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Wening Lestari
Center for Radioisotopes and Radiopharmaceuticals Technology, National Nuclear Energy Agency, Puspiptek, Serpong 15314
Chemical Engineering, Chemistry & Bioengineering Chemistry

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Docking Sulochrin and Its Derivative as α-Glucosidase Inhibitors of Saccharomyces cerevisiae Wening Lestari; Rizna Triana Dewi; Leonardus Broto Sugeng Kardono; Arry Yanuar
Indonesian Journal of Chemistry Vol 17, No 1 (2017)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (430.473 KB) | DOI: 10.22146/ijc.23568

Abstract

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.
Co-Authors Arry Yanuar Leonardus Broto Sugeng Kardono Rizna Triana Dewi