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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/164344
Effect of E1(64-81) hepatitis G peptide on the in vitro interaction of HIV-1 Fusion Peptide with membrane models
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One way to gain information about the fusogenic potential of virus-derived synthetic peptides is to examine their interfacial properties and subsequently to study them in monolayers and bilayers. Here, we characterize the physicochemical surface properties of the peptide E1(64-81), whose sequence is AQLVGELGSLYGPLSVSA. This peptide is derived from the E1 structural protein of GBV-C/HGV which was previously shown to inhibit leakage of vesicular contents caused by the HIV-1 fusion peptide (HIV-1 FP). Mixed isotherms of E1(64-81) and HIV-1 FP were obtained and their Brewster angle microscopy (BAM) and atomic force microscopy (AFM) images showed that the peptide mixture forms a different structure that is not present in the pure peptide images. Studies with lipid monolayers (1,2-dimyristoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (DMPG) and 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) (DPPG)) show that both peptides interact with all the lipids assayed but the effect that HIV-1 FP has on the monolayers is reduced in the presence of E1(64-81). Moreover, differential scanning calorimetry (DSC) experiments show the capacity of HIV-1 FP to modify the properties of the bilayer structure and the capacity of E1(64-81) to inhibit these modifications. Our results indicate that E1(64-81) interacts with HIV-1 FP to form a new structure, and that this may be the cause of the previously observed inhibition of the activity of HIV-1 FP by E1(64-81).
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SÁNCHEZ MARTÍN, Ma. Jesús, et al. Effect of E1(64-81) hepatitis G peptide on the in vitro interaction of HIV-1 Fusion Peptide with membrane models. Biochimica et Biophysica Acta-Biomembranes. 2011. Vol. 1808, num. 9, pags. 2178-2188. ISSN 0005-2736. [consulted: 9 of June of 2026]. Available at: https://hdl.handle.net/2445/164344