Study of the miscibility of the hepatitis A synthetic antigen [Lys]113VP3110 with lipids

P. Sospedra; M. A. Alsina; M. Espina; I. Haro; C. Mestres

doi:10.1051/jp4:20011040

Study of the miscibility of the hepatitis A synthetic antigen [Lys]¹¹³VP3110 with lipids

P. Sospedra
, M. A. Alsina
, M. Espina
, I. Haro^*
, C. Mestres

^*Autor corresponent d’aquest treball

Producció científica: Article en revista indexada › Article de conferència › Avaluat per experts

Resum

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 (ΔG^EX_M), interaction parameter (α) and the enthalpy (ΔH).

Idioma original	Anglès
Pàgines (de-a)	Pr10/247-Pr10/251
Revista	Journal De Physique. IV : JP
Volum	11
Número	10
DOIs	https://doi.org/10.1051/jp4:20011040
Estat de la publicació	Publicada - de des. 2001
Publicat externament	Sí
Esdeveniment	27th Meeting of Studies about Equilibria between Phases JEEP 2001 - Montpellier, France Durada: 22 de març 2001 → 23 de març 2001

SDG de les Nacions Unides

Aquest resultat contribueix als següents objectius de desenvolupament sostenible.

ODS 3 Salut i benestar

Accés al document

10.1051/jp4:20011040

Altres arxius i enllaços

Link to publication in Scopus

Com citar-ho

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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).",

author = "P. Sospedra and Alsina, \{M. A.\} and M. Espina and I. Haro and C. Mestres",

year = "2001",

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AU - Sospedra, P.

AU - Alsina, M. A.

AU - Espina, M.

AU - Haro, I.

AU - Mestres, C.

PY - 2001/12

Y1 - 2001/12

N2 - 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).

AB - 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).

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DO - 10.1051/jp4:20011040

M3 - Conference article

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