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Eur J Med Chem ; 198: 112392, 2020 Jul 15.
Article in English | MEDLINE | ID: mdl-32388113

ABSTRACT

In this study, novel dithiocarbamate-sulfonamide derivatives (3a-3k) were synthesized to investigate their inhibitory activity on purified human carbonic anhydrase (hCA) I and II. The IC50 and Ki values of the compounds were calculated to compare their inhibition profiles on hCA I and II isoenzymes. Acetazolamide was used as the standard inhibitor in the enzyme inhibition assay. Compounds 3a, 3e, 3g, 3h, 3j and 3k showed notable inhibitory effects against hCA I and II. Among these compounds, compound 3h was found to be the most active derivate against both the hCA I and II enzymes with Ki values of 0.032 ± 0.001 µM and 0.013 ± 0.0005 µM, respectively. The cytotoxicity of compounds 3a, 3e, 3g, 3h, 3j and 3k toward NIH/3T3 (mouse embryonic fibroblast cell line) was observed and the compounds were found to be non-cytotoxic. Furthermore, molecular docking studies were performed to investigate the interaction types between compound 3h and the hCA I and II enzymes. As a result of this study a novel and potent class of CA inhibitors with good activity potential were identified.


Subject(s)
Carbonic Anhydrase II/antagonists & inhibitors , Carbonic Anhydrase I/antagonists & inhibitors , Carbonic Anhydrase Inhibitors/chemical synthesis , Sulfonamides/chemical synthesis , Thiocarbamates/chemistry , 3T3 Cells , Acetazolamide/chemistry , Acetazolamide/metabolism , Animals , Carbonic Anhydrase Inhibitors/metabolism , Catalytic Domain , Cations, Divalent/chemistry , Cell Survival/drug effects , Humans , Kinetics , Mice , Molecular Conformation , Molecular Docking Simulation , Structure-Activity Relationship , Sulfonamides/metabolism , Zinc/chemistry
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