Interfacial properties and structure stability of the gp41 tryptophan-rich peptide from HIV-1

in Journal of Colloid & Interface Science (2010), 352

The HIV-1 envelope glycoprotein 41 (gp41) undergoes large-scale conformational changes in order to induce the fusion of the virus and cell membranes. Thus, we investigated a possible structure transit at ... [more ▼]

The HIV-1 envelope glycoprotein 41 (gp41) undergoes large-scale conformational changes in order to induce the fusion of the virus and cell membranes. Thus, we investigated a possible structure transit at the air-water interface for the tryptophan-rich peptide of gp41 (gp41W). The synthetic peptide (KWASLWNWFNITNWLWYIK), corresponding to gp41W, shows interfacial properties on pure water and Tris buffer at pH 8.5. Isotherm measurements and Brewster angle microscopy (BAM) imaging showed that the behavior of the peptide monolayer was dependent on the subphase composition. A homogenous film was formed on buffer during the peptide monolayer compression, while the appearance of condensed domains on pure water could indicate the oligomerization of gp41W during the surface pressure increase. Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) showed that, whatever the subphase, gp41W adopts an α-helix structure at the air-water interface and does not transit for any other structure even at high surface pressures. [less ▲]

Approches biomimétiques de l’analyse des interactions entre un lipopeptide bactérien antifongique, la mycosubtiline, et la membrane cytoplasmique des cellules cibles

Conference (2009)

Conformational and interfacial analyses of K3A18K3 and alamethicin in model membranes.

in Journal of Physical Chemistry B (2009), 113

The involvement of membrane-bound peptides and the influence of protein conformations in several neurodegenerative diseases lead us to analyze the interactions of model peptides with artificial membranes ... [more ▼]

The involvement of membrane-bound peptides and the influence of protein conformations in several neurodegenerative diseases lead us to analyze the interactions of model peptides with artificial membranes. Two model peptides were selected. The first one, an alanine-rich peptide, K3A18K3, was shown to be in R-helix structures in TFE, a membrane environment-mimicking solvent, while it was mostly -sheeted in aqueous buffer as revealed by infrared spectroscopy. The other, alamethicin, a natural peptide, was in a stable R-helix structure. To determine the role of the peptide conformation on the nature of its interactions with lipids, we compared the structure and topology of the conformational-labile peptide K3A18K3 and of the R-helix rigid alamethicin in both aqueous and phospholipid environments (Langmuir monolayers and multilamellar vesicles). K3A18K3 at the air-water interface showed a pressure-dependent orientation of its -sheets, while the R-helix axis of alamethicin was always parallel to the interface, as probed by polarization modulation infrared reflection absorption spectroscopy. The -sheeted K3A18K3 peptide was uniformly distributed into DPPC condensed domains, while the helical-alamethicin insertion distorted the DPPC condensed domains, as evidenced by Brewster angle microscopy imaging of the air/interface. The -sheeted K3A18K3 interacted with DMPC multilamellar vesicles via hydrophilic interactions with polar heads and the helical-alamethicin via hydrophobic interactions with alkyl chains, as shown by infrared spectroscopy and solid state NMR. Our findings are consistent with the prevailing assumption that the conformation of the peptide predetermines the mode of interaction with lipids. More precisely, helical peptides tend to be inserted via hydrophobic interactions within the hydrophobic region of membranes, while -sheeted peptides are predisposed to interact with polar groups and stay at the surface of lipid layer [less ▲]

Influence of natural and synthetic peptides on biomimetic membranes

Poster (2008)