Target Identification of Bio-Inhibitor Against Mycobacterium Tuberculosis by Subtractive Proteomics Approach

The success of any particular enzyme inhibition depends heavily on target identification, which is a critical step in the inhibitor discovery and development process. In the current study, the subtractive proteomics approach was used to identify potential targets against Mycobacterium tuberculosis H37Rv. Various database and tools were used for an essential nonhomologous cytoplasmic enzyme in unique metabolic pathways identification. Only 173 proteins were identified as essential nonhomologous proteins in unique pathways. Eventually, an isocitrate lyase was selected as a potential target for further molecular docking of natural product obtained from NPASS database. Four natural products were the potential candidates based on their binding energy in ranged of −5.09 to −6.92 kcal/mol. Metadynamic simulations also confirmed the binding stability of aconitic acid in isocitrate lyase. Thus, this study gives a platform for target identification that is potentially rapid and costly. Even the most promising results from computational studies should be validated through further wet-lab study before application.