Inhibition Effects of Lisinopril and Quinapril on The activity of Carbonic Anhydrase: in Vitro and Molecular Docking Studies | ||||
| Egyptian Journal of Chemistry | ||||
| Volume 65, Issue 132, December 2022, Page 281-289 PDF (1.54 MB) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/ejchem.2022.122405.5479 | ||||
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| Author | ||||
Mohammed S. M. Al-Tameemi 
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| Department of Chemistry, Faculty of Education, Al Iraqia University, Baghdad-Iraq | ||||
| Abstract | ||||
| α-Carbonic anhydrase family (α-CAs) exist in different body tissues and have an essential function in the physiology of cells. In this study, the possible inhibitory effects of Lisinopril and quinapril had investigated on the activities of CA I and II. CA I and II were purified from human erythrocytes using an affinity gel chromatography column (sepharose 4B-tyrosine –sulfanilamide). The purity of isozymes was analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).The esterase activity was determined spectrophotometrically at 348 nm using 4-nitrophenyl acetate as a substrate. The half concentration of inhibition (IC50) values had calculated from graphs from the relation between the %Activity and the concentration of drugs at micromolar (µM), also, Calculated the inhibition constant (Ki) and inhibition types via Lineweaver-Burk plots. Finally, Drugs were docked into proteins (CA I and II) using molecular operating environment software (MOE). Lisinopril showed better inhibition values (IC50 and Ki) against the CA I and II than quinapril. The results of this study may be significant in the drug development field for treating disorders related to abnormal activities of these isozymes. | ||||
| Keywords | ||||
| Carbonic anhydrase; CAI; CAII; Esterase activity; Lisinopril; Quinapril; Enzyme inhibition | ||||
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