首页> 外文OA文献 >Inhibition and binding studies of carbonic anhydrase isozymes I, II and IX with benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides
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Inhibition and binding studies of carbonic anhydrase isozymes I, II and IX with benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides

机译:苯并咪唑并[1,2-c] [1,2,3]噻二唑-7-磺酰胺对碳酸酐酶同工酶I,II和IX的抑制和结合研究

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摘要

The binding and inhibition strength of a series of benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides were determined for recombinant human carbonic anhydrase isoforms I, II, and IX. The inhibition strength was determined by a stop-flow method to measure carbon dioxide hydration. Inhibitor-enzyme binding was determined by two biophysical techniques--isothermal titration calorimetry and thermal shift assay. The co-crystal structure was determined by X-ray crystallography. Comparing the results obtained using three different inhibition and binding methods increased the accuracy of compound affinity ranking and the ability to determine compound inhibitory specificity towards a particular carbonic anhydrase isoform. In most cases, all three methods yielded the same results despite using very different approaches to measure the binding and inhibition reactions. Some of the compounds studied are submicromolar inhibitors of the isoform IX, a prominent cancer target.
机译:测定了一系列苯并咪唑并[1,2-c] [1,2,3]噻二唑-7-磺酰胺对重组人碳酸酐酶同工型I,II和IX的结合和抑制强度。通过停止流动法测定抑制强度,以测量二氧化碳的水合作用。抑制剂-酶结合是通过两种生物物理技术确定的-等温滴定量热法和热位移测定法。通过X射线晶体学测定共晶体结构。比较使用三种不同抑制和结合方法获得的结果,可以提高化合物亲和力排名的准确性,并可以确定化合物对特定碳酸酐酶同工型的抑制特异性。在大多数情况下,尽管使用了非常不同的方法来测量结合和抑制反应,但所有三种方法均产生了相同的结果。研究的某些化合物是亚型IX的亚微摩尔抑制剂,后者是重要的癌症靶标。

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