Neuraminidase inhibitor has been an attractive target for the development of novel antiinfluenza drugs. In present work we have carried out docking analysis of Zanamivir with Human Neuraminidase (H1N1) to understand the structural features responsible for their potent anti- Anti-Aiv activity. The analysis reveals that the majority of interactions of Zanamivir are hydrophobic, polar and steric in nature. Zanamivir forms hydrogen bond with the amino acid residues Asp(a)151, Arg(a)118, Arg(a) 371, Arg(a) 292,Glu(a)277, Glu(a)276, Arg(a) 152,Trp(a) 178,Glu(a)227(Figure 4(b) ). The present docking analysis reveals that three water molecules directly affect the interaction of Zanamivir with neuraminidase. Field analysis divulge that acetamido group at c-3 position of pyran nucleus is serve as strong electronegative centre (charges -9.88 and -10.18) and act as electron acceptor in Zanamivir neuraminidase H-bond interaction. This can be useful to get alert about the particular part of the field is required for binding.
