Interaction of two overlapped synthetic peptides from GB virus C with charged mono and bilayers

The physical chemistry properties and interactions of E2 (125–139) and E2 (120–139) peptide sequences from GB virus C with model cell membranes were investigated by means of several biophysical techniques in order to gain better understanding of the effect of peptide length and lipid charge on membrane binding. The peptides, having one net negative charge at the pH of the assays, interacted with monolayers of all the phospholipids regardless of the charge but with more extent with the cationic DPTAP thus indicating that the interaction had both a hydrophobic and an electrostatic component as has been observed for other peptides of the same family. The peptides were able to leakage contents of liposomes and showed fluorescence energy transfer in vesicles depending on the vesicles lipid composition. On another hand, circular dichroism has shown that the peptides exist mainly as a mixture of disordered structure and β-type conformations in aqueous solution but diminished its unstructured content, folding preferentially into α-helical conformation upon interaction with hydrophobic solvents or positively charged lipid surfaces. Altogether, results of this work indicate that the peptides interact at a surface level, penetrate into bilayers composed of fluid lipids and that conformational changes could be responsible for this effect.

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► Physical chemistry properties of E2 (120–139) and (125–139) from GBV-C are compared.
► Two peptide sequences from the E2 protein of GB virus C insert into lipid monolayers.
► Peptide chain length does not modify the nature of the interaction.
► Peptides interaction with bilayers is strongly dependent on lipid composition.
► E2 (125–139) adopts a random coil conformation in solution and α-helix in bilayers.