Docking sulochrin and its derivative as α-glucosidase inhibitors of Saccharomyces cerevisiae

Wening Lestari, Rizna Triana Dewi, Leonardus Broto Sugeng Kardono, Arry Yanuar

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16 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)144-150
Number of pages7
JournalIndonesian Journal of Chemistry
Issue number1
Publication statusPublished - 2017


  • S. cerevisiae
  • Sulochrin
  • Sulochrin-I
  • α-glucosidase inhibitor


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