Effects of Acyl versus Aminoacyl Conjugation on the Properties of Antimicrobial Peptides

摘要: To investigate the importance of increased hydrophobicity at amino end antimicrobial peptides, a dermaseptin derivative was used as template for systematic acylation study. Through gradual increase acyl moiety chain length, monitored and further modulated by conversion to aminoacyl. The lengths derivatives correlated with in peptide's global stabilization its helical structure. effect on cytolytic properties, however, fluctuated different cells. Whereas gradually enhanced hemolysis human red blood cells antiprotozoan activity against Leishmania major, bacteria displayed more complex behavior. gram-positive organism Staphylococcus aureus most sensitive intermediate chains, while longer acyls led total loss activity. All were detrimental Escherichia coli, namely, but not solely, because peptide aggregation. Although aminoacyl behaved essentially similarly nonaminated acyls, they reduced hydrophobicity, consequently, long-chain all microorganisms (e.g., up 12-fold aminolauryl derivative) significantly less hemolytic than their counterparts. Acylation also bactericidal kinetics resistance plasma proteases. similarities differences upon MSI-78 LL37 are presented discussed. Overall, data suggest an approach that can be enhance potencies acylated short peptides preventing hydrophobic interactions lead self-assembly solution and, thus, inefficacy cell wall-containing target