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dc.contributor.authorLarios, Cristina-
dc.contributor.authorChristiaens, Bart-
dc.contributor.authorGómara Elena, María José-
dc.contributor.authorAlsina, M. Asunción-
dc.contributor.authorHaro Villar, Isabel-
dc.identifier.citationFEBS Journal 272(10): 2456-2466 (2005)en_US
dc.description11 pages, 7 figures, 2 tables.-- PMID: 15885095 [PubMed].-- Printed version published May 2005.en_US
dc.description.abstractThe interaction with phospholipid bilayers of two synthetic peptides with sequences corresponding to a segment next to the native N-terminus and an internal region of the E2 structural hepatitis G virus (HGV/GBV-C) protein [E2(7–26) and E2(279–298), respectively] has been characterized. Both peptides are water soluble but associate spontaneously with bilayers, showing higher affinity for anionic than zwitterionic membranes. However, whereas the E2(7–26) peptide is hardly transferred at all from water to the membrane interface, the E2(279–298) peptide is able to penetrate into negatively charged bilayers remaining close to the lipid/water interface. The nonpolar environment clearly induces a structural transition in the E2(279–298) peptide from random coil to α-helix, which causes bilayer perturbations leading to vesicle permeabilization. The results indicate that this internal segment peptide sequence is involved in the fusion of HGV/GBV-C to membrane.en_US
dc.description.sponsorshipThis work was funded by grants BQU2003-05070-CO2-01/02 from the Ministerio de Ciencia y Tecnología (Spain) and a predoctoral grant awarded to C. L.en_US
dc.format.extent22195 bytes-
dc.publisherBlackwell Publishingen_US
dc.subjectCircular dichroismen_US
dc.subjectFluorescence assaysen_US
dc.subjectHepatitis G virus (HGV/GBV-C)en_US
dc.subjectLipid vesiclesen_US
dc.subjectSynthetic peptidesen_US
dc.titleInteraction of synthetic peptides corresponding to hepatitis G virus (HGV/GBV-C) E2 structural protein with phospholipid vesiclesen_US
dc.description.peerreviewedPeer revieweden_US
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