title: Lipid II-mediated pore formation by the peptide antibiotic nisin: a black lipid membrane study.
abstract: The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.
authors.affiliation: Institut für Medizinische Mikrobiologie und Immunologie der Universität Bonn, D-53105 Bonn, Germany. imke.wiedemann@ukb.uni-bonn.de
authors.forename: Imke
authors.initials: I
authors.lastname: Wiedemann
authors.forename: Roland
authors.initials: R
authors.lastname: Benz
authors.forename: Hans-Georg
authors.initials: HG
authors.lastname: Sahl
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects*; D008564:Membrane Potentials / Q000187:drug effects; D009561:Nisin / Q000494:pharmacology*; D014538:Uridine Diphosphate N-Acetylmuramic Acid / Q000031:analogs & derivatives* / Q000502:physiology*
chemical_list: D000900:Anti-Bacterial Agents; D014538:Uridine Diphosphate N-Acetylmuramic Acid; C069249:muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol; D009561:Nisin