The covalent coupling of HAV-VP3 (110–121) synthetic peptide to liposomes: physicochemical studies

Abstract

In this work we have studied the conjugation of the immunogenic peptide sequence (110–121) belonging to the VP3 capsid protein of hepatitis A virus to the surface of preformed liposomes by means of an amide bond between the vesicles and the synthetic peptide. The surface activity of the conjugate at air/water interface was determined. Moreover, the interaction of the conjugate with lipids was also studied recording the pressure increases produced after the injection of the liposome–peptide preparation under dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG) and stearylamine (SA) monolayers at different initial surface pressures. As expected, due to the negative net charge of the liposome–peptide complex, the higher interaction was found with positive charge monolayers (SA). However, the conjugate was also able to incorporate to zwitterionic and anionic lipids. This behaviour was also confirmed performing compression isotherms of monolayers of these lipids spread on subphases containing the conjugate. These results suggest that the coupling of VP3 (110–121) to liposomes does not influence its ability to interact with membrane lipids such as DPPC and DPPG. Then it can be assumed that its immunogenicity will be preserved or even increased after this modification. All these results are also useful in the preparation of liposome-based synthetic peptide vaccines.