Abstract
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 π-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 (24–30mNm−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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