Interactions of primary amphipathic vector peptides with membranes. Conformational consequences and influence on cellular localization.
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.
Vidal
P
P
CRBM-CNRS (UPR 1086), 1919, Route de Mende, F. 34293 Montpellier Cedex 5, France.
Chaloin
L
L
Heitz
A
A
Van Mau
N
N
Méry
J
J
Divita
G
G
Heitz
F
F
D000595:Amino Acid Sequence; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D011487:Protein Conformation; D013057:Spectrum Analysis; D014867:Water
D015700:HIV Envelope Protein gp41; D008567:Membranes, Artificial; D010455:Peptides; D010743:Phospholipids; D014867:Water