Sánchez Martín, Ma. JesúsHristova, KalinaPujol Cubells, MontserratGómara Elena, María JoséHaro, IsabelAlsina Esteller, Ma. AsunciónBusquets i Viñas, Ma. Antonia2020-06-042020-06-042011-08-010021-9797https://hdl.handle.net/2445/164342The 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.8 p.application/pdfeng(c) Elsevier, 2011VIH (Virus)Síntesi de pèptidsHepatitis GLiposomesMicroscòpia confocalHIV (Viruses)Peptide synthesisHepatitis GLiposomesConfocal microscopyinfo:eu-repo/semantics/article6020372020-06-04info:eu-repo/semantics/openAccess21565353