Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry.

@article{Breukink2000BindingON,
  title={Binding of Nisin Z to bilayer vesicles as determined with isothermal titration calorimetry.},
  author={Eefjan Breukink and Peter A Ganz and Ben de Kruijff and Joachim Seelig},
  journal={Biochemistry},
  year={2000},
  volume={39 33},
  pages={10247-54}
}
Nisin Z, a 34-residue lantibiotic, is secreted by some lactic acid bacteria and exerts its antibacterial activity against various Gram-positive bacteria by permeabilizing the cell membrane. It is a cationic amphiphilic peptide with several unusual dehydro residues and thioether-bridged lanthionines. Isothermal titration calorimetry was used to provide a quantitative thermodynamic description for nisin Z adsorption to and penetration into negatively charged and neutral lipid bilayers. The… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 17 extracted citations

Advances in membrane receptor screening and analysis.

Journal of molecular recognition : JMR • 2004
View 11 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…