MOLECULAR DOCKING STUDIES ON INTERACTIONS OF ANTIMICROBIAL PEPTIDES WITH BACTERIAL TARGETS
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Date
2023-02-03
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dustry. Many antibiotics have become susceptible to the bacterial pathogens like E coli and Salmonella. Finding new antibiotic alternatives is essential because antibiotic resistance brought on by misuse, particularly the growth of multi-drug resistant bacteria which poses a severe threat to human health. An efficient therapeutic approach must be developed immediately to control infections. AMPs have become powerful alternative agents that have met the need for novel anti-infectives to overcome increasing antibiotic resistance problems. The present work conducted protein-peptide docking by using Autodock Vina with the list of 10 screened AMPs against the poultry bacterial targets (PBP 6 and LptA proteins) and by using Discovery Studio which revealed different binding interaction with target proteins. The original unmodified AMP (AP00551) and the modified AMP (FFHLHFHYWWW) showed favourable interactions with highest binding affinity of -8.7 Kcal/mol and-8.6 Kcal/mol with penicillin binding protein of E coli. For Salmonella the original unmodified AMP (AP00551) and the modified AMP (FFHLHFHYWWW) showed favourable interactions with highest binding affinity of -9.4 Kcal/mol and -9.0 Kcal/mol with LptA protein. Molecular docking studies indicated that these peptides could be used to block PBP 6 which is responsible for cell morphology development of E coli and the LptA enzyme which is responsible for membrane synthesis of Salmonella. Based on the binding energy score, the 10 AMPs could serve as a therapeutic option against the bacterial targets and enhance its treatment outcome.
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