In vitro and in vivo characterization of therapeutically effective serine protease inhibitor isolated from Momordica charantia L. | [Abstract Book on International Conference on Food and Applied Sciences (ICFAS-23) 3-5 August 23 • 2023]

Author(s):

1. Shagufta Kamal: Dept. of Biochemistry, GCU, Faisalabad, Pakistan

2. Naheed Akhter: Dept. of Botany, Division of S&T, University of Education, Lahore, Pakistan

3. Sadia Zafar: Dept. of Botany, Division of S&T, University of Education, Lahore, Pakistan

4. Saima Rehman: Dept. of Chemistry, GCU, Faisalabad, Pakistan

5. Ismat Bibi: Dept. of Chemistry, IUB, Bahawalpur, Pakistan

6. Kanwal Rehman: Dept. of Pharmacy, University of Agriculture, Faisalabad, Pakistan

Abstract:

In the present study, peptides were isolated from locally available and identified strain of Momordica charantia (Bitter gourd) to determine its serine protease inhibition potential. Three-step purification resulted in 11.8% purification fold. Newly isolated hexapeptide showed potent inhibition potential of serine protease. The alkaline protease inhibitory activity was found to be in the range of Ki = 0.13 ± 0.05 µM to 1.89±0.25 µM, IC50 = 0.048±0.85 to 0.68±0.15µM than interferons (0.08±0.005 µM) as peptides having carboxylate as a strong electron-withdrawing group was recorded as a most potent inhibitor of alkaline protease inhibitor while (%) inhibition against trypsin was ranging between 62.65±2.45 to 94.24±2.61. The kinetic study predicted that isolated peptides followed the uncompetitive and mixed type of inhibition against serine protease. In silico molecular docking of the most potent peptide (COP) was performed at the active site of the alkaline protease co-crystal structure (PDB ID:1NEN). The results of molecular docking approved the experimental findings. A primary indication of hepatic damage induced by CCl4 was obtained by the evaluation of hepatic enzymatic markers of injury such as ALP, AST and ALT. The levels of ALP, AST and ALT, 48 h after the administration of CCl4, were significantly elevated relative to the control group. These enzymes enter the circulatory system due to altered permeability of membranes and their increased levels reflected severe damage to the structural integrity of the liver. The administration of peptides significantly attenuated CCl4-induced elevation of AST and ALT, indicating its hepatoprotective activity.

Page(s): 146-146

DOI: DOI not available

Published: Journal: Abstract Book on International Conference on Food and Applied Sciences (ICFAS-23) 3-5 August 23, Volume: 0, Issue: 0, Year: 2023

Keywords:

molecular docking , Trypsin , Electron withdrawing group , uncompetitive and mixed Inhibition

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