Design, synthesis and biological activity studies of new carbonic anhydrase inhibitors

Carbonic anhydrase (CA) enzymes are a common catalytic enzyme in many organisms. Vertebrates and invertebrates have different isoforms. 16 different isozymes of the α-CA isoform found in vertebrates have been identified so far. The main task of this enzyme is to catalyze the reversible conversion of carbon dioxide into bicarbonate and hydrogen ions in the body. It is widely distributed in many organs and tissues. They are involved in important physiologicalprocesses such as pH and CO2homeostasis, biosynthetic reactions such as gluconeogenesis, lipogenesis, ureogenesis, bone resorption, calcification, tumorigenicity, and electrolyte secretion.As a result of the researches, it has been determined that the most effective inhibitor of the carbonic anhydrase enzyme is sulfonamides. The R group in the general molecular structure of R-SO2-NH2generally consists of aromatic or heteroaromatic ring systems. The sulfonamides interact strongly with the Zn+2ion in the active site of the enzyme. In this study; 10 sulfonamide derivative compounds were synthesized. Analysis of the obtained compounds; 1H-NMR, 13C-NMR and Mass spectroscopic methods are illuminated by the analysis findings. The inhibition effect of the obtained compounds on the carbonic anhydrase enzyme was investigated.For the selected compounds, docking studies were performed and the enzyme active site and binding points were determined. It was revealed that the strongest interaction with CA enzyme active sites was observed with the 2e coded compound.