Abstract
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).
| Original language | English |
|---|---|
| Pages (from-to) | Pr10/247-Pr10/251 |
| Journal | Journal De Physique. IV : JP |
| Volume | 11 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Dec 2001 |
| Externally published | Yes |
| Event | 27th Meeting of Studies about Equilibria between Phases JEEP 2001 - Montpellier, France Duration: 22 Mar 2001 → 23 Mar 2001 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
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