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首页> 外文期刊>International journal of computational biology and drug design >Computational molecular docking and structural specificity of bipyrazoles as non-zinc cheiating inhibitors of MMP-13
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Computational molecular docking and structural specificity of bipyrazoles as non-zinc cheiating inhibitors of MMP-13

机译：联吡唑作为MMP-13的非锌螯合抑制剂的计算分子对接和结构特异性

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摘要

Matrix metalloproteinases (MMP) degrade extra cellular matrix proteins. Matrix MMPs are structurally similar, but differ in substrate specificity. A large number of MMP inhibitors have been described as zinc binding groups; however, in this paper we report computational identification of novel bipyrazoles as non-zinc cheiating inhibitors of MMP-13. Molecular docking analysis performed between a set of 37 bipyrazoles vs. MMP-13 resulted in compound 26 observed with a score of -241 kcal/mol which is nearly half fold than the 456C bound ligand (-155.299 kcal/mol). The binding orientations of all bipyrazoles are geometrically similar to the co-crystallised ligand of 456C. Considering the Distance (A°) between zinc atom and nearest N atom on pyrazole as well as Lipinski's rule of 5, compound 2 might act as a non-zinc cheiating inhibitor.
机译：基质金属蛋白酶（MMP）降解细胞外基质蛋白。基质MMP在结构上相似，但底物特异性不同。大量的MMP抑制剂已被描述为锌结合基团。但是，在本文中，我们报告了新型联吡唑作为MMP-13的非锌螯合抑制剂的计算鉴定。在一组37种联吡唑与MMP-13之间进行的分子对接分析导致观察到化合物26的得分为-241 kcal / mol，几乎是456C结合配体（-155.299 kcal / mol）的一半。所有联吡唑的结合取向在几何上均类似于456C的共结晶配体。考虑到吡唑上锌原子和最接近的N原子之间的距离（A°）以及Lipinski规则5，化合物2可能充当非锌螯合抑制剂。

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