Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Vilnius University, Graičiūno 8, Vilnius LT-02241, Lithuania.
Bioorg Med Chem. 2013 Nov 15;21(22):6937-47. doi: 10.1016/j.bmc.2013.09.029. Epub 2013 Sep 20.
Two groups of benzenesulfonamide derivatives, bearing pyrimidine moieties, were designed and synthesized as inhibitors of carbonic anhydrases (CA). Their binding affinities to six recombinant human CA isoforms I, II, VI, VII, XII, and XIII were determined by the thermal shift assay (TSA). The binding of several inhibitors was measured by isothermal titration calorimetry (ITC). Direct demonstration of compound inhibition was achieved by determining the inhibition constant by stopped-flow CO2 hydration assay. The most potent compounds demonstrated selectivity towards isoform I and affinities of 0.5 nM. The crystal structures of selected compounds in complex with CA II, XII, and XIII were determined to atomic resolution. Compounds described here were compared with previously published pyrimidinebenzenesulfonamides.(1) Systematic structure-activity analysis of 40 compound interactions with six isoforms yields clues for the design of compounds with greater affinities and selectivities towards target CA isoforms.
两组苯磺酰胺衍生物,带有嘧啶部分,被设计并合成作为碳酸酐酶(CA)的抑制剂。它们对六种重组人 CA 同工酶 I、II、VI、VII、XII 和 XIII 的结合亲和力通过热位移测定法(TSA)确定。通过等温滴定量热法(ITC)测量了几种抑制剂的结合。通过停止流动 CO2 水合测定法确定抑制常数直接证明了化合物的抑制作用。最有效的化合物对同工酶 I 具有选择性,亲和力为 0.5 nM。选择的化合物与 CA II、XII 和 XIII 的复合物的晶体结构被确定到原子分辨率。本文中描述的化合物与以前发表的嘧啶苯磺酰胺进行了比较。(1)对 40 种化合物与 6 种同工酶相互作用的系统结构-活性分析为设计对靶标 CA 同工酶具有更高亲和力和选择性的化合物提供了线索。