关键词: 白藜芦醇, α-葡萄糖苷酶, 抑制动力学, 分子对接, 同源模建

Abstract: Due to its extensive biological activities such as hypoglycemic effects, resveratrol has gained much attention. Besides, α-glucosidase inhibitors can decrease hyperglycemia, which is closely related to the treatment of type-2 diabetes. In the present study, enzyme-inhibitory kinetics and computer simulation were applied to investigate the effect of resveratrol on the activity of α-glucosidase. The activity of α-glucosidase was measured by spectrophotometry, the inhibition kinetics was investigated using Lineweaver-Burk method, and the binding mechanisms between resveratrol and α-glucosidase were explored using molecular docking simulation. The results indicated that resveratrol was a stronger inhibitor (half maximal inhibitory concentration (IC50) = 5.047 μmol/L) than acarbose (IC50 = 632.6 μmol/L). The inhibition type was noncompetitive, and the value of Ki was 5.743 μmol/L. Molecular docking results demonstrated that the existence of multiple binding modes between resveratrol and α-glucosidase did not affect the binding interaction between acarbose and α-glucosidase. Therefore, resveratrol had potent inhibitory activity against α-glucosidase, and thus had the potential to be developed as an antidiabetic drug or as a dietary supplement in a synergetic manner with acarbose for the treatment of diabetes.

Key words: resveratrol, α-glucosidase, inhibition kinetics, molecular docking, homology modeling