Please use this identifier to cite or link to this item:
Title: Analysis of HIV-1 Fusion Peptide inhibition by synthetic peptides from E1 protein of GB virus C
Author: Sánchez Martín, Ma. Jesús
Hristova, Kalina
Pujol Cubells, Montserrat
Gómara Elena, María José
Haro, Isabel
Alsina Esteller, Ma. Asunción
Busquets i Viñas, Ma. Antonia
Keywords: VIH (Virus)
Síntesi de pèptids
Hepatitis G
Microscòpia confocal
HIV (Viruses)
Peptide synthesis
Hepatitis G
Confocal microscopy
Issue Date: 1-Aug-2011
Publisher: Elsevier
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.
Note: Versió postprint del document publicat a:
It is part of: Journal of Colloid and Interface Science, 2011, vol. 360, num. 1, p. 124-131
Related resource:
ISSN: 0021-9797
Appears in Collections:Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)

Files in This Item:
File Description SizeFormat 
602037.pdf849.14 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.