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               <dc:title>Analysis of HIV-1 Fusion Peptide inhibition by synthetic peptides from E1 protein of GB virus C</dc:title>
               <dc:creator>Sánchez Martín, Ma. Jesús</dc:creator>
               <dc:creator>Hristova, Kalina</dc:creator>
               <dc:creator>Pujol Cubells, Montserrat</dc:creator>
               <dc:creator>Gómara Elena, María José</dc:creator>
               <dc:creator>Haro, Isabel</dc:creator>
               <dc:creator>Alsina Esteller, Ma. Asunción</dc:creator>
               <dc:creator>Busquets i Viñas, Ma. Antonia</dc:creator>
               <dc:subject>VIH (Virus)</dc:subject>
               <dc:subject>Síntesi de pèptids</dc:subject>
               <dc:subject>Hepatitis G</dc:subject>
               <dc:subject>Liposomes</dc:subject>
               <dc:subject>Microscòpia confocal</dc:subject>
               <dc:subject>HIV (Viruses)</dc:subject>
               <dc:subject>Peptide synthesis</dc:subject>
               <dc:subject>Hepatitis G</dc:subject>
               <dc:subject>Liposomes</dc:subject>
               <dc:subject>Confocal microscopy</dc:subject>
               <dc:description>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:description>
               <dc:date>2020-06-04T15:28:12Z</dc:date>
               <dc:date>2020-06-04T15:28:12Z</dc:date>
               <dc:date>2011-08-01</dc:date>
               <dc:date>2020-06-04T15:28:12Z</dc:date>
               <dc:type>info:eu-repo/semantics/article</dc:type>
               <dc:type>info:eu-repo/semantics/acceptedVersion</dc:type>
               <dc:relation>Versió postprint del document publicat a: https://doi.org/10.1016/j.jcis.2011.04.053</dc:relation>
               <dc:relation>Journal of Colloid and Interface Science, 2011, vol. 360, num. 1, p. 124-131</dc:relation>
               <dc:relation>https://doi.org/10.1016/j.jcis.2011.04.053</dc:relation>
               <dc:rights>(c) Elsevier, 2011</dc:rights>
               <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
               <dc:publisher>Elsevier</dc:publisher>
               <dc:source>Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)</dc:source>
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