Analysis of HIV-1 Fusion Peptide inhibition by synthetic peptides from E1 protein of GB virus C

dc.contributor.authorSánchez Martín, Ma. Jesús
dc.contributor.authorHristova, Kalina
dc.contributor.authorPujol Cubells, Montserrat
dc.contributor.authorGómara Elena, María José
dc.contributor.authorHaro, Isabel
dc.contributor.authorAlsina Esteller, Ma. Asunción
dc.contributor.authorBusquets i Viñas, Ma. Antonia
dc.date.accessioned2020-06-04T15:28:12Z
dc.date.available2020-06-04T15:28:12Z
dc.date.issued2011-08-01
dc.date.updated2020-06-04T15:28:12Z
dc.description.abstractThe aim of this study was to identify proteins that could inhibit the activity of the peptide sequence representing the N-terminal of the surface protein gp41 of HIV, corresponding to the fusion peptide of the virus (HIV-1 FP). To do this we synthesized and studied 58 peptides corresponding to the envelope protein E1 of the hepatitis G virus (GBV-C). Five of the E1 synthetic peptides: NCCAPEDIGFCLEGGCLV (P7), APEDIGFCLEGGCLVALG (P8), FCLEGGCL VALGCTICTD (P10), QAGLAVRPGKSAAQLVGE (P18) and AQLVGELGSLYGPLSVSA (P22) were capable of inhibiting the leakage of vesicular contents caused by HIV-1 FP. A series of experiments were carried out to determine how these E1 peptides interact with HIV-1 FP. Our studies analyzed the interactions with and without the presence of lipid membranes. Isothermal titration calorimetry revealed that the binding of P7, P18 and P22 peptides to HIV-1 FP is strongly endothermic, and that binding is entropy-driven. Gibbs energy for the process indicates a spontaneous binding between E1 peptides and HIV-1 FP. Moreover, confocal microscopy of Giant Unilamellar Vesicles revealed that the disruption of the lipid bilayer by HIV-1 FP alone was inhibited by the presence of any of the five selected peptides. Our results highlight that these E1 synthetic peptides could be involved in preventing the entry of HIV-1 by binding to the HIV-1 FP. Therefore, the continued study into the interaction between GBV-C peptides and HIV-1 FP could lead to the development of new therapeutic agents for the treatment of AIDS.
dc.format.extent8 p.
dc.format.mimetypeapplication/pdf
dc.identifier.idgrec602037
dc.identifier.issn0021-9797
dc.identifier.pmid21565353
dc.identifier.urihttps://hdl.handle.net/2445/164342
dc.language.isoeng
dc.publisherElsevier
dc.relation.isformatofVersió postprint del document publicat a: https://doi.org/10.1016/j.jcis.2011.04.053
dc.relation.ispartofJournal of Colloid and Interface Science, 2011, vol. 360, num. 1, p. 124-131
dc.relation.urihttps://doi.org/10.1016/j.jcis.2011.04.053
dc.rights(c) Elsevier, 2011
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.sourceArticles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)
dc.subject.classificationVIH (Virus)
dc.subject.classificationSíntesi de pèptids
dc.subject.classificationHepatitis G
dc.subject.classificationLiposomes
dc.subject.classificationMicroscòpia confocal
dc.subject.otherHIV (Viruses)
dc.subject.otherPeptide synthesis
dc.subject.otherHepatitis G
dc.subject.otherLiposomes
dc.subject.otherConfocal microscopy
dc.titleAnalysis of HIV-1 Fusion Peptide inhibition by synthetic peptides from E1 protein of GB virus C
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/acceptedVersion

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