In silico Analysis of Molecules for the Inhibition of Trypsin, and its Inhibition Assay using Trilobatin

Trypsin is a serine protease enzyme that has a wide range of functions in physiological and pathological processes. Although most of its functions are often associated with positive effects, there is still a need for its inhibition, because its overexpression has been associated with various forms of cancers and poses to be fatal if left unaddressed. Early detection of elevated trypsin levels can help diagnose cancer, and its inhibition can prevent its progression. Therefore, Molecular Docking was performed for four compounds, allantoin, barbituric acid, azoindole, and trilobatin, to test their inhibition potential against human trypsin. The binding affinities and the interacting residues were predicted using AutoDock. Azoindole, out of the four compounds, showed the highest binding affinity, followed by trilobatin. Moreover, the trypsin inhibition assay was performed using trilobatin as the inhibitor. A constant concentration of trypsin was maintained at 0.013mg/mL. To assess the use of trilobatin as a drug, SwissADME was employed. Its use as a potential oral drug was discovered.