PMID: 9543498May 16, 1998Paper

Interactions of primary amphipathic vector peptides with membranes. Conformational consequences and influence on cellular localization

The Journal of Membrane Biology
P VidalF 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, alpha-helical when incorporated into SDS micelles where the helical domain concerns the hydrophobic part of the peptides. Interactions with lipids induce the formation of beta-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.

Citations

Jun 7, 2000·European Journal of Pharmaceutics and Biopharmaceutics : Official Journal of Arbeitsgemeinschaft Für Pharmazeutische Verfahrenstechnik E.V·I LebedevaM Vilenchik
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Jan 7, 2005·Journal of Peptide Science : an Official Publication of the European Peptide Society·Allison Langham, Yiannis Kaznessis
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Oct 4, 2005·Biophysical Journal·Thomas PlénatChristian Le Grimellec
Dec 8, 2004·Biochimica Et Biophysica Acta·Sébastien DeshayesFrédéric Heitz
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Aug 7, 2013·The Journal of Physical Chemistry. B·V Volkov, M Bonn
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