Screened pathogens, S. enterica serovar Typhimurium C610, E. coli D31, A. salmonicida A449, Y. ruckeri 96-4, and L. anguillarum 02-11 were found to be highly sensitive to myxinidin at the MBC of 1.0-2.5 ug/mL; S. epidermis C621 and yeast (C. albicans C627) had an MBC of 10.0 microg/mL. Also active against E. coli, K. pneumobiae, P. aeruginosa, and S. typhimurium. The antimicrobial activity of myxinidin was found to be two to 16 times more active than a potent fish-derived antimicrobial peptide, pleurocidin (NRC-17), against most of the screened pathogens. (Salt-insensitive) The microbicidal activity of myxinidin was retained in the presence of sodium chloride (NaCl) at concentrations up to 0.3 M and had no hemolytic activity against mammalian red blood cells. These results suggest that myxinidin may have potential applications in fish and human therapeutics. 3D structure has been determined by NMR spectroscopy. In 50% TFE, the peptide has a helical structure (residues 2-8) with the C-terminal 4 residues GKPS disordered (Cantisani M et al., 2014). Optimized antibacterial activity was obtained by adding a tryptophan residue at the N terminus and by the simultaneous substitution of residues present in positions 3, 4, and 11 with arginine. Update 12/2014. Myxinidin has Antibacterial, Antifungal activity. Myxinidin was found in Epidermal mucus, Myxine glutinosa L..
Lombardi L, Shi Y, Falanga A, Galdiero E, de Alteriis E, Franci G, Chourpa I, Azevedo HS, Galdiero S. Enhancing the Potency of Antimicrobial Peptides through Molecular Engineering and Self-Assembly. Biomacromolecules. 2019 Mar 11;20(3):1362-1374.