Synthesis, lighting of structures of sulfonamide drugs with biological activity and molecular doking works

Sulfonamides are known as one of the strongest inhibitors of carbonic anhydrase enzyme. Carbonic anhydrase enzyme plays a very important role in metabolism. Especially CA (II); It plays a target enzyme role in the treatment of important diseases such as ulcer, obesity, cancer, epilepsy and glaucoma. Therefore, CA inhibitors are important molecules in drug design. In this study, sulfonamide derivative Schiff bases and Cu (II) complexes were synthesized and their structures were elucidated. The carbonic anhydrase inhibition of the synthesized compounds was tested by looking at the esterase activity on hCA (II) isoenzymes. Among the compounds, Cu (L2)2 complex shows the highest inhibition effect against hCA II with 0.73 mM. In general, it has been observed that the complexes show a better inhibition effect against hCA II than the ligands. In order to determine the enzyme-compound interactions at the molecular level, a doking study was conducted using the Molegro Virtual Docker MVD 2019.7.0 program. In molecular docking studies for the hCA (II) enzyme, the binding energies of each inhibitor molecule to the active site of the enzyme were calculated. The energies obtained also support that the best interaction with the enzyme is realized by Cu(L2)2. In addition, according to the docking results, it has been observed that steric interactions and hydrogen bonds play an important role in the interaction between molecules and the active site of the enzyme.