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Analytical and Bioanalytical Chemistry

, Volume 394, Issue 4, pp 1003–1010 | Cite as

Fluorescence study of the dynamic interaction between E1(145–162) sequence of hepatitis GB virus C and liposomes

  • Maria Jesús Sánchez-MartínEmail author
  • José Manuel Amigo
  • Montserrat Pujol
  • Isabel Haro
  • M. Asunción Alsina
  • M. Antonia Busquets
Original Paper

Abstract

The physicochemical characterization of the peptide sequence E1(145–162) corresponding to the structural protein E1 of the hepatitis G virus was done by studying its interaction with model membranes. Small unilamellar vesicles (SUVs) of dimyristoylphosphatidylglycerol or dimyristoylphosphatidylcholine were chosen as mimetic membranes. Peptide incorporation and location in the phospholipid bilayer was investigated by fluorescence anisotropy with SUVs labeled with diphenylhexatriene (DPH) or trimethylammonium–DPH. The addition of the peptide E1(145–162) showed significant changes in the anisotropy values of the probe located at the air/water interface. These results indicate that the peptide E1(145–162) preferably interacts with the lipid surface without penetrating inside the bilayer. A series of fluorescence experiments based on tryptophan peptide fluorescence were modeled by means of multivariate curve resolution-alternating least squares (MCR-ALS) algorithm to further study the peptide interaction with bilayers at different temperatures. The preliminary results obtained with MCR-ALS showed how the peptide concentration decay is directly linked to the appearance of a new specie, which corresponds to the lipid-peptide binding. These results provide useful information for the design of synthetic immunopeptides that can be incorporated into a liposomal system with potential to promote a direct delivery of the membrane-incorporated immunogen to the immunocompetent cells, thus increasing the immuno response from the host.

Keywords

Hepatitis GB virus C HGV/GBV-C MCR-ALS Tryptophan fluorescence Liposomes Synthetic peptides Anisotropy 

Notes

Acknowledgments

This work is supported by project CTQ2006-15396-C02-02/01-BQU from Secretaría de Estado de Investigación, Ministerio de Ciencia e Innovación, Dirección General de Programas y transferencia de conocimiento, Subdirección General de Proyectos de Investigación (Spain). M.J. Sánchez-Martín is a recipient of a FPI program pre-doctoral grant. José Manuel Amigo wants to thank the Danish Research Council for Technology and Production Sciences for his post-doctoral fellowship. The authors are members of the consolidated research group by the Generalitat de Catalunya: Peptides and Proteins: physicochemical studies (2005SGR00278).

Supplementary material

216_2008_2593_Fig7_ESM.tif (556 kb)
Fig. S1 (TIF 555 KB)

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Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  • Maria Jesús Sánchez-Martín
    • 1
    Email author
  • José Manuel Amigo
    • 2
  • Montserrat Pujol
    • 1
  • Isabel Haro
    • 3
  • M. Asunción Alsina
    • 1
  • M. Antonia Busquets
    • 1
  1. 1.Physical Chemistry Department, Faculty of PharmacyUniversity of Barcelona, Associated Unit to the CSIC: Peptides and Proteins: Physicochemical StudiesBarcelonaSpain
  2. 2.Department of Food Science Quality & TechnologyUniversity of CopenhagenFrederiksberg-CDenmark
  3. 3.Unit of Synthesis and Biomedical Application of Peptides, Department of Biomedical ChemistryIQAC-CSICBarcelonaSpain

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