Jerah Ahmed, Hobani Yahya, Kumar B Vinod, Bidwai Anil
College of Applied Medical Sciences, Jazan University, Jazan, KSA.
College of Applied Medical Sciences, Jazan University, Jazan, KSA ; ndex Medical College Hospital and Research Center, Indore, India.
Bioinformation. 2015 Aug 31;11(8):387-92. doi: 10.6026/97320630011387. eCollection 2015.
In silico interaction of curcumin with the enzyme MMP-3 (human stromelysin-1) was studied by molecular docking using AutoDock 4.2 as the docking software application. AutoDock 4.2 software serves as a valid and acceptable docking application to study the interactions of small compounds with proteins. Interactions of curcumin with MMP-3 were compared to those of two known inhibitors of the enzyme, PBSA and MPPT. The calculated free energy of binding (ΔG binding) shows that curcumin binds with affinity comparable to or better than the two known inhibitors. Binding interactions of curcumin with active site residues of the enzyme are also predicted. Curcumin appears to bind in an extendended conformation making extensive VDW contacts in the active site of the enzyme. Hydrogen bonding and pi-pi interactions with key active site residues is also observed. Thus, curcumin can be considered as a good lead compound in the development of new inhibitors of MMP-3 which is a potential target of anticancer drugs. The results of these studies can serve as a starting point for further computational and experimental studies.
使用AutoDock 4.2作为对接软件应用程序，通过分子对接研究了姜黄素与MMP-3酶（人基质溶素-1）的计算机模拟相互作用。AutoDock 4.2软件是研究小分子与蛋白质相互作用的有效且可接受的对接应用程序。将姜黄素与MMP-3的相互作用与该酶的两种已知抑制剂PBSA和MPPT的相互作用进行了比较。计算得到的结合自由能（ΔG结合）表明，姜黄素的结合亲和力与两种已知抑制剂相当或更好。还预测了姜黄素与酶活性位点残基的结合相互作用。姜黄素似乎以伸展构象结合，在酶的活性位点形成广泛的范德华接触。还观察到与关键活性位点残基的氢键和π-π相互作用。因此，姜黄素可被视为开发MMP-3新抑制剂的良好先导化合物，MMP-3是抗癌药物的潜在靶点。这些研究结果可作为进一步计算和实验研究的起点。
