Research Article Open Access

Bioactive Compounds Screening from Zingiberaceae Family as Influenza A/Swine Flu Virus Neuraminidase Inhibitor through Docking Approach

Usman Sumo Friend Tambunan1, Fadilah 1 and Arli Aditya Parikesit1
  • 1 University of Indonesia, Indonesia

Abstract

Problem statement: Influenza A/H1N1 is a disease caused by infection of influenza a virus subtype H1N1. It is a major health problem in tropical and subtropical countries. This virus constantly mutates and consequently will be developed into new drug-resistant strains. Approach: In this research, we have conducted docking study to screen bioactive compounds from Zingiberaceae family, which has a role as neuraminidase inhibitor of influenza a virus. Results: The docking result identified that 1, 2-di-O- β-D-glucopyranosyl-4-allylbenzene (BGA) compound has the affinity and ability to inhibit neuraminidase. There are fourteen residues contact of BGA compound to neuraminidase and eight residues contact of enzyme that formed hydrogen bond with catalytic site. Conclusion/recommendation: The docking result showed that BGA has better binding energy and affinity compared with other bioactive compounds and the standard compounds.

OnLine Journal of Biological Sciences
Volume 10 No. 4, 2010, 151-156

DOI: https://doi.org/10.3844/ojbsci.2010.151.156

Submitted On: 29 January 2011 Published On: 31 December 2010

How to Cite: Tambunan, U. S. F., Fadilah, & Parikesit, A. A. (2010). Bioactive Compounds Screening from Zingiberaceae Family as Influenza A/Swine Flu Virus Neuraminidase Inhibitor through Docking Approach. OnLine Journal of Biological Sciences, 10(4), 151-156. https://doi.org/10.3844/ojbsci.2010.151.156

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Keywords

  • Neuraminidase inhibitory
  • molecular docking
  • influenza A/H1N1
  • bioactive compounds
  • neuraminidase inhibitor
  • initial screening process
  • screen bioactive
  • subtropical countries
  • catalytic site
  • hydrogen bond
  • conducted docking study
  • β-D-glucopyranosyl-4- allylbenzene (BGA)
  • surface glycoprotein