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There has been great interest in the development of extremely potent antibacterial lantibiotic peptides for medicinal use and in food preservation. Of central importance to this endeavor is a strong understanding of which parts of the peptides are required for activity and which parts are expendable. Nisin, lacticin 481, nukacin ISK-1, mersacidin, lacticin 3147 and haloduracin represent many different types of lantibiotic peptides. In recent years, considerable advances toward understanding the structure-activity relationship of each of these lantibiotic systems have been achieved. This review will focus on the individual systems and the valuable information obtained from the many mutants produced.

Fundamental functionality: recent developments in understanding the structure–activity relationships of lantibiotic peptides