Inhibition of human carbonic anhydrase isozymes I, II and VI with a series of bisphenol, methoxy and bromophenol compounds

被引:46
|
作者
Balaydin, Halis Turker [3 ]
Durdagi, Serdar [4 ]
Ekinci, Deniz [5 ]
Senturk, Murat [1 ]
Goksu, Suleyman [2 ]
Menzek, Abdullah [2 ]
机构
[1] Ibrahim Cecen Univ Agri, Fac Sci & Art, Dept Chem, Agri, Turkey
[2] Ataturk Univ, Dept Chem, Fac Sci, Erzurum, Turkey
[3] Artvin Coruh Univ, Fac Educ, Artvin, Turkey
[4] Univ Calgary, Dept Biol Sci, Inst Biocomplex & Informat, Calgary, AB T2N 1N4, Canada
[5] Ondokuz Mayis Univ, Dept Agr Biotechnol, Fac Agr, Samsun, Turkey
关键词
Carbonic anhydrase; molecular docking; bisphenol; bromophenol; hCA II; hCA VI; ERYTHROCYTE GLUTATHIONE-REDUCTASE; THERAPEUTIC APPLICATIONS; VITRO INHIBITION; METAL-COMPLEXES; SULFONAMIDES; PURIFICATION; THIOXOLONE; DRUGS;
D O I
10.3109/14756366.2011.596836
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Carbonic anhydrase inhibitors (CAI) are valuable molecules as they have several therapeutic applications, including anti-glaucoma activity. In this study, inhibition of three human carbonic anhydrase (hCA, EC 4.2.1.1) isozymes I, II and VI with a series of bisphenol and bromophenol derivatives was investigated. Molecular docking studies of a set of such inhibitors within CA I and II were also performed. K-I values of the molecules 2-9 were in the range of 10.025-892.109 mu M for hCA I, 1.437-59.107 mu M for hCA II and 11.143-919.182 mu M for hCA VI, respectively. Reported inhibitory activities of molecules 2-9 will assist in better understanding of structure-activity relationship studies of CAI.
引用
收藏
页码:467 / 475
页数:9
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