In silico approach for therapeutic profiling and physiochemical findings of serratiopeptidase an anti-inflammatory enzyme

Abstract

Inflammation and inflammatory disorders are the leading cause of death and physical deformities worldwide. The management of inflammatory diseases entirely relies on mainly two classes of synthetic compounds i.e. non-steroidal anti-inflammatory drugs (NSAIDs) and steroidal drugs. Often these drugs are associated with several side effects and adverse drug reactions. To combat inflammation, more efficiently enzyme-based medications emerged in last once decade. Several serine proteases were studied and characterized as anti-inflammatory in nature. Serratiopeptidase was reported as one potent anti-inflammatory enzyme-based drug and employed in the management of acute inflammation. Though the enzyme has a long history as anti-inflammatory therapeutic presently in sports medicine, however the critical mechanism remains unknown entirely. The major challenge associated with the serratiopeptidase is lack of molecular mechanism. In this study, using in silico approaches, we have investigated structural and functional insights of serratiopeptidase associated with potent anti-inflammatory activity. The physicochemical properties were characterized to explore therapeutic potential. Secondary structure was predicted for stability of enzyme. Molecular modeling and docking studies were carried out to explore exact molecular mechanism. The different substrates were docked with the enzyme to investigate its affinity for its target. The affinity of enzyme with COX I (-458.36 kcal/mol), COX-II (- 486.24 kcal/mol) and LOX (-462.24 kcal/mol) was determined via docking analysis. The anti-inflammatory activity of serratiopeptidase was determined as function of RBC cell membrane lysis with reference to diclofenac sodium as a standard anti-inflammatory drug. We report here a high degree of RBC cell membrane lysis (70.5%) at higher concentration of serratiopeptidase (2.5mg/ml). © 2021 World Research Association. All rights reserved.