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

Jorge Casas, Marta Espina, Marta Haro, Flix Royo, M. Asunción Alsina, Isabel Haro, Concepción Mestres

Research output: Indexed journal article Articlepeer-review

13 Citations (Scopus)

Abstract

A 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, LLGTEVSEV-LGGAGLTGG, 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 α-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.

Original languageEnglish
Pages (from-to)246-254
Number of pages9
JournalLangmuir
Volume22
Issue number1
DOIs
Publication statusPublished - 3 Jan 2006
Externally publishedYes

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