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Evaluation of antibacterial activity of enterocin A-colicin E1 fusion peptide.

Hadis Fathizadeh, Mahmood Saffari, Davoud Esmaeili, Rezvan Moniri, Morteza Salimian

2020PubMed27 citationsDOIOpen Access PDF

Abstract

OBJECTIVES: Bacterial resistance to most common antibiotics is a harbinger of the requirement to find 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 E1 modified against pathogens. MATERIALS AND METHODS: (ATCC 33591). 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 E1 peptide can serve as an efficient antibacterial compound to treat or prevent bacterial infections.

Topics & Concepts

ColicinBacteriocinAntibacterial peptidePeptideFusionAntibacterial activityFusion proteinComputational biologyChemistryBiologyMicrobiologyBacteriaEscherichia coliGeneticsBiochemistryAntimicrobialGeneRecombinant DNAPhilosophyLinguisticsProbiotics and Fermented FoodsAntimicrobial Peptides and ActivitiesProtein Hydrolysis and Bioactive Peptides
Evaluation of antibacterial activity of enterocin A-colicin E1 fusion peptide. | Litcius