1. Synthesis, characterization andin vitroinhibition of metal complexes of pyrazole based sulfonamide on human erythrocyte carbonic anhydrase isozymes I and II
- Author
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Rahmi Kasımoğulları, Bülent Büyükkıdan, Nurgün Büyükkidan, Metin Bülbül, and Samet Mert
- Subjects
0301 basic medicine ,Carbonic Anhydrase I ,Erythrocytes ,Stereochemistry ,Carbonic anhydrase II ,metal complexes ,Pyrazole ,010402 general chemistry ,Carbonic Anhydrase II ,01 natural sciences ,Structure-Activity Relationship ,03 medical and health sciences ,chemistry.chemical_compound ,Metals, Heavy ,Carbonic anhydrase ,hydratase and esterase activities ,sulfonamide ,Drug Discovery ,Organometallic Compounds ,medicine ,Humans ,Structure–activity relationship ,Carbonic Anhydrase Inhibitors ,Pharmacology ,chemistry.chemical_classification ,Sulfonamides ,Dose-Response Relationship, Drug ,Molecular Structure ,biology ,Chemistry ,Ligand ,lcsh:RM1-950 ,General Medicine ,0104 chemical sciences ,Sulfonamide ,Isoenzymes ,pyrazole ,lcsh:Therapeutics. Pharmacology ,030104 developmental biology ,biology.protein ,Pyrazoles ,Acetazolamide ,Research Article ,medicine.drug - Abstract
Sulfonamides represent an important class of biologically active compounds. A sulfonamide possessing carbonic anhydrase (CA) inhibitory properties obtained from a pyrazole based sulfonamide, ethyl 1-(3-nitrophenyl)-5-phenyl-3-((5-sulfamoyl-1,3,4-thiadiazol-2-yl)carbamoyl)-1H-pyrazole-4-carboxylate (1), and its metal complexes with the Ni(II) for (2), Cu(II) for (3) and Zn(II) for (4) have been synthesized. The structures of metal complexes (2–4) were established on the basis of their elemental analysis, 1H NMR, IR, UV–Vis and MS spectral data. The inhibition of two human carbonic anhydrase (hCA, EC 4.2.1.1) isoenzymes I and II, with 1 and synthesized complexes (2–4) and acetazolamide (AAZ) as a control compound was investigated in vitro by using the hydratase and esterase assays. The complexes 2, 3 and 4 showed inhibition constant in the range 0.1460–0.3930 µM for hCA-I and 0.0740–0.0980 µM for hCA-II, and they had effective more inhibitory activity on hCA-I and hCA-II than corresponding free ligand 1 and than AAZ. © 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group., This work was supported by Scientific and Technological Research Council of Turkey (TUB€ İTAK) with Grant No. TBAG-104T406.
- Published
- 2017