The synthesis and physicochemical characterization of a Laminin peptide sequence is described. Peptides showed good spreadibility characteristics giving monolayers stable up to 40-50 mN/m of compression pressures. All of the peptides penetrate neutral, cationic, and anionic monolayers. The peptides interaction with lipids, studied by tyrosine fluorescence changes, resulted in conformational changes in the tyrosine environment. After incubation with either carboxyfluorescein loaded liposomes or red blood cells almost no release of entrapped material was detected. Moreover, the presence of these peptides induces a very low and slow fusion process of liposomes as determined by resonance energy transfer.