Development of novel antimicrobial peptides

Antimicrobial peptides (AMPs) are evolutionarily conserved main effector molecules of the innate immune system of many organisms. Due to their wide-range of activities and low potential to develop resistance against them, AMPs offer ideal templates to design novel peptide-based antimicrobial agents that can effectively control drug-resistance pathogens. In this study, novel AMPs were designed based on the unique Trp-rich domain (TRD) of a wheat endosperm protein, puroindoline A (PINA) with improved activity and biocompatibility properties. The potency, efficacy and specificity of the designed peptides to microbial cells, including persistent pathogens such as bacterial biofilms and endospores, as well as their lack of haemolytic and toxicity activities toward mammalian cells indicates these peptides, which originate from a most common edible source (wheat), could be highly valuable in pharmaceutical, food and/or agriculture industries. Another dimension of this study was to investigate the mechanism of action of these PIN-based peptides at cellular and intracellular levels to properly exploit their use as novel and efficient antimicrobial agents.