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
Author: Wening Lestari, Rizna
Triana Dewi, Leonardus Broto Sugeng Kardono, Arry Yanuar
Journal Code: jpkimiagg170027
Artikel Terkait :
Jp Kimia gg 2017
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