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Volumn 242, Issue 2, 1996, Pages 243-248

Structural properties of the putative fusion peptide of hepatitis B virus upon interaction with phospholipids. Circular dichroism and Fourier-transform infrared spectroscopy studies

Author keywords

Fusion peptide; Hepatitis B virus

Indexed keywords

HYBRID PROTEIN; VITRONECTIN;

EID: 0029808164     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0243r.x     Document Type: Article
Times cited : (20)

References (40)
  • 1
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. (1992) Membrane fusion, Science 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 2
    • 0023080494 scopus 로고
    • The molecular biology of the hepatitis B viruses
    • Ganem, D. & Varmus, H. E. (1987) The molecular biology of the hepatitis B viruses, Annu. Rev. Biochem. 56, 651-693.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 651-693
    • Ganem, D.1    Varmus, H.E.2
  • 3
    • 0023353201 scopus 로고
    • The structure of hepatitis B surface antigen and its antigenic sites
    • Peterson, D. L. (1987) The structure of hepatitis B surface antigen and its antigenic sites, Bioessays 6, 258-262.
    • (1987) Bioessays , vol.6 , pp. 258-262
    • Peterson, D.L.1
  • 4
    • 0000523194 scopus 로고
    • Surface proteins of hepatitis B viruses
    • (MacLachlan, A., ed.) CRL Press, Boca Raton
    • 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.
    • (1991) Molecular Biology of Hepatitis B Virus , pp. 109-143
    • Heermann, K.H.1    Gerlich, W.H.2
  • 8
    • 0026482964 scopus 로고
    • FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins
    • 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 α-helices of membrane proteins, Biochemistry 31, 11 572-11 578.
    • (1992) Biochemistry , vol.31 , pp. 11572-11578
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 9
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • 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.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 10
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • 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.
    • (1991) Protein Eng. , vol.4 , pp. 669-679
    • Perczel, A.1    Hollósi, M.2    Tusnády, G.3    Fasman, G.4
  • 11
    • 0002529507 scopus 로고
    • Fourier transform infrared studies of lipid-protein interactions
    • (Watts, A. & DePont, A., eds) Elsevier Science Publisher, New York
    • 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.
    • (1986) Progress in Protein-lipid Interactions , pp. 103-146
    • Mendelsohn, R.1    Mantsch, H.H.2
  • 12
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H. J. & Wright, P. E. (1991) Defining solution conformations of small linear peptides, Annu. Rev. Biophys. Biophys. Chem 20, 519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 0026628269 scopus 로고
    • Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel β-sheet in proteins
    • Perczel, A., Park, K. & Fasman, G. D. (1992) Deconvolution of the circular dichroism spectra of proteins: the circular dichroism spectra of the antiparallel β-sheet in proteins, Protein Struct. Funct. Genet. 13, 57-69.
    • (1992) Protein Struct. Funct. Genet. , vol.13 , pp. 57-69
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 14
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M. & Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 15
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated film
    • 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.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 16
    • 0026443750 scopus 로고
    • Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy
    • 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.
    • (1992) Biochem. J. , vol.288 , pp. 421-426
    • Fernández-Ballester, G.1    Castresana, J.2    Arrondo, J.-L.R.3    Ferragut, J.A.4    González-Ros, J.M.5
  • 17
    • 0026718395 scopus 로고
    • Fourier resolution enhancement of infrared spectral data
    • Moffatt, D. J. & Mantsch, H. H. (1992) Fourier resolution enhancement of infrared spectral data. Methods Enzymol. 210, 192-200.
    • (1992) Methods Enzymol. , vol.210 , pp. 192-200
    • Moffatt, D.J.1    Mantsch, H.H.2
  • 18
    • 0012601229 scopus 로고
    • Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance
    • 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.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 1406-1410
    • Wallace, B.A.1    Kohl, N.2    Teeter, M.M.3
  • 19
    • 0021844629 scopus 로고
    • Secondary structure and assembly mechanism of an oligomeric channel protein
    • Tobkes, N., Wallace, B. A. & Bayley, H. (1985) Secondary structure and assembly mechanism of an oligomeric channel protein, Biochemistry 24, 1915-1920.
    • (1985) Biochemistry , vol.24 , pp. 1915-1920
    • Tobkes, N.1    Wallace, B.A.2    Bayley, H.3
  • 20
    • 0002940495 scopus 로고
    • Studies of theoretical circular dichroism of polypeptides: Contributions of β turns
    • (Blont, E. R., Bovery, F. A., Goodman, M. & Lotan, N., eds) Wiley, New York
    • Woody, R. (1974) Studies of theoretical circular dichroism of polypeptides: contributions of β turns, in Peptides, polypeptides and proteins (Blont, E. R., Bovery, F. A., Goodman, M. & Lotan, N., eds) pp. 338-350, Wiley, New York.
    • (1974) Peptides, Polypeptides and Proteins , pp. 338-350
    • Woody, R.1
  • 21
    • 0025350848 scopus 로고
    • Structural studies with the uveopathogenic peptide M derived from retinal S-antigen
    • 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.
    • (1990) Biochemistry , vol.29 , pp. 2925-2930
    • Muga, A.1    Surewicz, W.K.2    Wong, P.T.T.3    Mantsch, H.H.4
  • 22
    • 0026731832 scopus 로고
    • Conformation of magainin-2 and related in aqueous solution and membrane environments proved by Fourier transform infrared spectroscopy
    • 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.
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Mantsch, H.H.2    Spencer, J.H.3
  • 23
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • 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.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goñi, F.M.4    Wilschut, J.5
  • 24
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • 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.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 25
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. J. & Fasman, G. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.J.1    Fasman, G.2
  • 26
    • 0025253204 scopus 로고
    • Design and synthesis of basic peptides having amphipathic β-structure and their interaction with phospholipid membranes
    • Ono, S., Lee, S., Mihara, H., Aoyagi, H., Kato, T. & Yamasaki, N. (1990) Design and synthesis of basic peptides having amphipathic β-structure and their interaction with phospholipid membranes, Biochim. Biophys. Acta 1022, 237-244.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 237-244
    • Ono, S.1    Lee, S.2    Mihara, H.3    Aoyagi, H.4    Kato, T.5    Yamasaki, N.6
  • 27
    • 0017822448 scopus 로고
    • Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins
    • Woody, R. W. (1978) Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins, Biopolymers 17, 1451-1467.
    • (1978) Biopolymers , vol.17 , pp. 1451-1467
    • Woody, R.W.1
  • 28
    • 0023847752 scopus 로고
    • Lipid-induced changes in the secondary structure of snake venom cardiotoxins
    • 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.
    • (1988) J. Biol. Chem. , vol.263 , pp. 786-790
    • Surewicz, W.K.1    Stepanik, T.M.2    Szabo, A.G.3    Mantsch, H.H.4
  • 30
    • 0025952118 scopus 로고
    • Amphipathic β structure of a leucine-rich repeat peptide
    • Krantz, D. D., Zidovetzki, R., Kagan, B. L. & Zipursky, S. L. (1991) Amphipathic β structure of a leucine-rich repeat peptide, J. Biol. Chem. 266, 16 801-16 807.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16801-16807
    • Krantz, D.D.1    Zidovetzki, R.2    Kagan, B.L.3    Zipursky, S.L.4
  • 32
    • 0027484593 scopus 로고
    • Orientation of fusion-active synthetic peptides in phospholipids bilayers: Determination by Fourier transform infrared spectroscopy
    • 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.
    • (1993) Biochemistry , vol.32 , pp. 9792-9797
    • Ishiguro, R.1    Kimura, N.2    Takahashi, S.3
  • 34
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • 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.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, F.W.3
  • 36
    • 0025761657 scopus 로고
    • Cytolytic pore-forming proteins and peptides: Is there a common structural motif?
    • 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.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 225-229
    • Ojcius, D.M.1    Young, J.D.-E.2
  • 37
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • 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.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 38
    • 0024440709 scopus 로고
    • Circular dichroism studies on synthetic signal peptides indicate β-conformation as a common structural feature in a highly hydrophobic environment
    • Reddy, G. L. & Nagaraj, R. (1989) Circular dichroism studies on synthetic signal peptides indicate β-conformation as a common structural feature in a highly hydrophobic environment, J. Biol. Chem. 264, 16591-16597.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16591-16597
    • Reddy, G.L.1    Nagaraj, R.2
  • 39
    • 0002843412 scopus 로고
    • Model for the protein arrangement in HBsAg particles based on physical and chemical studies
    • (Zuckerman, A. J., ed.) Alan R. Liss, Inc., New York
    • 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.
    • (1988) Viral Hepatitis and Liver Disease , pp. 606-613
    • Guerrero, E.1    Gavilanes, F.2    Peterson, D.L.3
  • 40
    • 0029887665 scopus 로고    scopus 로고
    • Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line
    • 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.
    • (1996) J. Virol. , vol.70 , pp. 2277-2285
    • Lu, X.1    Block, T.M.2    Gerlich, W.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.