Abstract
Tinospora cordifolia extract decreased the activity of glycogen phosphorylase in the liver and widely used in the treatment of diabetes mellitus. This in silico study aimed to screen the active compound(s) of T. cordifolia which play a role in its hypoglycemic activity as glycogen phosphorylase inhibitor by molecular docking analysis. Thirteen chemical constituents of T. cordifolia were used as ligands for docking study. The glycogen phosphorylase structure was obtained from Brookhaven protein databank (1LWO). Docking analysis was performed using Autodock Vina and PyRx 8. The inhibitory activity was analyzed by comparison the binding energy and binding mode of interaction of T. cordifolia chemical constituents on glycogen phosphorylase. The results indicate that magnoflorine, cordiofolioside A, and syringin exhibited good affinity to glycogen phosphorylase, by interacted at catalytic site of enzyme
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