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

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Author(s): Meshram R.J. | Jangle S.N.

Journal: International Journal of Drug Discovery
ISSN 0975-4423

Volume: 1;
Issue: 2;
Start page: 34;
Date: 2009;
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Keywords: Universal Force Field | Parametric Method 3 | ArgusLab | AScore Scoring Function | Binding Affinity

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

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