Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin

Arch Microbiol. 1987;149(2):120-4. doi: 10.1007/BF00425076.


The peptide antibiotic nisin is shown to disrupt valinomycin-induced potassium diffusion potentials imposed on intact cells of Staphylococcus cohnii 22. Membrane depolarization occurred rapidly at high diffusion potentials while at low potentials nisin-induced depolarization was slower suggesting that nisin requires a membrane potential for activity. This assumption was proven in experiments with planar lipid bilayers (black lipid membranes). Macroscopic conductivity measurements indicated a voltage-dependent action of nisin. The potential must have a trans-negative orientation with respect to the addition of nisin (added to the cis-side) and a sufficient magnitude (ca.-100 mV). With intact cells the threshold potential was lower (-50 to -80 mV at pH 7.5 and below -50 mV at pH 5.5). Single channel recordings resolved transient multi-state pores, strongly resembling those introduced by melittin into artificial bilayers. The pores had diameters in the range of 0.2-1 nm, and lifetimes of few to several hundred milliseconds. The results indicate that nisin has to be regarded as a membrane-depolarizing agent which acts in a voltage-dependent fashion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Hydrogen-Ion Concentration
  • Lipid Bilayers / metabolism*
  • Membrane Potentials / drug effects
  • Nisin / pharmacology*
  • Potassium / metabolism
  • Staphylococcus / drug effects*
  • Staphylococcus / metabolism


  • Lipid Bilayers
  • Nisin
  • Potassium