Ribosomally synthesized antimicrobial peptides in prokaryotic and eukaryotic organisms

Abstract

Abstract Ribosomally synthesized antimicrobial peptides are found both in prokaryotes and eukaryotes. They possess a low molecular weight and are characterized by compact structures, thermal stability and potent antimicrobial activity. Their typical amphipathic character is responsible for their detergent‐like mode of action. Since these peptides are directly gene‐encoded, it is possible to modify their structure by mutagenesis to produce structure analogues with an expanded spectrum of antimicrobial activity. Furthermore, the production of these peptides in heterologous expression systems could enable yield improvement to make them accessible for industrial application and to reduce the processing costs by using optimized isolation procedures. They might be useful as effective natural food preservatives because of their chemical and physical properties.