Inhibition mechanism and behaviour of wedelolactone against α-glucosidase.

Abstract

The quest for effective and safe treatments for diabetes mellitus has led to the exploration of natural metabolites as potential α-glucosidase inhibitors. This study delves into the inhibition mechanism of wedelolactone against α-glucosidase and its hypoglycaemic activity. Activity assay results discovered that wedelolactone functioned as a mixed-type inhibitor, with an IC₅₀ of 39.12 ± 2.54 μM, surpassing the potency of the standard drug acarbose. Employing multi-spectra methods, our findings indicated that wedelolactone binding induced conformation changes in α-glucosidase to attenuate its enzymatic activity, as evidenced by fluorescence quenching, synchronous fluorescence, 3D fluorescence, CD spectra, and ANS assay. Molecular docking studies provided insights into the specific interactions between wedelolactone and α-glucosidase. Collectively, these results laid the groundwork for the potential application of wedelolactone as a natural therapeutic agent in diabetes management.