| Title | In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II. | | Author(s) | Bayram E, Senturk M, Irfan Kufrevioglu O, Supuran CT | | Institution | Ataturk University, Arts and Science Faculty, Department of Chemistry, Erzurum, Turkey. | | Source | Bioorg Med Chem 2008 Sep 13. | | Abstract | The inhibition of two human cytosolic carbonic anhydrase (hCA, EC 4.2.1.1) isozymes, hCA I and II, with a series of salicylic acid derivatives was investigated by using the esterase method with 4-nitrophenyl acetate as substrate. IC(50) values for sulfasalazine, diflunisal, 5-chlorosalicylic acid, dinitrosalicylic acid, 4-aminosalicylic acid, 4-sulfosalicylic acid, 5-sulfosalicylic acid, salicylic acid, acetylsalicylic acid (aspirin) and 3-metylsalicylic acid were of 3.04muM, 3.38muM, 4.07muM, 7.64muM, 0.13mM, 0.29mM, 0.42mM, 0.56mM, 2.71mM and 3.07mM for hCA I and of 4.49muM, 2.70muM, 0.72muM, 2.80muM, 0.75mM, 0.72mM, 0.29mM, 0.68mM, 1.16mM and 4.70mM for hCA II, respectively. Lineweaver-Burk plots were also used for the determination of the inhibition mechanism of these substituted phenols, most of which were noncompetitive inhibitors with this substrate. Some salicylic acid derivatives investigated here showed effective hCA I and II inhibitory activity, and might be used as leads for generating enzyme inhibitors eventually targeting other isoforms which have not been assayed yet for their interactions with such agents. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 18819808 |
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