Contact
    Start Publications Lipid domains in LB films and giant vesicles to study GBV-C ...
    ←  Publication Finder
    KSV NIMA

    Lipid domains in LB films and giant vesicles to study GBV-C peptides interaction in the context of HIV-1 FP inhibition at membranes

    Year: 2019

    Journal: Colloid Surf. A-Physicochem. Eng. Asp., Volume 578, 1-Oct

    Authors: Ortiz, A.; Arciniegas, S.; Prat, J.; Munoz-Juncosa, M.; Pujol, M.

    Organizations: Ministerio de Economia y Competitividad of Spain [CTQ2012-37589-C02-01]; Generalitat de CatalunyaGeneralitat de Catalunya [2017 SGR 1629]

    Keywords: Langmuir-Blodgett films; GUVs; Lipid-peptide interaction; HIV-1 FP inhibition; GBV-C peptides

    Lipid domains have been obtained using Langmuir-Blodgett films (LBs) and giant unilamellar vesicles (GUVs). Three membranes compositions were chosen, the canonical DOPC: DOPS (3:2)/SM/CHOL (1:1:1), the more physiological one: DOPC: DOPS (3:2)/SM/CHOL (2:1:1) and another one with more phospholipid content: DOPC: DOPS (3:2)/SM/CHOL (3:1:1). All systems were well characterized by pi-A isotherms. As the (SM/CHOL (1:1:1)) concentration increases, the membrane fluidity decreases as demonstrated by the compressibility modulus and area per molecule values. Lipid domains morphology was examined by confocal microscopy. Images corroborated the presence of two liquid immiscible phases: a phospholipid-enriched L-d phase and a sphingomyelin enriched L-o phase. GBV-C peptide membrane interaction was examined using P6-2VIR576 peptide and tryptophan (Trp) fluorescence spectroscopy. P6-2VIR576 increased the fluidity of lipid monolayers and bilayers making hard to distinguish the L-d/L-o edges. Its capacity to inhibit the action of the fusion peptide of human immunodeficiency virus (HIV-1 FP) on membranes has been demonstrated.
    View publication