中文摘要：

Polyoxometalate (POM ) 举办有希望的抗病毒的活动。它显示出用途广泛的禁止的能力，高效率，和低毒性。试验性的试金证明包含 polyoxotungstates 的钛举办 anti-influenza-virus 活动。在这份报纸， di-Ti-substituted polyoxotungstate 的五异构体的有约束力的机制，[-1,2-PTi2W10O40]7？(-1,2),[-1,6-PTi2W10O40]7？(-1,6),[-1,5-PTi2W10O40]7？(-1,5),[-1,4-PTi2W10O40]7？(-1,4) 并且[-1,11-PTi2W10O40]7？(-1,11), 到流行性感冒病毒的五种子类型 neuraminidase (FluV -- NA ) 被使用分子的停靠在水的答案的上下文调查，分子的动力学学习。结果证明异构体 -1,2 作为到 neuraminidase 的一个潜在的禁止者比另外的异构体优异。在 NA 的活跃地点附近的断然控告的精氨酸残余能被否定地控告的 POM 导致使自己适应，形式盐能与 POM 衔接相互作用和氢契约相互作用。POM/NA 建筑群的有约束力的免费精力从 ? 5.36 到 ? 8.31 kcal 摩尔 ? 1。静电的相互作用被发现在到 NA 的 POM 的有约束力的过程期间是驱动力。POM 趋于在活跃衣袋的边首先与 N1 和 N8 绑的 conformational 分析表演，它引起铁钳的 conformational 变化组织包括残余 347 和循环 150。而， N2， N9 和 N4 的活跃衣袋被发现更广阔，它允许 POM 直接进入活跃衣袋并且坚定地在那里抛锚。当尽管有 NA 的曾经增加的异种， POM 能作为一个有希望的禁止者导致 NA 和热点 POM 的活跃地点的重组到 NA，这研究证明那否定地控告了 ligand。

英文摘要：

Polyoxometalate （POM） has promising antiviral activities. It shows broad-spectrum inhibiting ability, high efficiency, and low toxicity. Experimental assays show that titanium containing polyoxotungstates have anti-influenza-virus activity. In this paper, the binding mechanisms of five isomers of di-Ti-substituted polyoxotungstate, [α-PTi2W10O40]7- （α-1,2）, [α-1,6-PTi2W10O40]7- （α-1,6）, [α-1,5-PTi2W10O40]7 （α-1,5）, [α-1,4-PTi2W10O40]7- （α-1,4） and [α-1,11-PTi2W10O40]7- （α-1,11）, to five subtypes of influenza virus A neuraminidase （FluV-A NA） were investigated in the context of aqueous solution by using molecular docking and molecular dynamics studies. The results show that the isomer α-1,2 is superior to other isomers as a potential inhibitor to neuraminidase. The positively charged arginine residues around the active site of NA could be induced by negatively charged POM to adapt themselves and could form salt bridge interactions and hydrogen bond interactions with POM. The binding free energies of POM/NA complexes range from -5.36 to -8.31 kcal mo1-1. The electrostatic interactions are found to be the driving force during the binding process of POM to NA. The conformational analysis shows that POM tends to bind primarily with N1 and N8 at the edge of the active pocket, which causes the conformational change of the pincers structure comprising residue 347 and loop 150. Whereas, the active pockets of N2, N9 and N4 are found to be more spacious, which allows POM to enter into the active pockets directly and anchor there firmly. This study shows that negatively charged ligand as POM could induce the reorganization of the active site of NA and highlights POM as a promising inhibitor to NA despite the ever increasing mutants of NA.