A 3D-QSAR model was constructed for 53 N-BPs with the inhibition activities on hFPPS. A series of novel N-BPs inhibitors were designed and six novel N-BPs inhibitors with better biological activities and higher lipophilicity were screened out. Molecular docking and ONIOM (B3LYP/6-31 + G*:PM6:Amber) calculations showed that the inhibitors bound to the active site of hFPPS via hydrogen-bonding interactions, hydrophobic interactions, and cation-π interactions.

中文翻译：

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3D-QSAR，分子对接和ONIOM研究含氮双膦酸酯的结构-活性关系和作用机理

针对53个N-BPs构建了对hFPPS具有抑制活性的3D-QSAR模型。设计了一系列新型的N-BPs抑制剂，并筛选出了六种具有更好的生物活性和更高的亲脂性的新型N-BPs抑制剂。分子对接和ONIOM（B3LYP / 6-31 + G *：PM6：Amber）计算表明，抑制剂通过氢键相互作用，疏水相互作用和阳离子-π相互作用与hFPPS的活性位点结合。