Molecular docking and binding energy studies on nuraminidase of h1n1 reveal possible answer to its resistance for oseltamivir

Meshram R.J.¹*, Jangle S.N.^2
1Center for Biotechnology, Pravara Institute of Medical Sciences, Loni, MS, India,
²Center for Biotechnology, Pravara Institute of Medical Sciences, Loni, MS, India,
* Corresponding Author : rohan_meshram@rediffmail.com

Received : -     Accepted : -     Published : 21-12-2009
Volume : 1     Issue : 2       Pages : 34 - 39
Int J Drug Discov 1.2 (2009):34-39
DOI : http://dx.doi.org/10.9735/0975-4423.1.2.34-39

Keywords : Universal Force Field, Parametric Method 3, ArgusLab, AScore Scoring Function, Binding Affinity
Conflict of Interest : None declared

Neuraminidase (NA) is the enzyme coded by Influenza-A virus genome that catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. It cleaves off the terminal sialic acids on the glycosylated NA during virus budding to facilitate virus release, making it most important target for designing drug against Flu. Recently cases are reported of Influenza virus becoming resistant to NA inhibitors like Oseltamivir. The outbreak of Swine flu and its resistance to oseltamivir is suspected to be caused due to mutation H274Y in the enzyme neuraminidase of H1N1 strain of influenza virus. This work involved active site analysis, molecular docking and binding energy studies on NA that demonstrate the conformational changes in active site which might result in increase in binding energy of oseltamivir when it is mutated as H274Y.