Using the Langmuir technique, we have studied the proper-ties at the air/water interface and the interaction of the hepatitis G virus synthetic peptide E1(53-66) and its palmitoyl derivative with membrane phospholipids. These phospholipids had different characteristics referring to the net charge and saturation of the acyl chain. The palmitoyl derivative was more stable at the air/water interface and in the kinetic at constant area measurements showed higher incorporation to the monolayer. The interaction was higher for saturated phospholipids and those with a negative net charge. When the peptides were in the subphase, they produced changes in the miscibility of mixed monolayers composed of DPPC/DPPG or DOPC/DOPG. It can be deduced from the results obtained that electrostatic interactions play a major role, but when the peptide is derivatized with the palmitoyl chain, hydrophobic interactions are added to the former ones. The interaction is also influenced by the saturation of the acyl chain.