Interactions of Primary Amphipathic Vector Peptides with Membranes. Conformational Consequences and Influence on Cellular Localization |
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Authors: | P. Vidal L. Chaloin A. Heitz N. Van Mau J. Méry G. Divita F. Heitz |
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Affiliation: | (1) CRBM-CNRS (UPR 1086), 1919, Route de Mende, F. 34293 Montpellier Cedex 5, France, FR;(2) CBS-CNRS (UMR 9955) and INSERM U 414, Faculté de Pharmacie, 15, Avenue Charles Flahault, F. 34060 Montpellier Cedex, France, FR |
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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. Received: 10 October 1997/Revised: 15 January 1998 |
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Keywords: | : Amphipathic peptides — Conformations — Lipid-peptide interactions |
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