Mechanisms of sesamol and sesamin inhibiting α-glucosidase activity by spectroscopy and molecular docking

Sesamol and sesamin inhibit α-glucosidase activity and may therefore be effective in treating type 2 diabetes, but their mechanisms remain unknown. Therefore, the inhibitory effects of sesamol and sesamin on α-glucosidase activity were analyzed by multispectral technique and molecular docking. Our findings indicated that the sesamol and sesamin had a significant influence on α-glucosidase activity, with IC50 values of 0.96 mM and 0.33 mM, respectively, and their inhibition types were non-competitive. Both sesamol and sesamin quenched the fluorescence by a static quenching mechanism. The results of three-dimensional (3D) fluorescence, circular dichroism (CD) spectroscopy and Fourier transform infrared spectrometer (FT-IR) showed that both sesamol and sesamin had certain effects on the conformation of α-glucosidase. Molecular docking results revealed that both sesamol and sesamin could spontaneously bind to α-glucosidase and form hydrogen bonds with some of the amino acid residues of the enzyme. As a result, this study sheds new light on sesamol/sesamin as a potential α-glucosidase inhibitor.