Selective antibacterial peptides: a review on their polarity

Selective antibacterial peptides usually contain 10-45 amino acid residues, most of them have positive charge to fold into amphipathic conformations and the cecropin type of linear peptides without cysteine. These peptides are featured by having high toxicity to bacteria membrane, low toxicity to mammal cells and not adopting an α-helical structure in aqueous solution. The peptide-membrane interaction has been studied for decades but so far the mechanism ruling it is still unknown. The aim of this paper is to summarize existing information about the correlation between polarity profile and selective antibacterial activity.