Abstract
The utilization of fluorinated amino acids in antimicrobial peptides (AMPs) is suggested as an effective approach to enhance membrane permeability and, thus, strengthen the non‐specific AMP targeting onto the bacterial envelope. Koksch and co‐workers report on the influence of aliphatic side chain fluorination on the antimicrobial activities of artificial β‐hairpin peptides. Among this work, the AMP SAJO‐PfpGly (“AMP OF THE MONTH”) equipped with two pentafluoro‐alkylated residues was identified as the most potent agent, while owning near to zero values of blood cell hemolysis and cytotoxicity. Its enzyme‐degradability despite the degree of fluorine‐substitution underlines the tremendous perspective tailor‐made fluorinated amino acids bear as orthogonal tool in modern peptide engineering. (doi: 10.1002/pep2.24306) image
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