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Abstract
Serine 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 glabra L. using trypsin as the model enzyme. In silico studies 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 vitro enzyme 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
Acknowledgments
The authors acknowledge Inter University Centre for Bioscience and Bioinformatics Infrastructure Facility at the Department of Biotechnology and Microbiology, Dr. Janaki Ammal Campus, Kannur University supported by Department of Biotechnology (DBT), Government of India, for computational facilities. Abhithaj J acknowledges the Indian Council for Medical Research (ICMR), New Delhi, India, for research fellowship (ICMR-RA). Sharanya CS acknowledges Rajagiri College of Social Sciences for the financial support. Arun KG acknowledges the Inter University Centre for Bioscience for the Junior Research Fellowship.
Disclosure statement
The authors declare no conflicts of interest.