Docking Sulochrin and Its Derivative as α-Glucosidase Inhibitors of Saccharomyces cerevisiae

Sulochrin is known to have an activity as inhibitors of the alpha-glucosidase enzyme. In this report interaction of sulochrin to the active site of the alpha-glucosidase enzyme from Saccharomyces cerevisiae was studied by docking method. The crystal structure of alpha-glucosidase from S. cerevisiae obtained from the homology method using alpha-glucosidase from S. cerevisiae (Swiss-Prot code P53341) as a target and crystal structure of isomaltase from S. cerevisiae (PDB code 3A4A) as a template. These studies show that sulochrin and sulochrin-I could be bound in the active site of alpha-glucosidase from S. cerevisiae through the formation of hydrogen bonds with Arg213, Asp215, Glu277, Asp352. Sulochrin-I has stability and inhibition of the alpha-glucosidase enzyme better than sulochrin. The iodine atom in the structure of sulochrin can increase the activity as an inhibitor of the alpha-glucosidase enzyme.