Interaction study of peptide from VP3 capsid protein of hepatitis A virus through monolayers and fluorescence spectroscopy

P. Sospedra, J. Prat, I. Haro, C. Mestres, M. A. Busquets

Producción científica: Artículo en revista indizadaArtículorevisión exhaustiva

1 Cita (Scopus)

Resumen

A synthetic peptide with the sequence [Lys113]VP3(110-121): FWRKDLVFDFQV, corresponding to an epitope of the VP3 capsid protein of hepatitis A virus (HAV), was synthesized by solid phase and characterized. To obtain insight into its physicochemical properties and to understand its possible mechanism of action at the membrane level, interaction with DPPC or DPPC/DPPG (95/5) liposomes and lipid monolayers of DPPC, DPPG, SA, PS, PA and SM were studied by fluorescence spectroscopy and Langmuir-Blotgett films technique, respectively. Fluorescence studies showed that the peptide was in a hydrophobic environment when DPPC liposomes were used. The addition of a 5% of a charged lipid, DPPG, to the preparations changed the preference of the peptide towards a polar surrounding. However, the peptide had a high surface activity (nmol/L) and was able to incorporate into lipid monolayers. Interaction was higher with charged phospholipids than with neutral ones. These results may have physiological significance in the mechanism of infection of host hepatic cells by HAV.

Idioma originalInglés
Páginas (desde-hasta)103-107
Número de páginas5
PublicaciónLuminescence
Volumen16
N.º2
DOI
EstadoPublicada - mar 2001
Publicado de forma externa

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