磺胺类化合物与碳酸酐酶同工型 I、II、VII、XII 和 XIV 结合的抑制模式。
Inhibition pattern of sulfamide-related compounds in binding to carbonic anhydrase isoforms I, II, VII, XII and XIV.
机构信息
Medicinal Chemistry, Department of Biological Sciences, Faculty of Exact Sciences, National University of La Plata, 47 and 115, La Plata B1900BJW, Argentina.
出版信息
Bioorg Med Chem. 2013 Mar 15;21(6):1410-8. doi: 10.1016/j.bmc.2012.10.048. Epub 2012 Nov 29.
A set of sulfamides and sulfamates were synthesized and tested against several isoforms of carbonic anhydrase: CA I, CA II, CA VII, CA XII and CA XIV. The biological assays showed a broad range of inhibitory activity, and interesting results were found for several compounds in terms of activity (Ki <1μm) and selectivity: some aromatic sulfamides are active against CA I, CA II and/or CA VII; while they are less active in CA XII and CA XIV. On the other hand, bulky sulfamides are selective to CA VII. To understand the origin of the different inhibitory activity against each isozyme we used molecular modeling techniques such as docking and molecular dynamic simulations.
一组磺胺类和磺胺酸盐被合成并针对几种碳酸酐酶同工酶进行了测试
CA I、CA II、CA VII、CA XII 和 CA XIV。生物测定显示出广泛的抑制活性，并且发现一些化合物在活性（Ki<1μm）和选择性方面具有有趣的结果：一些芳香磺胺类化合物对 CA I、CA II 和/或 CA VII 具有活性；而对 CA XII 和 CA XIV 的活性较低。另一方面，大体积的磺胺类化合物对 CA VII 具有选择性。为了了解对每种同工酶的不同抑制活性的起源，我们使用了 docking 和分子动力学模拟等分子建模技术。
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