Inhibition of α-glucosidase by trilobatin and its mechanism: kinetics, interaction mechanism and molecular docking

was 0.24 ± 0.02 mM. The analysis of fluorescence spectra demonstrated that the formation of the trilobatin-α-glucosidase complex was driven mainly by hydrogen bonding and van der Waals forces, resulting in the conformational changes of α-glucosidase. Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD) measurements suggested that the interaction could change the micro-environment and conformation of α-glucosidase affected by trilobatin. Molecular docking analysis determined the exact binding sites of trilobatin on α-glucosidase. These results indicated that trilobatin is a strong α-glucosidase inhibitor, thus it could be conducive to ameliorate T2DM.