Synthetic Antimicrobial Peptides: III—Effect of Cationic Groups of Lysine, Arginine, and Histidine on Antimicrobial Activity of Peptides with a Linear Type of Amphipathicity

Abstract We have studied the antimicrobial and hemolytic activity of synthetic peptides (SAMPs), i.e., Arg 9 Phe 2 ( P1 -Arg), Lys P2 -Lys), His P3 -His), which a “linear” type amphipathicity contain cationic amino acid residues arginine, lysine, or histidine. In this study, we used various pathogenic microorganism strains gram-negative bacteria Pseudomonas aeruginosa , Escherichia coli, Salmonella enterica ) gram-positive Staphylococcus aureus ), conditionally yeast fungus Candida albicans . It has been shown that replacement arginine by lysine histidine in tested SAMPs significantly degrades their antibacterial properties series: -Arg > -Lys $$ \gg -His. The analog SAMP, -Arg, highest (MIC 50 = 43–76 ?M), while peptide -His does not exhibit 100 ?M). were 6–10 times more active against opportunistic C. 6.7 10.9 ?M, respectively) 100-times increased antimycotic 0.6 ?M) compared with effect on bacterial cells. All linear low hydrophobicity, -Lys, -His, only two regardless presence acids (Arg, Lys, His) relatively (not than 4% hemolysis at 1000 ?M concentration). Thus, considering same synthesis efficiency (56–63%) approximately toxicity amphipathicity, it is recommended to use those create antifungal agents, respectively.