ArticleBiomolecules2024
Enhancing Selective Antimicrobial and Antibiofilm Activities of Melittin through 6-Aminohexanoic Acid Substitution.
Article in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Multidimensional Modification and Functional Optimization of Melittin: From Natural Toxic Peptide to Safe and Effective Therapeutics.Pharmaceutics · 2026Review
- Design and Evaluation of the Antibacterial Peptide FK18: a Therapeutic Approach for Mastitis in Dairy Animals.Probiotics and antimicrobial proteins · 2026Article
- Rational design of thrombin-derived VFR12 analogs with enhanced antimicrobial, antibiofilm, and anti-inflammatory properties.Scientific reports · 2025Article
- Therapeutic Bioactivity Exerted by theMolecules (Basel, Switzerland) · 2025Article
- Expansion of the antibacterial spectrum of symmetrical amino acid-paired antifungal peptides through structural optimization.BMC microbiology · 2025Article
- Discovery of a Novel Antimicrobial Peptide fromAntibiotics (Basel, Switzerland) · 2025Article
- Antimicrobial Peptides: Mechanisms, Applications, and Therapeutic Potential.Infection and drug resistance · 2025Review
- Antibacterial and antibiofilm features ofHeliyon · 2024Article
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Authors and funding
4 authors.
Funding
Abstract
Leucine residues are commonly found in the hydrophobic face of antimicrobial peptides (AMPs) and are crucial for membrane permeabilization, leading to the cell death of invading pathogens. Melittin, which contains four leucine residues, demonstrates broad-spectrum antimicrobial properties but also significant cytotoxicity against mammalian cells. To enhance the cell selectivity of melittin, this study synthesized five analogs by replacing leucine with its structural isomer, 6-aminohexanoic acid. Among these analogs, Mel-LX3 exhibited potent antibacterial activity against both Gram-positive and Gram-negative bacteria. Importantly, Mel-LX3 displayed significantly reduced hemolytic and cytotoxic effects compared to melittin. Mechanistic studies, including membrane depolarization, SYTOX green uptake, FACScan analysis, and inner/outer membrane permeation assays, demonstrated that Mel-LX3 effectively permeabilized bacterial membranes similar to melittin. Notably, Mel-LX3 showed robust antibacterial activity against methicillin-resistant
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