Evaluation of antibacterial activity of enterocin A-colicin E۱ fusion peptide

Background and Aim : Bacterial resistance to most common antibiotics is a harbinger of the requirement to detect novel anti-infective, antimicrobials agents, and increase innovative strategies to struggle them. Numerous bacteria produce small peptides with antimicrobial activities called bacteriocin. This study aimed to investigate the antibacterial properties of the fusion protein of Enterocin A and Colicin E۱ modified against pathogens.Methods : Analysis of recombinant bacteriocin Enterocin A and Colicin E۱ (ent A-col E۱) was done to assay the stability and antibacterial activity of this fusion protein. The pET-۲۲b vector was employed to express the coding sequence of the ent A-col E۱ peptide in E. coli BL۲۱ (DE۳). Minimum inhibitory concentration (MIC), disk diffusion, and time-kill tests were performed to evaluate the antibacterial activity of the ent A-col E۱ against Pseudomonas aeruginosa (ATCC ۹۰۲۷), Escherichia coli (ATCC ۱۰۵۳۶), Enterococcus faecalis (ATCC ۲۹۲۱۲), and Staphylococcus aureus (ATCC ۳۳۵۹۱).Results : The suggested recombinant peptide had good antibacterial activity against both Gram-negative and Gram-positive pathogens. It has also good stability at various temperatures, pH levels, and salt concentrations.Conclusion : Because bacteriocins are harmless compounds, they can be recommended as therapeutic or preventive supplements to control pathogens. According to the obtained results, the ent A-col E۱ peptide can serve as an efficient antibacterial compound to treat or prevent bacterial infections.

کلیدواژه ها:

Bacteriocins ، Fusion peptide ، Enterocin A ، Colicin E۱ ، Antibacterial activity