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.
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Zouhir, A., Jemli, S., Omrani, R. et al. In Silico Molecular Analysis and Docking of Potent Antimicrobial Peptides Against MurE Enzyme of Methicillin Resistant Staphylococcus Aureus. Int J Pept Res Ther 27, 1253–1263 (2021). https://doi.org/10.1007/s10989-021-10165-4
- Methicillin‐resistant Staphylococcus Aureus (MRSA)
- AntiMRSA peptides
- Molecular modeling
- Molecular docking
- Muramyl ligase E (MurE)
- Antimicrobial peptides