In vitro Inhibition Profiles and Molecular Docking Analysis of Benzohy-drazide Derivatives on Red Blood Cell Carbonic Anhydrases Isozymes

© 2022 Bentham Science Publishers.Background: Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes that contain zinc ions on the active side and convert carbon dioxide to bicarbonate in metabolism. Human CA-I and CA-II, which are the most abundant CA isozymes in erythrocytes, have been therapeutic targets in the treatment of glaucoma, hypertension, ulcer, osteoporosis, and, neurological disorders. Ben-zohydrazides are biologically active compounds, and their various pharmacological effects have been reported. Aim: In light of this, the objective of this study was to investigate the in vitro effects of benzohy-drazide derivatives on the activities of hCA-I and hCA-II, determine the compounds as selective in-hibitors for these isoenzymes, and estimate the inhibition mechanism through molecular docking studies. Methods: In this work, we synthesized the 10 different derivatives of benzohydrazide containing various functional group of different positions. Results: As a result, all benzohydrazide derivatives inhibited both isozymes in vitro and 2-amino 3-nitro benzohydrazide (10) was found to be the most efficient inhibitor of both hCA isozymes with the IC50 values of 0.030 and 0.047 μM, respectively. In the molecular docking studies, 3-amino 2-methyl benzohydrazide (3) had the lowest estimated free binding energies against hCA isozymes as-6.43 and-6.13 kcal/mol. Conclusion: In this study, hCA-I & II isozymes were isolate from human erythrocytes. CA iso-zymes are one of these target enzymes. WBC hope that the benzohydrazide derivatives, can guide remedies targeting carbonic anhydrase.