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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/16228
Título

Analysis of the effect of a peptide sequence of the E2 protein (HGV/GBV-C) on the physicochemical properties of zwitterionic and negatively charged bilayers

AutorAlay, Maite; Alsina, M. Asunción; Haro Villar, Isabel; Prat, Josefina; Busquets, M. Antònia
Palabras claveHGV/GBV-C
Synthetic peptide
Liposomes
Anisotropy
Trp fluorescence
FRET
Fecha de publicación20-jun-2005
EditorJohn Wiley & Sons
CitaciónLuminescence 20(6): 445-450 (2005)
ResumenThe membrane-interacting properties of a potential epitope of GB virus C/hepatitis G virus located at the region (99–118) of the E2 structural protein were investigated using several fluorescence techniques. SUV of DMPC:DPPC (1:1) or DMPG:DPPC (1:1) zwitterionic and anionic mixtures, respectively, were used as model membranes. FRET with NBD-PE as energy donor and Rho-PE as energy acceptor-labelled SUV indicated that the peptide was able to fuse both zwitterionic and anionic SUVs, the latter requiring lower peptide concentrations. However, the peptide increased the steady-state anisotropy of DPH embedded in the hydrophobic centre of the membrane with zwitterionic headgroups and to a lesser extent in anionic bilayers, suggesting that charge–charge interactions are not required for membrane interactions and also confirming the FRET results. No changes in anisotropy were observed with the probe TMA-DPH located at the surface of the bilayer. Finally, analysis of the intrinsic emission fluorescence of the tryptophan residue, upon incubation with SUV, showed a blue shift in the presence of anionic bilayers, both below and above the main transition temperature (Tm) (gel to liquid-crystalline state) and, to a lesser extent, with the zwitterionic model membrane.
Descripción6 pages, 6 figures, 1 table.-- PMID: 15966052 [PubMed].-- Printed version published Nov 2005.
Versión del editorhttp://dx.doi.org/10.1002/bio.871
URIhttp://hdl.handle.net/10261/16228
DOI10.1002/bio.871
ISSN1522-7235 (Print)
1522-7243 (Online)
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