forapin has been researched along with Keratitis* in 2 studies
2 other study(ies) available for forapin and Keratitis
| Article | Year |
|---|---|
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 |
Rational Design of Short Peptide Variants by Using Kunitzin-RE, an Amphibian-Derived Bioactivity Peptide, for Acquired Potent Broad-Spectrum Antimicrobial and Improved Therapeutic Potential of Commensalism Coinfection of Pathogens.
Commensalism coinfection of pathogens has seriously jeopardized human health. Currently, Kunitzin-RE, as an amphibian-derived bioactivity peptide, is regarded as a potential antimicrobial candidate. However, its antimicrobial properties were unsatisfactory. In this study, a set of shortened variants of Kunitzin-RE was developed by the interception of a peptide fragment and single-site mutation to investigate the effect of chain length, positive charge, hydrophobicity, amphipathicity, and secondary structure on antimicrobial properties. Among them, W8 (AARIILRWRFR) significantly broadened the antimicrobial spectrum and showed the highest antimicrobial activity (GM Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Antifungal Agents; Antimicrobial Cationic Peptides; Candida albicans; Cell Membrane; Cell Membrane Permeability; Coinfection; Drug Design; Escherichia coli; Eye Infections, Fungal; Keratitis; Mice; Microbial Sensitivity Tests; Protein Conformation, alpha-Helical; Protein Engineering; RAW 264.7 Cells; Salmonella typhimurium; Staphylococcus aureus | 2019 |