par Martin, Isabelle 
;Quertain, Fabienne ;Mandieau, Valérie ;Nielsen, N M;Saermark, T;Burny, Arsène ;Brasseur, Robert ;Ruysschaert, Jean Marie ;Vandenbranden, Michel
Référence Biochemical and biophysical research communications, 175, 3, page (872-879)
Publication Publié, 1991-03
;Quertain, Fabienne ;Mandieau, Valérie ;Nielsen, N M;Saermark, T;Burny, Arsène ;Brasseur, Robert ;Ruysschaert, Jean Marie ;Vandenbranden, Michel Référence Biochemical and biophysical research communications, 175, 3, page (872-879)
Publication Publié, 1991-03
Article révisé par les pairs
| Résumé : | Peptides of 12, 16 and 24 amino acids length corresponding to the NH2 terminal sequence of SIV gp32 were synthesized. Fluorescence energy transfer studies have shown that those peptides can induce lipid mixing of SUV (Small Unilamellar Vesicles) of various compositions at pH 7.4 and 37 degrees C. LUV (Large Unilamellar Vesicles) were shown to undergo fusion, provided they contained PE in their lipid composition. This work is an attempt to determine how the fusogenic activity depends on the structure of the peptide inserted into a lipidic environment. The peptides secondary structure and orientation in the lipid bilayer were determined using Fourier Transform infrared spectroscopy (FTIR). They adopt mainly a beta-sheet conformation in the absence of lipids. After interaction with DOPC SUV, the beta-sheet is partly converted into alpha-helix oriented obliquely with respect to the membrane interface. We bring here evidence that this oblique orientation is a prerequisite to the fusion process. |
