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dc.contributor.authorPérez, S.-
dc.contributor.authorMiñones Jr., J.-
dc.contributor.authorEspina, Marta-
dc.contributor.authorAlsina, M. Asunción-
dc.contributor.authorHaro Villar, Isabel-
dc.contributor.authorMestres, Concepció-
dc.identifier.citationJournal of Physical Chemistry B 109(42): 19970–19979 (2005)en_US
dc.description10 pages, 11 figures, 3 tables.-- PMID: 16853582 [PubMed].-- Printed version published Oct 27, 2005.en_US
dc.description.abstractUsing the Langmuir technique, we have studied the properties at the air/water interface and the interaction of the hepatitis G virus synthetic peptide E1(53−66) and its palmitoyl derivative with membrane phospholipids. These phospholipids had different characteristics referring to the net charge and saturation of the acyl chain. The palmitoyl derivative was more stable at the air/water interface and in the kinetic at constant area measurements showed higher incorporation to the monolayer. The interaction was higher for saturated phospholipids and those with a negative net charge. When the peptides were in the subphase, they produced changes in the miscibility of mixed monolayers composed of DPPC/DPPG or DOPC/DOPG. It can be deduced from the results obtained that electrostatic interactions play a major role, but when the peptide is derivatized with the palmitoyl chain, hydrophobic interactions are added to the former ones. The interaction is also influenced by the saturation of the acyl chain.en_US
dc.description.sponsorshipThis work was supported by project BQU2003-0507-CO2-01/02, from the Ministerio de Ciencia y Tecnología (Spain).en_US
dc.format.extent22195 bytes-
dc.publisherAmerican Chemical Societyen_US
dc.subjectHepatitis G virusen_US
dc.subjectLangmuir techniqueen_US
dc.subjectSynthetic peptidesen_US
dc.subjectPeptide monolayersen_US
dc.titleInfluence of the saturation chain and head group charge of phospholipids in the interaction of hepatitis G virus synthetic peptidesen_US
dc.description.peerreviewedPeer revieweden_US
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