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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/14563
Título

Interfacial properties of a synthetic peptide derived from hepatitis G virus E2 protein: interaction with lipid monolayers

AutorCasas, Jordi; Espina, Marta; Haro Remón, Marta ; Royo, Félix; Alsina, M. Asunción; Haro Villar, Isabel; Mestres, Concepció
Palabras claveHepatitis G
Lipid monolayers
Peptide Derived
E2 protein
Fecha de publicación3-ene-2006
EditorAmerican Chemical Society
CitaciónLangmuir 22(1): 246-254 (2006)
ResumenA useful approach to get information about the potential fusogenic ability of virus synthetic peptides is the study of its interfacial properties and subsequent study in mono- and bilayers. In this work, we have characterized by means of physicochemical tools (i.e. compression isotherms and surface activity) the sequence 267-284, LLGTEVSEVLGGAGLTGG, derived from the E2 structural protein of HGV/GBV-C. The adsorption of the peptide at the air/water interface was monitored by following the increase in surface pressure as a function of time at two different pH values: 5 and 7. Parameters such as surface excess or molecular area were calculated from the equation of Gibbs. The peptide showed a tendency to migrate to the surface of a saline-buffered solution. It formed stable monolayers at the air/water interface giving a compression isotherm with a shape consistent with that of some R-helical peptide conformations. Brewster angle microscopy (BAM) showed that through compression the peptide formed multilayers. The studies with lipid monolayers (DPMC, DMPC/DMPG, and DMPC/DMTAP) showed that the peptide interacts with all the lipids assayed producing a marked disrupting effect upon them. In these effects electrostatic interactions seem to have some participation.
Descripción9 pages, 13 figures.-- PMID: 16378428 [PubMed].-- Available online Dec 3, 2005.-- Supporting information avaliable at: http://pubs.acs.org/doi/full/10.1021/la051812h
Versión del editorhttp://dx.doi.org/10.1021/la051812h
URIhttp://hdl.handle.net/10261/14563
DOI10.1021/la051812h
ISSN1520-5827
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