Department of Organic Chemistry, Kaunas University of Technology, LT-50254, Radvilėnų pl. 19, Kaunas, Lithuania.
Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, Vilnius LT-10257, Lithuania.
Bioorg Med Chem. 2019 Jan 15;27(2):322-337. doi: 10.1016/j.bmc.2018.12.011. Epub 2018 Dec 6.
Two series of benzenesulfonamides bearing methyl groups at ortho/ortho or meta/ortho positions and a pyrrolidinone moiety at para position were synthesized and tested as inhibitors of the twelve catalytically active human carbonic anhydrase (CA) isoforms. Observed binding affinities were determined by fluorescent thermal shift assay and intrinsic binding affinities representing the binding of benzenesulfonamide anion to the Zn(II)-bound water form of CA were calculated. Introduction of dimethyl groups into benzenesulfonamide ring decreased the binding affinity to almost all CA isoforms, but gained in selectivity towards one CA isoform. A chloro group at the meta position of 2,6-dimethylbenzenesulfonamide derivatives did not influence the binding to CA I, but it increased the affinity to all other CAs, especially, CA VII and CA XIII (up to 500 fold). The compounds may be used for further development of CA inhibitors with higher selectivity to particular CA isoforms.
两个系列的苯磺酰胺化合物在对位或间位带有甲基取代基,在对位带有吡咯烷酮部分,被合成并测试作为十二种催化活性的人碳酸酐酶(CA)同工酶的抑制剂。通过荧光热位移分析测定观察到的结合亲和力,并计算代表苯磺酰胺阴离子与 CA 的 Zn(II)-结合水形式结合的固有结合亲和力。在苯磺酰胺环中引入二甲基团会降低对几乎所有 CA 同工酶的结合亲和力,但对一种 CA 同工酶的选择性增强。2,6-二甲基苯磺酰胺衍生物的间位的氯取代基不会影响与 CA I 的结合,但会增加对所有其他 CA 的亲和力,特别是 CA VII 和 CA XIII(高达 500 倍)。这些化合物可用于进一步开发对特定 CA 同工酶具有更高选择性的 CA 抑制剂。