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UNDERSTANDING IMPACT OF 150-CAVITY IN INFLUENZA VIRUS NEURAMINIDASE FOR NOVEL ANTI-INFLUENZA DRUG DESIGN. Saroj Basnet, Janaynta Sarma, Amit Mittal, Yashwant Chaudhary

UNDERSTANDING IMPACT OF 150-CAVITY IN INFLUENZA VIRUS NEURAMINIDASE FOR NOVEL ANTI-INFLUENZA DRUG DESIGN.

Saroj Basnet, Janaynta Sarma, Amit Mittal, Yashwant Chaudhary

International Journal of Natural Product Science 2012: Spl Issue 1:108.

Abstract(RBIP-108)

We carried out systematic computational study to investigate the binding mechanism of six ligands to H1N1 and H5N1 neuraminidase enzymes. The group-1 neuraminidase of influenza virus possesses a 150-cavity, which is adjacent to the active pocket responsible for conformational change from the open form to the closed form when the enzyme is binding with a ligand. Using rigid and flexible mode algorithm, we have analysed additional interactions with the 150-cavity when substitution was done at C-3 position of available drugs in the market. The three derivatives selected in this study show good extension towards both H1N1 and H5N1 150-cavity region.This finding may stimulate new strategy or provide useful insights for working on the target vitally important for novel anti-influenza drug design.

Keywords: Induced Fit Docking, Neuraminidase, H1N1, 150-cavity, H5N1, Resistance, Antigenic Shift, Drug Design,
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