Inhibitory Mechanism of Baicalein Against α-Glucosidase

Baicalein is one of the main bioactive compounds in Scutellaria baicalensis. In this study, its inhibitory mechanism against α-glucosidase from Saccharomyces cerevisiae was clarified based on experimental and molecular simulation methods. According to HPLC analysis, the α-glucosidase inhibitory activity of S. baicalensis (IC 50 , 6.75 ± 0.08 μg mL −1 ) was superior to that of acarbose (IC 50 , 2.52 ± 0.12 mg mL −1 ). The fluorescence results suggested that baicalein could form a complex with α-glucosidase at the molar ratio of 1 under the drive of hydrogen bonding and van der Waals force. Molecular docking showed that baicalein could form hydrogen bonds with Trp391, Arg428, Gly566,and Glu771 of α-glucosidase, and interacted with Phe385, Phe389, Arg387, Glu429, Phe444, Trp789, and Trp710 by hydrophobic force, which coincided with the experimental results. It can be concluded that baicalein is a potential α-glucosidase inhibitor for controlling the postprandial blood glucose level of diabetics.