https://www.selleckchem.com/pr....oducts/isoproterenol
C3G could spontaneously bind with α-glucosidase to form complexes by hydrogen bonds. The secondary structure of α-glucosidase changed in varying degrees after complexation with C3G. The α-helical and β-turn contents of α-glucosidase decreased, whereas the β-sheet content and the irregular coil structures increased. Molecular docking speculated that C3G could form hydrogen bonds with α-glucosidase by binding to the active sit (Leu 313, Ser 157, Tyr 158, Phe 314, Arg 315, and two Asp 307). These findings may be use
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