Synthesis, characterization and in vitro inhibition of metal complexes of pyrazole based sulfonamide on human erythrocyte carbonic anhydrase isozymes I and II.

Autor: Büyükkıdan N; a Department of Chemistry , Arts and Science Faculty, Dumlupinar University , Kutahya , Turkey., Büyükkıdan B; a Department of Chemistry , Arts and Science Faculty, Dumlupinar University , Kutahya , Turkey., Bülbül M; a Department of Chemistry , Arts and Science Faculty, Dumlupinar University , Kutahya , Turkey., Kasımoğulları R; a Department of Chemistry , Arts and Science Faculty, Dumlupinar University , Kutahya , Turkey., Mert S; a Department of Chemistry , Arts and Science Faculty, Dumlupinar University , Kutahya , Turkey.
Jazyk: angličtina
Zdroj: Journal of enzyme inhibition and medicinal chemistry [J Enzyme Inhib Med Chem] 2017 Dec; Vol. 32 (1), pp. 208-213.
DOI: 10.1080/14756366.2016.1247056
Abstrakt: 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, 1 H 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.
Databáze: MEDLINE
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