<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-04-14T06:11:23Z</responseDate><request verb="GetRecord" identifier="oai:www.recercat.cat:2445/164342" metadataPrefix="oai_dc">https://recercat.cat/oai/request</request><GetRecord><record><header><identifier>oai:recercat.cat:2445/164342</identifier><datestamp>2025-11-19T10:41:37Z</datestamp><setSpec>com_2072_1057</setSpec><setSpec>col_2072_478815</setSpec><setSpec>col_2072_478917</setSpec></header><metadata><oai_dc:dc xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
   <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:identifier>0021-9797</dc:identifier>
   <dc:identifier>https://hdl.handle.net/2445/164342</dc:identifier>
   <dc:identifier>602037</dc:identifier>
   <dc:identifier>21565353</dc:identifier>
   <dc:language>eng</dc:language>
   <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:format>8 p.</dc:format>
   <dc:format>application/pdf</dc:format>
   <dc:format>application/pdf</dc:format>
   <dc:publisher>Elsevier</dc:publisher>
   <dc:source>Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)</dc:source>
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