Recent studies on the mode of action have revealed exciting features of multiple activities of nisin and related lantibiotics making these peptides interesting model systems for the design of new antibiotics (Molec. Microbiol. 30 (1998) 317; Science 286 (1999) 2361; J. Biol. Chem. 276 (2001) 1772.). In contrast to other groups of antibiotic peptides, the lantibiotics display a substantial degree of specificity for particular components of bacterial membranes. Mersacidin and actagardine were shown to bind with high affinity to the lipid coupled peptidoglycan precursor, the so-called lipid II, which prevents the polymerisation of the cell wall monomers into a functional murein sacculus. The lantibiotics nisin and epidermin also bind tightly to this cell wall precursor; however, for these lantibiotics the binding of lipid II has two consequences. Like with mersacidin blocking of lipid II inhibits peptidoglycan biosynthesis; in addition, lipid II is used as a specific docking molecule for the formation of pores. This combination of lethal effects explains the potency of these peptides, which are active in nanomolar concentration. Other type-A lantibiotics are believed to also use docking molecules for pore formation, although identification of such membrane components has not yet been achieved.