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Structural properties of hepetitis B virus fusion peptide upon interaction with lipids: a FTIR and CD spectroscopy study. Rodríguez-Crespo, I., Gómez-Gutiérrez, J., Encinar, J.A., González-Ros, J.M., Albar, J.P., Peterson, D.L. and Gavilanes, F. (1996) Eur. J. Biochem. 242, 243-248.

  1. White, J. M. (1992) Membrane fusion, Science 258, 917–924.
  2. Ganem, D. & Varmus, H. E. (1987) The molecular biology of the hepatitis B viruses, Annu. Rev. Biochem. 56, 651–693.
  3. Peterson, D. L. (1987) The structure of hepatitis B surface antigen and its antigenic sites, Bioessays 6, 258–262.
  4. Heermann, K. H. & Gerlich, W. H. (1991) Surface proteins of hepatitis B viruses, in Molecular biology of hepatitis B virus (MacLachlan, A., ed.) pp. 109–143, CRL Press, Boca Raton.
  5. Rodríguez-Crespo, I., Gómez-Gutiérrez, J., Nieto, M., Peterson, D. L. & Gavilanes, F. (1994) Prediction of a putative fusion peptide in the S protein of hepatitis B virus, J. Gen. Virol. 75, 637–639.
  6. Rodríguez-Crespo, I., Gómez-Gutiérrez, J., Peterson, D. L. & Gavilanes, F. (1994) Interaction of a peptide corresponding to the amino-terminus region of the S protein with liposomes, Biochem. Soc. Trans. 22, 365S.
  7. Rodríguez-Crespo, I., Núñez, E., Gómez-Gutiérrez, J., Yélamos, B., Albar, J. P., Peterson, D. L. & Gavilanes, F. (1995) Phospholipid interactions of the putative fusion peptide of hepatitis B surface antigen S protein, J. Gen. Virol. 76, 301–308.
  8. Zhang, Y.-P., Lewis, R. N. A. H., Hodges, R. S. & McElhaney, R. N. (1992) FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane a-helices of membrane proteins, Biochemistry 31, 11572–11578.
  9. Surewicz, W. K., Mantsch, H. H. & Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment, Biochemistry 32, 389–394.
  10. Perczel, A., Hollósi, M., Tusnády, G. & Fasman, G. (1991) Convex constraint analysis: a natural deconvolution of circular dichroism curves of proteins, Protein Eng. 4, 669–679.
  11. Mendelsohn, R. & Mantsch, H. H. (1986) Fourier transform infrared studies of lipid-protein interactions, in Progress in protein-lipid interactions (Watts, A. & DePont, A., eds) pp. 103–146, Elsevier Science Publisher, New York.
  12. Dyson, H. J. & Wright, P. E. (1991) Defining solution conformations of small linear peptides, Annu. Rev. Biophys. Biophys. Chem 20, 519–538.
  13. Perczel, A., Park, K. & Fasman, G. D. (1992) Deconvolution of the circular dichroism spectra of proteins: the circular dichroism spectra of the antiparallel ß-sheet in proteins, Protein Struct. Funct. Genet. 13, 57–69.
  14. Byler, D. M. & Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469–487.
  15. Goormaghtigh, E., Cabiaux, V. & Ruysschaert, J.-M. (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated film, Eur. J. Biochem. 193, 409–420.
  16. Fernández-Ballester, G., Castresana, J., Arrondo, J.-L. R., Ferragut, J. A. & González-Ros, J. M. (1992) Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy, Biochem. J. 288, 421–426.
  17. Moffatt, D. J. & Mantsch, H. H. (1992) Fourier resolution enhancement of infrared spectral data, Methods Enzymol. 210, 192–200.
  18. Wallace, B. A., Kohl, N. & Teeter, M. M. (1984) Crambin in phospholipid vesicles: circular dichroism analysis of crystal structure relevance, Proc. Natl Acad. Sci. USA 81, 1406–1410.
  19. Tobkes, N., Wallace, B. A. & Bayley, H. (1985) Secondary structure and assembly mechanism of an oligomeric channel protein, Biochemistry 24, 1915–1920.
  20. Woody, R. (1974) Studies of theoretical circular dichroism of polypeptides: contributions of ß turns, in Peptides, polypeptides and proteins (Blont, E. R., Bovery, F. A., Goodman, M. & Lotan, N., eds) pp. 338–350, Wiley, New York.
  21. Muga, A., Surewicz, W. K., Wong, P. T. T. & Mantsch, H. H. (1990) Structural studies with the uveopathogenic peptide M derived from retinal S-antigen, Biochemistry 29, 2925–2930.
  22. Jackson, M., Mantsch, H. H. & Spencer, J. H. (1992) Conformation of magainin-2 and related in aqueous solution and membrane environments proved by Fourier transform infrared spectroscopy, Biochemistry 31, 7289–7293.
  23. Nieva, J. L., Nir, S., Muga, A., Goñi, F. M. & Wilschut, J. (1994) Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage, Biochemistry 33, 3201–3209.
  24. Sönnichsen, F. D., Van Eyk, J. E., Hodges, R. S. & Sykes, B. D. (1992) Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide, Biochemistry 31, 8790–8798.
  25. Greenfield, N. J. & Fasman, G. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108–4116.
  26. Ono, S., Lee, S., Mihara, H., Aoyagi, H., Kato, T. & Yamasaki, N. (1990) Design and synthesis of basic peptides having amphipathic ß-structure and their interaction with phospholipid membranes, Biochim. Biophys. Acta 1022, 237–244.
  27. Woody, R. W. (1978) Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins, Biopolymers 17, 1451–1467.
  28. Surewicz, W. K., Stepanik, T. M., Szabo, A. G. & Mantsch, H. H. (1988) Lipid-induced changes in the secondary structure of snake venom cardiotoxins, J. Biol. Chem. 263, 786–790.
  29. Goormaghtigh, E., Vigneron, L., Knibiehler, M., Lazdunski, C. & Ruysschaert, J.-M. (1991) Secondary structure of the membrane-bound form of the pore-forming domain of colicin A, Eur J. Biochem. 202, 1299–1305.
  30. Krantz, D. D., Zidovetzki, R., Kagan, B. L. & Zipursky, S. L. (1991) Amphipathic ß structure of a leucine-rich repeat peptide, J Biol. Chem. 266, 16801–16807.
  31. Lear, J. D. & DeGrado, W. F. (1987) Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2, J. Biol. Chem. 262, 6500–6505.
  32. Ishiguro, R., Kimura, N. & Takahashi, S. (1993) Orientation of fusion-active synthetic peptides in phospholipids bilayers: determination by Fourier transform infrared spectroscopy, Biochemistry 32, 9792–9797.
  33. Martin, I., Dubois, M.-C., Defrise-Quertain, F., Saemark, T., Burny, A., Brasseur, R. & Ruysschaert, J.-M. (1994) Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study, J. Virol. 256, 1139–1148.
  34. Rafalski, M., Lear, J. D. & DeGrado, F. W. (1990) Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41, Biochemistry 29, 7917–7922.
  35. Epand, R. M., Cheetham, J. J., Epand, R. F., Yeagle, P. L., Richardson, C. D., Rockwell, A. & DeGrado, W. F. (1992) Peptide models for the membrane destabilizing actions of viral fusion proteins, Biopolymers 32, 309–314.
  36. Ojcius, D. M. & Young, J. D.-E. (1991) Cytolytic pore-forming proteins and peptides: is there a common structural motif, Trends Biochem. Sci. 16, 225–229.
  37. Muga, A., Neugebauer, W., Hirama, T. & Surewicz, W. K. (1994) Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion, Biochemistry 33, 4444–4448.
  38. Reddy, G. L. & Nagaraj, R. (1989) Circular dichroism studies on synthetic signal peptides indicate ß-conformation as a common structural feature in a highly hydrophobic environment, J. Biol. Chem. 264, 16591–16597.
  39. Guerrero, E., Gavilanes, F. & Peterson, D. L. (1988) Model for the protein arrangement in HBsAg particles based on physical and chemical studies, in Viral hepatitis and liver disease (Zuckerman, A. J., ed.) pp. 606–613, Alan R. Liss, Inc., New York.
  40. Lu, X., Block, T. M. & Gerlich, W. H. (1996) Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line, J. Virol. 70, 2277–2285.