Profiling the disintegration of BRPs released by massive wasp stings using serratiopeptidase: An in-silico insight

Serratiopeptidase is 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 facilitate 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. To accomplish this objective, we docked selected BRPs onto the binding pocket of wild and previously identified mutant (N412D) of serratiopeptidase. Based on their docked scores, the 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 identical ΔG values when compared to the reference complex. Further, we condemned the external pulling forces on both peptides to observe the force needed in the disassociation process to endorse the binding affinity findings in terms of unbinding mechanism. This analysis suggested that BRP-7 (Wasp kinin PMM1) peptide was tightly anchored and laid out the highest pulling force to get detach from the active pocket of serratiopeptidase in contrast to the BRP-6 peptide. The current study endorses up the present findings and paves the way for serratiopeptidase to be used as an anti-angioedemic peptidase as well as a fixed-dose combination (FDC) in hypotensive drugs.