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Objective and design: Serratiopeptidase a multifaceted therapeutic enzyme renowned for its anti-inflammatory, analgesic, anti-biofilm, fibrinolytic and anti-edemic properties. It is vital to uncover more about the assets of such efficacious enzyme in order to facilitates their contribution in all health-related issues, notably inflammatory ailments. The current study sought to determine whether serratiopeptidase would disintegrate bradykinin related peptides (BRPs) from wasp venom in the same manner as it does with human bradykinin. Methods: To accomplish this objective, we used molecular modeling, docking, MD simulation, MMG/PBSA along with the SMD simulations. Results: We docked selected BRPs on to the binding pocket of wild and previously identified mutant (N412D) of serratiopeptidase. Based on their docked scores, top two BRPs were selected and their conformational behavior was analyzed employing molecular dynamics studies. Additionally, thermodynamics end-state energy analysis reported that both the complexes exhibited higher stability and analogous ∆G values when compared to the reference complex. Further, to understand the unbinding mechanism, we condemned external pulling force on both peptides and observed that BRP-7 peptide was tightly anchored and laid out the highest pulling force to get detach from the active pocket of serratiopeptidase. Conclusion: The current study endorses up the current findings and paves the way for serratiopeptidase to be used as an anti-angioedemic as well as fixed dose combination in hypotensive drugs.

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