In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II
BIOORGANIC & MEDICINAL CHEMISTRY, vol.16, no.20, pp.9101-9105, 2008 (SCI-Expanded, Scopus)
- Publication Type: Article / Article
- Volume: 16 Issue: 20
- Publication Date: 2008
- Doi Number: 10.1016/j.bmc.2008.09.028
- Journal Name: BIOORGANIC & MEDICINAL CHEMISTRY
- Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Page Numbers: pp.9101-9105
- Erzincan Binali Yildirim University Affiliated: No
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. IC50 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 3.04 mu M, 3.38 mu M, 4.07 mu M, 7.64 mu M, 0.13 mM, 0.29 mM, 0.42 mM, 0.56 mM, 2.71 mM and 3.07 mM for hCA I and of 4.49 mu M, 2.70 mu M, 0.72 mu M, 2.80 mu M, 0.75 mM, 0.72 mM, 0.29 mM, 0.68 mM, 1.16 mM and 4.70 mM 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. (C) 2008 Elsevier Ltd. All rights reserved.