Abstract
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. KI values of the molecules 2–9 were in the range of 10.025–892.109 μM for hCA I, 1.437–59.107 μM for hCA II and 11.143–919.182 μM for hCA VI, respectively. Reported inhibitory activities of molecules 2–9 will assist in better understanding of structure-activity relationship studies of CAI.
Acknowledgments
We are grateful to Prof. Dr. Claudiu T. Supuran, University of Florence, for various valuable studies on CAIs.
Declaration of interest
This study was financed by Turkish Republic Prime Ministry State Planning Organization (DPT), (project no: 2010K120440) and Agri Ibrahim Cecen University Scientific Research Council, (project no: Agri BAP-2010/K-10) for (MS) and by the Scientific and Technological Research Council of Turkey (TUBITAK, Grant No: TBAG-107T/348) for (SG, HTB and AM).