ABSTRACT
One alternative strategy is based on antimicrobial peptides (AMPs), eector molecules of innate immunity that provide a rst line of defense against a substantial array of pathogenic microorganisms (Hancock 2001; Zaslo 2002). Currently, more than 2500 natural and synthetic AMPs are listed in the Antimicrobial Peptide Database (https://aps. unmc.edu/AP) (Wang et al. 2009). In contrast to conventional antibiotics, these cationic amphipathic peptides composed of 10-40 amino acid residues predominantly act without specic receptors, but interfere with the lipid matrix of bacterial cell membranes (Lohner and Blondelle 2005). ere is consensus that the positive charge of the peptide is essential for initial binding to the negatively charged bacterial membrane surface, which allows discrimination between bacterial and host cell membranes, and its hydrophobicity is needed for insertion into and disruption of the membrane (e.g., Henderson and Lee 2013; Lohner and Blondelle 2005). ese two parameters determine the window of activity (Findlay et al. 2010). us, presumably, the amphipathic topology of AMPs, that is, their physicochemical properties rather than a specic amino acid sequence, is responsible for their biological activities.
