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The Journal of Membrane Biology

, Volume 162, Issue 3, pp 259–264 | Cite as

Interactions of Primary Amphipathic Vector Peptides with Membranes. Conformational Consequences and Influence on Cellular Localization

  • P.  Vidal
  • L.  Chaloin
  • A.  Heitz
  • N.  Van Mau
  • J.  Méry
  • G.  Divita
  • F.  Heitz

Abstract.

The conformations of two peptides produced by the combinations of a nuclear localization sequence and a sequence issued from the fusion protein gp41 of HIV 1 have been analyzed both in solution and in membranes or in membrane mimicking environments. Both are shown to be nonordered in water, α-helical when incorporated into SDS micelles where the helical domain concerns the hydrophobic part of the peptides. Interactions with lipids induce the formation of β-sheet and the lipid-peptide interactions are governed by the nature of the lipid polar headgroups. A monolayer study shows that replacement of the sequence separating the two sequences with an arginine favors the lipid-peptide interactions which may contribute to the understanding of the different, nuclear and membrane associated, cellular localizations of the peptides.

Key words: Amphipathic peptides — Conformations — Lipid-peptide interactions 

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Copyright information

© Springer-Verlag New York Inc. 1998

Authors and Affiliations

  • P.  Vidal
    • 1
  • L.  Chaloin
    • 1
  • A.  Heitz
    • 2
  • N.  Van Mau
    • 1
  • J.  Méry
    • 1
  • G.  Divita
    • 1
  • F.  Heitz
    • 1
  1. 1.CRBM-CNRS (UPR 1086), 1919, Route de Mende, F. 34293 Montpellier Cedex 5, FranceFR
  2. 2.CBS-CNRS (UMR 9955) and INSERM U 414, Faculté de Pharmacie, 15, Avenue Charles Flahault, F. 34060 Montpellier Cedex, FranceFR

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