ArticleFrontiers in chemistry2025
Engineering of antimicrobial peptide Brevinin-1pl: arginine, lysine, and histidine substitutions enhance antimicrobial-anticancer efficacy with reduced cytotoxicity.
Article in Frontiers in chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Arginine-substituted Mastoparan-C derivatives combat dual bacterial pathogens:Microbiology spectrum · 2026Article
- A comprehensive review of AI innovations for tackling antimicrobial resistance.Le infezioni in medicina · 2026Review
- Microbial communities and metabolome profiles of fermented Chinese mustard greens from diverse regions in Guangdong province, China.Frontiers in microbiology · 2026Article
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10 authors.
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Abstract
Introduction: Antimicrobial peptides (AMPs) are promising candidates for combating multidrug-resistant infections, but their clinical application is often limited by challenges such as poor selectivity and high cytotoxicity. This study aimed to optimize the therapeutic potential of brevinin-1pl, a frog-derived AMP with broad-spectrum antimicrobial and anticancer activities. Methods: Major experimental approaches encompassed antibacterial activity evaluation, hemolytic potential assessment, bactericidal rate determination via time-kill kinetics, SYTOX Green-based membrane integrity analysis, and MTT assays for anti-proliferative effects. Results: Substitutions with arginine (brevinin-1pl-2R and brevinin-1pl-5R) enhanced activity against Gram-positive bacteria but reduced efficacy against Gram-negative strains. Lysine substitution (brevinin-1pl-6K) decreased activity against Gram-positive bacteria due to reduced hydrophobicity. In contrast, histidine substitution (brevinin-1pl-3H) showed diminished activity against Gram-negative bacteria (e.g., MRSA MIC increased from 2 µM to 4 µM) but reduced hemolysis, indicating improved selectivity. Mechanistic studies using SYTOX green assays confirmed membrane disruption as a primary mode of action, while suggesting alternative mechanisms for Gram-positive Conclusion: These findings demonstrate that strategic amino acid substitutions can optimize the therapeutic potential of AMPs, offering a promising approach to develop peptides with enhanced efficacy and reduced clinical side effects.
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