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Analysis of HIV-1 fusion peptide inhibition by synthetic peptides from E1 protein of GB virus C

AuthorsSánchez Martín, M. Jesús ; Hristova, Kalina; Pujol, Montserrat; Haro Villar, Isabel ; Alsina, M. Asunción ; Busquets, M. Antònia; Gómara Elena, María José
KeywordsHIV-1 FP inhibition
Hepatitis G virus
Peptide synthesis
Bilayers as model membranes
Giant unilamellar vesicles
Confocal microscopy
Issue Date2011
CitationJournal of Colloid and Interface Science
AbstractThe 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), FCLEGGCLVALGCTICTD (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.
Publisher version (URL)http://dx.doi.org/10.1016/j.jcis.2011.04.053
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