Letters in Peptide Science

, Volume 4, Issue 4, pp 359–364

Conformational studies of a benzodiazepine-like peptide in SDS micelles by circular dichroism,1H NMR and molecular dynamics simulation

  • Marc Lecouvey
  • Céline Frochot
  • Laurent Miclo
  • Piotr Orlewski
  • Michel Marraud
  • Jean-Luc Gaillard
  • Manh Thong Cung
  • Régis Vanderesse
Article

DOI: 10.1007/BF02442900

Cite this article as:
Lecouvey, M., Frochot, C., Miclo, L. et al. Lett Pept Sci (1997) 4: 359. doi:10.1007/BF02442900

Summary

The conformation of a benzodiazepine-like decapeptide corresponding to the YLGYLEQLLR fragment of a casein has been examined in a sodium dodecyl sulfate micellar medium using circular dichroism, two-dimensional1H NMR spectroscopy and restrained molecular dynamics simulation. The decapeptide adopts an amphipathic 310-helicoid structure in which the E6...R10 ionic bridge stabilizes the C-terminus.

Keywords

BenzodiazepinesCircular dichroismGABAA receptorMicellar mediumMolecular dynamics2D NMR

Copyright information

© Kluwer Academic Publishers 1997

Authors and Affiliations

  • Marc Lecouvey
    • 1
  • Céline Frochot
    • 1
  • Laurent Miclo
    • 2
  • Piotr Orlewski
    • 1
  • Michel Marraud
    • 1
  • Jean-Luc Gaillard
    • 2
  • Manh Thong Cung
    • 1
  • Régis Vanderesse
    • 1
  1. 1.LCPM, CNRS-URA 494ENSIC-INPLNancy CedexFrance
  2. 2.LBSA, Unité associé à l'INRAUniversité Henri PoincaréVandœuvre lès Nancy CedexFrance