Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII

被引：31

作者：

Capkauskaite, Edita ^{[1
,2
]}

Baranauskiene, Lina ^{[1
]}

Golovenko, Dmitrij ^{[3
]}

Manakova, Elena ^{[3
]}

Grazulis, Saulius ^{[3
]}

Tumkevicius, Sigitas ^{[2
]}

Matulis, Daumantas ^{[1
]}

机构：

[1] Inst Biotechnol, Lab Biothermodynam & Drug Design, LT-02241 Vilnius, Lithuania

[2] Vilnius Univ, Fac Chem, Dept Organ Chem, LT-03225 Vilnius, Lithuania

[3] Inst Biotechnol, Lab Protein DNA Interact, LT-02241 Vilnius, Lithuania

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 2010年 / 18卷 / 21期

关键词：

Carbonic anhydrase isozymes I; II; VII; and XIII; Isothermal titration calorimetry; Thermal shift assay; ThermoFluor (R); Sulfonamides; X-ray crystallography; THERAPEUTIC APPLICATIONS; MODEL; 2-ALKYLBENZIMIDAZOLES; DERIVATIVES; DIURETICS; PROTEINS; AFFINITY;

D O I：

10.1016/j.bmc.2010.09.016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A series of novel 2-chloro-5-[(1-benzimidazolyl- and 2-benzimidazolylsulfanyl) acetyl] benzene-sulfonamides were designed and synthesized. Their binding to recombinant human carbonic anhydrase (hCA)isozymes I, II, VII, and XIII was determined by isothermal titration calorimetry and thermal shift assay. The designed S-alkylated benzimidazole derivatives exhibited stronger binding than the indapamide-like N-alkylated benzimidazoles, with the K-d reaching about 50-100 nM with drug-targeted hCAs VII and XIII. The cocrystal structures of selected compounds with hCA II were determined by X-ray crystallography, and structural features of the binding event were revealed. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：7357 / 7364

页数：8

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