The miscibility of the synthetic peptide antigen of hepatitis A, [Lys]113VP3110 with zwitterionic, anionic and cationic lipids was studied through compression isotherms of monolayers at the air/water interface. Deviations from ideality was found, with a different behaviour to the one observed with the parent peptide VP3(110-121). Deviations were quantified through the calculation of thermodynamic parameters such as the free energy of mixing (ΔGEXM), interaction parameter (α) and the enthalpy (ΔH).
|Journal||Journal De Physique. IV : JP|
|Publication status||Published - Dec 2001|
|Event||27th Meeting of Studies about Equilibria between Phases JEEP 2001 - Montpellier, France|
Duration: 22 Mar 2001 → 23 Mar 2001