Binding mode of neuraminidase target of H1N1 influenza virus with three inhibitors
Neuraminidase (NA) inhibitors play an important role against influenza virus recently. The binding mode of H1N1 influenza virus NA target with three commercial drugs, zanamivir (ZMR), oseltamivir (G39), and peramivir (BCX) were investigated by Autodock software. The obtained results showed that the hydrogen bond interaction, electrostatic interaction and hydrophobic effect contribute to the binding of the NA target with three inhibitors. The hydrogen bond interactions are very important to recognize the target which mainly focus on the Site1 and Site2 region of the NA biniding pocket. Electrostatic interactions also mainly exsit in the Site1 and Site2 region of target. The novel hydrophobic binding effect are found in the Site4 region of the NA target. The hydrophobic alkyl chain in G39 and BCX replace the glyceryl group of ZMR and rotate freely without the limitation of the hydrogen bond binding action. Thus the hydrophobic alkyl chain group in G39 and BCX could form some strong hydrophobic interactions with the surrounding residues in target NA. It is hopeful that these studies could provide an insight into novel NA inhibitor design based on the influenza virus target NA.
NETL
NSTL
万方数据
维普
