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    Interaction of the GBV-C E2-derived peptide, P6-2VIR576, with anionic phospholipid membranes

    Year: 2017

    Journal: Colloid Surf. A-Physicochem. Eng. Asp., Volume 532, NOV 5, page 483–492

    Authors: Ortiz, Alba; Girona, Victoria; Prat, Josefina; Montserrat Munoz-Juncosa, M.; Asuncion Alsina, M.; Pujol, Montserrat

    Organizations: Ministerio de Economia y Competitividad of Spain [CTQ2012-37589-C02-01/02]; Generalitat de Catalunya [SGR 216]

    Keywords: GBV-C peptides; LB films; Fluorescence microscopy; HIV-1 inhibitors; Peptide-lipid interaction

    The interaction of P6-2VIR576, a peptide derived from the GBV-C E2 structural protein, with anionic lipid membranes (DMPC: DMPS (3:2) and DPPC: DPPS (3:2)) and its effect on HIV-1 fusion peptide (HIV-1 FP) binding with the membrane were studied. P6-2VIR576 showed higher surface activity than its parent peptide AcP6-2, with an area per molecule value in pi-A compression isotherms approximately twice that of AcP6-2. Interaction studies, involving penetration experiments in lipid monolayers and lipid bilayer binding assays, demonstrated that P6-2VIR576 interacted better with the more rigid membrane DPPC: DPPS (3: 2), with an exclusion pressure slightly lower than the biological membrane pressure (24-30 mN m(-1)). This, together with the results of the binding experiments and considering the effect of ionic strength and changes in membrane dipole potential, indicate a lipid-peptide interaction driven by electrostatic forces followed by hydrophobic interactions. Morphological surface analysis by fluorescence microscopy of Langmuir-Blodgett monolayers revealed that P6-2VIR576 suppressed the interaction of HIV-1 FP with the membrane.
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