ArticleIranian biomedical journal2026
Design and Mode of Action of a New Synthetic Antibacterial Peptide against Pseudomonas aeruginosa.
Article in Iranian biomedical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: Research into antimicrobial peptides (AMPs) and other novel antimicrobial strategies continues to be a focus of the scientific community to address the growing challenges posed by antibiotic resistance. The aim of this study was the specific bioinformatic design of a novel hybrid AMP that combines the potent antibacterial properties of Temporins and Brevinin while minimizing its cytotoxic effects. Methods: The N-terminal of Brevinin peptides and the C-terminal of Temporin peptide were selected. To optimize the peptide, we replaced the amino acids at positions 1, 3, and 7 with glycine, lysine, and lysine, respectively. Various approaches were used to assess physicochemical characteristics, minimum inhibitory concentration (MIC), minimum bactericidal concentration (MBC), cytotoxicity, apoptosis, hemolytic activity, and reactive oxygen species generation. Results: The novel peptide had 57% hydrophobicity and four positive electric charges due to its lysine amino acid composition. The synthesized peptide exhibited MIC and MBC values of 80 µM against Pseudomonas aeruginosa. According to the MTT assay, the peptide showed neither cytotoxic nor hemolytic effects on human cells. The results of electron microscopy showed that this peptide can disrupt the integrity of P. aeruginosa membrane cells and induce morphological changes in their surface structure. Conclusion: This research suggests that the synthetic peptide could serve as a promising potential therapeutic agent to combat antibiotic-resistant strains of P. aeruginosa.
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