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Effect of Acylation on the Antimicrobial Activity of Temporin B Analogues

2018; Wiley; Volume: 13; Issue: 15 Linguagem: Inglês

10.1002/cmdc.201800289

1860-7187

Concetta Avitabile, Luca Domenico D’Andrea, Elisabetta D’Aversa, Roberta Milani, Roberto Gambari, Alessandra Romanelli,

Biochemical and Structural Characterization

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