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

Wening Lestari (Center for Radioisotopes and Radiopharmaceuticals Technology, National Nuclear Energy Agency, Puspiptek, Serpong 15314)
Rizna Triana Dewi (Research Center for Chemistry, Indonesian Institute of Sciences, Puspiptek, Serpong 15314)
Leonardus Broto Sugeng Kardono (Research Center for Chemistry, Indonesian Institute of Sciences, Puspiptek, Serpong 15314)
Arry Yanuar (Faculty of Pharmacy, Universitas Indonesia, Depok 16424)

Indonesian Journal of Chemistry
Vol 17, No 1 (2017)

Sulochrin is known to have an activity as inhibitors of the α-glucosidase enzyme. In this report interaction of sulochrin to the active site of the α-glucosidase enzyme from Saccharomyces cerevisiae was studied by docking method. The crystal structure of α-glucosidase from S. 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. These studies show that 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 the α-glucosidase enzyme.