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dc.contributor.authorLarios, Cristina-
dc.contributor.authorBusquets, M. Antònia-
dc.contributor.authorCarilla Auguet, Josep-
dc.contributor.authorAlsina, M. Asunción-
dc.contributor.authorHaro Villar, Isabel-
dc.date.accessioned2009-11-24T13:49:57Z-
dc.date.available2009-11-24T13:49:57Z-
dc.date.issued2004-11-06-
dc.identifier.citationLangmuir 20(25): 11149-11160 (2004)en_US
dc.identifier.issn0743-7463-
dc.identifier.urihttp://hdl.handle.net/10261/18977-
dc.description12 pages, 8 figures, 6 tables.-- PMID: 15568870 [PubMed].-- Printed version published Dec 7, 2004.en_US
dc.description.abstractThe present study was undertaken to examine the physicochemical properties of three overlapping peptides belonging to the E2 envelope protein of Hepatitis G virus (GBV-C/HGV) and its interaction with phospholipid biomembrane models using biophysical techniques. We describe our findings concerning the surface activity and the interaction of the peptides with monolayers and liposomes composed of the zwitterionic phospholipids dipalmitoylphosphatidylcholine and dimyristoylphosphatidylcholine (DMPC) and a mixture of DMPC with the anionic phospholipid dimyristoylphosphatidylglycerol. The results inform about the effect of the chain length on their interaction with biomembrane models. The longest chain peptide interacts in a higher extent with all the phospholipid studied as a result of a combination of hydrophobic and electrostatic forces.en_US
dc.description.sponsorshipThis work was funded by Grants BQU2003-05070-CO2-01/02 from the Ministerio de Ciencia y Tecnología (Spain).en_US
dc.format.extent22195 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsclosedAccessen_US
dc.subjectHepatitis G virus (GBV-C/HGV)en_US
dc.subjectPhospholipid biomembrane modelsen_US
dc.subjectLipid membrane systemen_US
dc.titleEffects of overlapping GB virus C/hepatitis G virus synthetic peptides on biomembrane modelsen_US
dc.typeartículoen_US
dc.identifier.doi10.1021/la048551g-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1021/la048551gen_US
dc.identifier.e-issn1520-5827-
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