| Autor: |
Abhithaj, J., Sharanya, C. S., Arun, K. G., Jayadevi Variyar, E., Sadasivan, C. |
| Zdroj: |
Journal of Biomolecular Structure and Dynamics; April 2024, Vol. 42 Issue: 6 p2957-2964, 8p |
| Abstrakt: |
AbstractSerine proteases are a class of hydrolytic enzymes involved in various physiological functions like digestion, coagulation, fibrinolysis and immunity. The present study evaluates the serine protease inhibitory potential of phytochemicals liquiritin and terpinen-4-ol present in the herb Glycyrrhiza glabraL. using trypsin as the model enzyme. In silicostudies showed that both the compounds have a significant binding affinity towards trypsin with a binding energy of −26.66 kcal/mol and −19.79 kcal/mol for liquiritin and terpinen-4-ol, respectively. Their binding affinity was confirmed through in vitroenzyme inhibition assays. The mode of inhibition was found to be uncompetitive. In order to explain the mode of inhibition, docking of the ligands to the enzyme-substrate complex was also done and binding energy was calculated after MD simulation. The energy values showed that the binding affinities of these compounds towards the enzyme substrate complex are more than that towards the enzyme alone. This explains the uncompetitive mode of inhibition.Communicated by Ramaswamy H. Sarma |
| Databáze: |
Supplemental Index |
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