Fine‐tuning the antimicrobial activity of β‐hairpin peptides with fluorinated amino acids

Antimicrobial peptides (AMPs) possess bactericidal activity against a variety of pathogens depending on an overall balance positively charged and hydrophobic residues. Selective fluorination serves to fine-tune the intrinsic hydrophobicity that could improve AMP bioactivity without affecting sequence length. Only few studies have focused impact this unique element antimicrobial potency came somewhat contractionary results. Moreover, influence fluorinated amino acids peptide proteolysis is yet not fully understood. In work, we tackle link between side chain both proteolytic stability for two series amphiphilic β-hairpin peptides. particular, synergy was determined. All were found be barely hemolytic non-toxic. Most surprisingly, susceptible enzymatic degradation. Hence, distinctive properties these polyfluorinated AMPs will serve future design peptide-based drugs.