Fragments of cathelicidins PMAP-36 and BMAP-27 and their D-enantiomers: Effects of all D substitutions on structure, protease resistance and antimicrobial properties

This is the authors' abstract. We don't add key points for this paper.

= 0.7-0.8). These structural differences between the two peptides were found to influence their antimicrobial activity and mode of membrane permeabilization. Moreover, the D enantiomers of both analogues were resistant to proteolysis. All peptides showed a broad spectrum of antibacterial activity (main MIC range: 1-16 μM). Cytotoxicity studies in fibroblast showed that the peptides were non-cytotoxic at concentrations corresponding to their antibacterial activity. Overall, this study led to the identification of structurally interesting short peptides that could serve as prototypes for the development of effective and practical antibacterial drugs.