Effect of acylation on the antimicrobial activity of temporin B analogues

New peptides derived from the natural antimicrobial temporin B were obtained. The design, the antimicrobial activity as well as the characterization of the secondary structure of peptides in the presence of bacterial cells is here described. We identified TB_KKG6K (KKLLPIVKNLLKSLL) as the most active analogue against Gram-positive and Gram-negative bacteria as compared to natural temporin B (LLPIVGNLLKSLL) and TB_KKG6A (KKLLPIVANLLKSLL). Acylation with hydrophobic moieties led generally to reduced activity, however, acylation at position 6 of TB_KKG6K led to retained submicromolar activity against Staphylococcus epidermidis.