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http://hdl.handle.net/2445/164342
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DC Field | Value | Language |
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dc.contributor.author | Sánchez Martín, Ma. Jesús | - |
dc.contributor.author | Hristova, Kalina | - |
dc.contributor.author | Pujol Cubells, Montserrat | - |
dc.contributor.author | Gómara Elena, María José | - |
dc.contributor.author | Haro, Isabel | - |
dc.contributor.author | Alsina Esteller, Ma. Asunción | - |
dc.contributor.author | Busquets i Viñas, Ma. Antonia | - |
dc.date.accessioned | 2020-06-04T15:28:12Z | - |
dc.date.available | 2020-06-04T15:28:12Z | - |
dc.date.issued | 2011-08-01 | - |
dc.identifier.issn | 0021-9797 | - |
dc.identifier.uri | http://hdl.handle.net/2445/164342 | - |
dc.description.abstract | The 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.extent | 8 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier | - |
dc.relation.isformatof | Versió postprint del document publicat a: https://doi.org/10.1016/j.jcis.2011.04.053 | - |
dc.relation.ispartof | Journal of Colloid and Interface Science, 2011, vol. 360, num. 1, p. 124-131 | - |
dc.relation.uri | https://doi.org/10.1016/j.jcis.2011.04.053 | - |
dc.rights | (c) Elsevier, 2011 | - |
dc.source | Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica) | - |
dc.subject.classification | VIH (Virus) | - |
dc.subject.classification | Síntesi de pèptids | - |
dc.subject.classification | Hepatitis G | - |
dc.subject.classification | Liposomes | - |
dc.subject.classification | Microscòpia confocal | - |
dc.subject.other | HIV (Viruses) | - |
dc.subject.other | Peptide synthesis | - |
dc.subject.other | Hepatitis G | - |
dc.subject.other | Liposomes | - |
dc.subject.other | Confocal microscopy | - |
dc.title | Analysis of HIV-1 Fusion Peptide inhibition by synthetic peptides from E1 protein of GB virus C | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.identifier.idgrec | 602037 | - |
dc.date.updated | 2020-06-04T15:28:12Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 21565353 | - |
Appears in Collections: | Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica) |
Files in This Item:
File | Description | Size | Format | |
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602037.pdf | 849.14 kB | Adobe PDF | View/Open |
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