Investigation of the effects of new carbonic anhydrase inhibitors on human erythrocyte carbonic anhydrase enzymes

Carbonic anhydrase enzyme (CA, E.C. 4.2.1.1) has a variety of catalytic activity and tissue distribution. It is encoded by eight known gene families with the α, β, γ, δ, ζ, η, θ and t-CA classes. The important reaction of living things is the metalloenzyme, which catalyzes the conversion of CO2 to HCO3- and H+, and contains Zn+2 ions in its active site. CA is in the form of a globular protein consisting of 260 amino acids. CA enzyme inhibitors are used in the treatment of various diseases such as epilepsy, tumors, blood pressure, glaucoma, obesity and Alzheimer's. In this study, it is aimed to investigate the inhibition effects of new CA inhibitors in vitro to contribute to the treatment of CA pathway diseases and to give an idea for new drug-enzyme systems to be developed. In this study, it was aimed to investigate the inhibitory effects of new CA inhibitors in vitro in order to contribute to the treatment of CA pathway diseases. In our study, hCA I and hCA II isoenzymes found in human erythrocytes were purified by affinity chromatography technique. Then, qualitative and quantitative protein determination was performed and the purity of CA isoenzymes was checked by SDS-PAGE. The effects of synthesized compounds 1-9 on the esterase activities of hCA I and hCA II isoenzymes were investigated. IC50 values and Ki values of compounds with inhibitory effect were determined. The Ki values of the compounds were found in the range of 0.117 – 27.641 μM for hCA I and in the range of 0.006 – 25.195 μM for hCA II.