The present study was undertaken to examine the physicochemical properties of three overlapping peptides belonging to the E2 envelope protein of Hepatitis G virus (GBV-C/HGV) and its interaction with phospholipid biomembrane models using biophysical techniques. We describe our findings concerning the surface activity and the interaction of the peptides with monolayers and liposomes composed of the zwitterionic phospholipids dipalmitoylphosphatidylcholine and dimyristoylphosphatidylcholine (DMPC) and a mixture of DMPC with the anionic phospholipid dimyristoylphosphatidylglycerol. The results inform about the effect of the chain length on their interaction with biomembrane models. The longest chain peptide interacts in a higher extent with all the phospholipid studied as a result of a combination of hydrophobic and electrostatic forces.