Mechanism of inhibition of α-glucosidase activity by bavachalcone

Abstract

Bavachalcone is an important active component of the traditional Chinese medicine Fructus Psoraleae. The inhibitory effect of bavachalcone on α-glucosidase activity is reported for the first time and the mechanism elucidated by molecular docking. The inhibition of α-glucosidase by bavachalcone (IC50 15.35 ± 0.57 μg/mL) was significantly superior to acarbose (IC50 2.77 ± 0.09 mg/mL). Inhibition type was mixed competitive and non-competitive. Molecular docking suggested this inhibition stems from hydrogen bonds formed with the trp391, arg428, and trp710 residues of α-glucosidase.