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

ABSTRACT: Sulochrin known has activity as inhibitors of α-glucosidase enzyme. Interaction of sulochrin to active site of α-glucosidase enzyme from S. cerevisiae has studied by docking method. The crystal structure of α-glucosidase from S.accharomyces cerevisiae obtained from the homology method using α-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. Sulochrin and sulochrin-I could be bound in the active site of α-glucosidase from S. cerevisiae through the formation of hydrogen bonds with Arg213, Asp215, Glu277, Asp352. Sulochrin-I has stability and inhibition of the α-glucosidase enzyme better than sulochrin. The iodine atom in the structure of sulochrin can increase the activity as an inhibitor of α-glucosidase enzyme
KEYWORDS: Sulochrin; sulochrin-I; α-glucosidase inhibitor; S. cerevisiae
Author: Wening Lestari, Rizna Triana Dewi, Leonardus Broto Sugeng Kardono, Arry Yanuar
Journal Code: jpkimiagg170027

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