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An increasing number of multidrug-resistant pathogens is a serious problem of modern medicine and new antibiotics are highly demanded. In this study, different n-alkyl acids (C 2 -C 14 ) and aromatic acids (benzoic and trans -cinnamic) were conjugated to the N -terminus of KR12 amide. The effect of this modification on antimicrobial activity (ESKAPE bacteria and biofilm of Staphylococcus aureus ) and cytotoxicity (human red blood cells and HaCaT cell line) was examined. The effect of lipophilic modifications on helicity was studied by CD spectroscopy, whereas peptide self-assembly was studied by surface tension measurements and NMR spectroscopy. As shown, conjugation of the KR12-NH 2 peptide with C 4 -C 14 fatty acid chains enhanced the antimicrobial activity with an optimum demonstrated by C 8 -KR12-NH 2 (MIC 1-4 μg/mL against ESKAPE strains; MBEC of S. aureus 4-16 μg/mL). Correlation between antimicrobial activity and self-assembly behavior of C 14 -KR12-NH 2 and C 8 -KR12-NH 2 has shown that the former self-assembled into larger aggregated structures, which reduced its antimicrobial activity. In conclusion, N -terminal modification can enhance antimicrobial activity of KR12-NH 2 ; however, at the same time, the cytotoxicity increases. It seems that the selectivity against pathogens over human cells can be achieved through conjugation of peptide N -terminus with appropriate n-alkyl fatty and aromatic acids.

Lipidated Analogs of the LL-37-Derived Peptide Fragment KR12—Structural Analysis, Surface-Active Properties and Antimicrobial Activity