melitten has been researched along with Keratitis* in 2 studies
2 other study(ies) available for melitten and Keratitis
Article | Year |
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Design of Heptad Repeat Amphiphiles Based on Database Filtering and Structure-Function Relationships to Combat Drug-Resistant Fungi and Biofilms.
Due to the emergence of reports of multidrug-resistant fungi, infections caused by multidrug-resistant fungi and biofilms are considered to be a global threat to human health due to the lack of effective broad-spectrum drugs. Here, we developed a series heptad repeat sequences based on an antimicrobial peptide database (APD) and structure-function relationships. Among the developed peptides, the target peptide ACR3 exhibited good activity against all fungi and bacteria tested, including fluconazole-resistant Topics: Amino Acid Sequence; Animals; Biocompatible Materials; Biofilms; Candida; Cell Wall; Drug Resistance, Bacterial; Drug Resistance, Fungal; Erythrocytes; Escherichia coli; Female; Hemolysis; Humans; Keratitis; Melitten; Membrane Potentials; Mice, Inbred C57BL; Microbial Sensitivity Tests; Ophthalmic Solutions; Peptides; Reactive Oxygen Species; Structure-Activity Relationship; Surface-Active Agents; Toxicity Tests | 2020 |
Rational Substitution of ε-Lysine for α-Lysine Enhances the Cell and Membrane Selectivity of Pore-Forming Melittin.
Here, we present a rational approach that enhances the membrane selectivity of a prolific pore-forming peptide, melittin, based on experimental observations that the cationic polymer, ε-polylysine, disrupts bacterial membranes with greater affinity over mammalian cells when compared to poly-l-lysine and poly-d-lysine. We systematically replaced three α-lysine residues in melittin with ε-lysine residues and identified key residues that are important for cytotoxicity. We then assessed the antimicrobial properties of the modified peptides which carry two or three ε-lysyl residues. Two modified melittin peptides displayed rapid bactericidal properties against antibiotic-resistant strains, low innate resistance development by pathogenic bacteria, remained nonimmunogenic for T lymphocytes, and increased bioavailability in tear fluids. In proof-of-concept Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Anti-Bacterial Agents; Antifungal Agents; Bacteria; Bees; Candida albicans; Cell Membrane; Cornea; Eye Infections, Bacterial; Female; Humans; Keratitis; Lysine; Melitten; Mice, Inbred C57BL; Microbial Sensitivity Tests; Proof of Concept Study; Rabbits; Unilamellar Liposomes | 2020 |