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Surface Location and Orientation of the Lantibiotic Nisin Bound to Membrane-Mimicking Micelles of Dodecylphosphocholine and of Sodium Dodecylsulphate

  1. Henno W. Van Den Hooven,
  2. Chris A. E. M. Spronk,
  3. Mart Van De Kamp,
  4. Ruud N. H. Konings,
  5. Cornelis W. Hilbers*,
  6. Frank J. M. Van De Ven

Article first published online: 31 AUG 2004

DOI: 10.1111/j.1432-1033.1996.00394.x

Issue

European Journal of Biochemistry

European Journal of Biochemistry

Volume 235, Issue 1-2, pages 394–403, January 1996

Additional Information

How to Cite

Van Den Hooven, H. W., Spronk, C. A. E. M., Van De Kamp, M., Konings, R. N. H., Hilbers, C. W. and Van De Ven, F. J. M. (1996), Surface Location and Orientation of the Lantibiotic Nisin Bound to Membrane-Mimicking Micelles of Dodecylphosphocholine and of Sodium Dodecylsulphate. European Journal of Biochemistry, 235: 394–403. doi: 10.1111/j.1432-1033.1996.00394.x

Author Information

  1. NSR Center for Molecular Structure, Design and Synthesis, Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands.

*C. W. Hilbers, NSR Center, Faculty of Science, Laboratory of Biophysical Chemistry, Toernooiveld, NL-6525 ED Nijmegen, The Netherlands. Fax:+31 24 3652112.

Publication History

  1. Issue published online: 31 AUG 2004
  2. Article first published online: 31 AUG 2004
  3. (Received 26 July 1995) – EJB 95 1241/3

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Keywords:

  • bacteriocin;
  • lanthionine-containing polypeptide;
  • mode of action;
  • NMR;
  • spin label

Abstract

  1. Top of page
  2. Abstract
  3. References

The interaction of nisin, a membrane-interacting cationic polypeptide, with membrane-mimicking micelles of zwitterionic dodecylphosphocholine and of anionic sodium dodecylsulphate was studied. Direct contacts have been established through the observation of NOEs between nisin and micelle protons. Spin-labeled DOXYL-stearic acids were incorporated into the two micellar systems. From the paramagnetic broadening effects induced in the 1H-NMR spectrum of nisin it is concluded that the molecule is localized at the surface of the micelles. The interactions of nisin with zwitterionic and with anionic micelles resemble each other as do the nisin conformations [van den Hooven, H. W., Doeland, C. C. M., van de Kamp, M., Konings, R. N. H., Hilbers, C. W. & van de Ven, F. J. M. (1995) Eur. J. Biochem. 235, 382–393]. The hydrophobic residues are immersed into the micelles and oriented towards the center, whereas the more polar or charged residues have an outward orientation. The micellar systems are considered to model the first step in the mechanism of antimicrobial action of nisin, this step is the binding of nisin to the cytoplasmic membrane of target bacteria. Detailed information on this initial binding step is obtained. Hydrophobic and electrostatic interactions appear to be involved in the nisin-micelle contacts. It is suggested that subtilin, a lantibiotic structurally related to nisin, has a comparable membrane interaction surface.

Abbreviations
Alas*

3-methylalanyl moiety of (2S, 3S, 6R)-3-methyllanthionine

Alas

d-alanyl moiety of meso -lanthionine

sAla

l-alanyl moicty of meso -lanthionine or of (2S, 3S, 6R)-3-methyllanthionine

1/2/3D

one-/two-/three-dimensional

Dha

dehydroalanine

Dhb

dehydrobutyrine (3-melhyldehydroalanine)

DodP Cho

dodecylphosphocholine

Δψ

transmembrane potential

NOESY

NOE spectroscopy

ppb

parts per billion

ppm

parts per million

TOCSY

total correlated Spectroscopy

TPPI

time-proportional phase incrementation

References

  1. Top of page
  2. Abstract
  3. References
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