and its aglycone resveratrol were found to show a notable inhibitory activity on α-GLU in a mixed-type manner with IC values of 18.07 and 16.73 μg/mL, respectively, which were further stronger than anti-diabetic drug acrabose (IC = 179.86 μg/mL). Multi-spectroscopic analysis results indicated that polydatin/resveratrol bound to α-GLU with one affinity binding site which was mainly driven by hydrogen bonds and van der Waals forces, and this binding process resulted in conformational alteration of α-GLU. In silico docking study showed that polydatin/resveratrol can well interact with the surrounding amino acid residues in the active cavity of α-GLU. Molecular dynamics simulation further clarified the structure and characterization of α-GLU-polydatin/resveratrol complexes. This study might supply a theoretical basis for the designing of novel functional foods with polydatin/resveratrol.