title: Investigation of the Effect of Some Optically Active Imine Compounds on the Enzyme Activities of hCA-I and hCA-II under In Vitro Conditions: An Experimental and Theoretical Study.
abstract: Inhibitors of carbonic anhydrase (hCA; EC 4.2.1.1) are used as medicines for many diseases. Therefore, they are very important. In this study, a known series of Schiff bases were synthesized and their effects on the activities of hCA-I and hCA-II, which are cytosolic isoenzymes of carbonic anhydrase, were investigated under in vitro conditions. The synthesized compounds (H1, H2, H3, and H4) were found to cause inhibition on enzyme activities of hCA-1 and hCA-II. IC50 values of H1, H2, H3, and H4 compounds were 140, 88, 201, and 271 μM for hCA-I enzyme activity and 134, 251, 79, and 604 μM for hCA-II enzyme activity, respectively. The synthesized Schiff bases were characterized by several methods, including (1) H NMR, FT-IR, elemental analysis, and polarimetric measurements. Correlation coefficient square values (R(2) ) of comparison of the theoretical and experimental (1) H NMR shifts for H1, H2, H3, and H4 compounds were found as 0.9781, 0.9814, 0.9758, and 0.8635, respectively.
authors.affiliation: Department of Chemistry, Faculty of Arts and Sciences, Siirt University, 56100, Siirt, Turkey. hacibaykara@gmail.com.
authors.forename: Osman
authors.initials: O
authors.lastname: Tektas
authors.affiliation: Faculty of Engineering and Architecture, Food Engineering, Siirt University, 56100, Siirt, Turkey. eakkemik@siirt.edu.tr.
authors.forename: Ebru
authors.initials: E
authors.lastname: Akkemik
authors.affiliation: Department of Chemistry, Faculty of Arts and Sciences, Siirt University, 56100, Siirt, Turkey.|Center of Nanotechnology Research and Development (CIDNA), Facultad de Ingeniería Mecánica y Ciencias de la Producción, Escuela Superior Politécnica del Litoral, ESPOL, Campus Gustavo Galindo Km 30.5 Vía Perimetral, Guayaquil, Ecuador.
authors.forename: Haci
authors.initials: H
authors.lastname: Baykara
mesh_terms: D024401:Carbonic Anhydrase I / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000302:isolation & purification; D024402:Carbonic Anhydrase II / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000302:isolation & purification; D002257:Carbonic Anhydrase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry*; D057075:Enzyme Assays; D004912:Erythrocytes / Q000737:chemistry / Q000201:enzymology; D006801:Humans; D007097:Imines / Q000138:chemical synthesis / Q000737:chemistry*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D012545:Schiff Bases / Q000138:chemical synthesis / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013329:Structure-Activity Relationship
chemical_list: D002257:Carbonic Anhydrase Inhibitors; D007097:Imines; D012545:Schiff Bases; D024401:Carbonic Anhydrase I; D024402:Carbonic Anhydrase II
keywords: Carbonic Anhydrase; Chirality; DFT; Inhibition; Theoretical NMR