In Silico Molecular Analysis and Docking of Potent Antimicrobial Peptides Against MurE Enzyme of Methicillin Resistant Staphylococcus Aureus

During the last decade there has been an alarming increase in the appearance of antibiotic-resistant bacteria. The drug-resistant microorganisms dubbed superbugs are projected to kill 10 million people a year by 2050. The annual frequency of deaths from Methicillin-resistant Staphylococcus aureus (MRSA) is rapidly increasing and surpassing those caused by human immunodeficiency virus/acquired immune deficiency syndrome (HIV/AIDS). Muramyl ligase E (MurE), an enzyme involved in the peptidoglycan biosynthesis of the bacterial cell wall, is a highly druggable target in MRSA. Six anti Methicillin-resistant Staphylococcus Aureus peptides were selected for deep bioinformatic analysis. The six anti-Methicillin-resistant Staphylococcus Aureus peptides were modeled and then docked to MurE ligase and their binding interactions were studied. The findings suggested that the interactions of three antimicrobial peptides (Flowlicidin-2, Ostricacin-2 and Ostricacin-3) with MurE could be essential for their inhibitory activity.