In silico evaluation of molecular interactions between known α-glucosidase inhibitors and homologous α-glucosidase enzymes from Saccharomyces cerevisiae, Rattus norvegicus, and GANC-human

Teni Ernawati, Abdul Mun'im, Muhamad Hanafi, Arry Yanuar

Research output: Contribution to journalArticle

Abstract

The aim of this study was to observe molecular interactions between α-glucosidase inhibitor (IAG) and α-glucosidase enzymes derived from Saccharomyces cerevisiae, Rattus norvegicus, and GANC-human. These enzymes were studied against four of the well-known IAG such as 1-deoxynojirimycin, acarbose, miglitol, and voglibose. We compared the selected IAG by means of a computer-aided drug design protocol involving homology modeling of the target protein and the virtual screening with docking simulations in the binding free energy function. Compared to acarbose, miglitol, voglibose, 1-deoxynojirimycin showed a significant inhibition of three target macromolecules of α-glucosidase enzyme. 1-Deoxynojirimycin had the highest inhibition on α-glucosidase, followed by miglitol, voglibose, and acarbose, respectively.

Original languageEnglish
Pages (from-to)14-20
Number of pages7
JournalThai Journal of Pharmaceutical Sciences
Volume42
Issue number1
Publication statusPublished - 1 Jan 2018

Keywords

  • Human (GANC) α-glucosidase enzyme
  • Molecular docking
  • Rattus norvegicus
  • Saccharomyces cerevisiae
  • α-Glucosidase

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