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Volumn 123, Issue 5, 1998, Pages 790-797

Interaction and orientation of an α-aminoisobutyric acid- and tryptophan-containing short helical peptide pore-former in phospholipid vesicles, as revealed by fluorescence spectroscopy

Author keywords

Fluorescence quenching; Gramicidin b Aib analogue (GBA); Helical peptide pore former; Peptide lipid interaction; Vesicle surface adsorption

Indexed keywords

2 AMINO 2 METHYLPROPIONIC ACID; GRAMICIDIN B; ION CHANNEL; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; TRYPTOPHAN;

EID: 0031970684     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022006     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane α-helices as autonomous folding domains
    • Popot, J.-L. (1993) Integral membrane protein structure: transmembrane α-helices as autonomous folding domains. Curr. Opinion Struct. Biol. 3, 532-540
    • (1993) Curr. Opinion Struct. Biol. , vol.3 , pp. 532-540
    • Popot, J.-L.1
  • 2
    • 0001913674 scopus 로고
    • Folding and assembly of integral membrane proteins: An introduction
    • (White, S.H., ed.) Oxford University Press, New York
    • Popot, J.-L., De Vitry, C., and Atteia, A. (1994) Folding and assembly of integral membrane proteins: an introduction in Membrane Protein Structure: Experimental Approaches (White, S.H., ed.) pp. 41-96, Oxford University Press, New York
    • (1994) Membrane Protein Structure: Experimental Approaches , pp. 41-96
    • Popot, J.-L.1    De Vitry, C.2    Atteia, A.3
  • 3
    • 0024848780 scopus 로고
    • The structure of ion channels in membranes of excitable membranes
    • Unwin, N. (1989) The structure of ion channels in membranes of excitable membranes. Neuron 3, 665-676
    • (1989) Neuron , vol.3 , pp. 665-676
    • Unwin, N.1
  • 4
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • Sansom, M.S.P. (1991) The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 55, 139-235
    • (1991) Prog. Biophys. Mol. Biol. , vol.55 , pp. 139-235
    • Sansom, M.S.P.1
  • 6
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • Woolley, G.A. and Wallace, B.A. (1993) Model ion channels: gramicidin and alamethicin. J. Membr. Biol. 129, 109-136
    • (1993) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 7
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J.D., Wasserman, Z.R., and DeGrado, W.F. (1988) Synthetic amphiphilic peptide models for protein ion channels. Science 240, 1177-1181
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 8
    • 0020697109 scopus 로고
    • Alamethicin pore formation: Voltage-dependent flip-flop of α-helix dipoles
    • Boheim, G., Hanke, W., and Jung, G. (1983) Alamethicin pore formation: voltage-dependent flip-flop of α-helix dipoles. Biophys. Struct. Mech. 9, 181-191
    • (1983) Biophys. Struct. Mech. , vol.9 , pp. 181-191
    • Boheim, G.1    Hanke, W.2    Jung, G.3
  • 9
    • 0015767632 scopus 로고
    • An obligatory α-helical amino acid residue
    • Burgess, A.W. and Leach, S.J. (1973) An obligatory α-helical amino acid residue. Biopolymers 12, 2599-2605
    • (1973) Biopolymers , vol.12 , pp. 2599-2605
    • Burgess, A.W.1    Leach, S.J.2
  • 10
    • 0001210551 scopus 로고
    • Non-standard amino acids in peptide design and protein engineering
    • Balaram, P. (1992) Non-standard amino acids in peptide design and protein engineering. Curr. Opinion Struct. Biol. 2, 845-851
    • (1992) Curr. Opinion Struct. Biol. , vol.2 , pp. 845-851
    • Balaram, P.1
  • 11
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R.E. and White, S.H. (1989) The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry 28, 3421-3437
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 12
    • 0027170648 scopus 로고
    • Membrane partitioning: Distinguishing bilayer effects from the hydrophobic effect
    • Wimley, W.C. and White, S.H. (1993) Membrane partitioning: distinguishing bilayer effects from the hydrophobic effect. Biochemistry 32, 6307-6312
    • (1993) Biochemistry , vol.32 , pp. 6307-6312
    • Wimley, W.C.1    White, S.H.2
  • 13
    • 0005384356 scopus 로고
    • The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas vlridis
    • Deisenhofer, J. and Michel, H. (1989) The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas vlridis. EMBO J. 8, 2149-2170
    • (1989) EMBO J. , vol.8 , pp. 2149-2170
    • Deisenhofer, J.1    Michel, H.2
  • 14
    • 0028140564 scopus 로고
    • Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution
    • Kreusch, A., Neubüser, A., Schiltz, E., Weckesser, J., and Schultz, G.E. (1994) Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci. 3, 58-63
    • (1994) Protein Sci. , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubüser, A.2    Schiltz, E.3    Weckesser, J.4    Schultz, G.E.5
  • 15
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel
    • Hu, W., Lee, K.-C., and Cross, T.A. (1993) Tryptophans in membrane proteins: indole ring orientations and functional implications in the gramicidin channel. Biochemistry 32, 7035-7047
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.-C.2    Cross, T.A.3
  • 16
    • 37049073063 scopus 로고
    • Conformational studies and pore-forming properties of an α-aminoisobutyric acid analogue of gramicidin B
    • Jelokhani-Niaraki, M., Kodama, H., Ehara, T., and Kondo, M. (1995) Conformational studies and pore-forming properties of an α-aminoisobutyric acid analogue of gramicidin B. J. Chem. Soc. Perkin Trans. 2, 801-808
    • (1995) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 801-808
    • Jelokhani-Niaraki, M.1    Kodama, H.2    Ehara, T.3    Kondo, M.4
  • 18
    • 37049082263 scopus 로고
    • Changes in conformation and antimicrobial properties caused by replacement of D-amino acids with α-aminoisobutyric acid in the gramicidin backbone: Synthesis and circular dichroic studies
    • Jelokhani-Niaraki, M., Yoshioka, K., Takahashi, H., Kato, F., and Kondo, M. (1992) Changes in conformation and antimicrobial properties caused by replacement of D-amino acids with α-aminoisobutyric acid in the gramicidin backbone: synthesis and circular dichroic studies. J. Chem. Soc. Perkin Trans. 2, 1187-1193
    • (1992) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1187-1193
    • Jelokhani-Niaraki, M.1    Yoshioka, K.2    Takahashi, H.3    Kato, F.4    Kondo, M.5
  • 20
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, Magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. (1995) Translocation of a channel-forming antimicrobial peptide, Magainin 2, across lipid bilayers by forming a pore. Biochemistry 34, 6521-6526
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 21
    • 84989678914 scopus 로고
    • Photoluminescent properties of octadecylrhodamine B in micelles of low-molecular-weight detergents and water-soluble triblock copolymers
    • Nakashima, K., Fujimoto, Y., and Anzai, T. (1995) Photoluminescent properties of octadecylrhodamine B in micelles of low-molecular-weight detergents and water-soluble triblock copolymers. Photochem. Photobiol. 61, 592-599
    • (1995) Photochem. Photobiol. , vol.61 , pp. 592-599
    • Nakashima, K.1    Fujimoto, Y.2    Anzai, T.3
  • 22
    • 84989762292 scopus 로고
    • Fluorescence studies on the adsorption of octadecylrhodamine B onto a latex surface
    • Nakashima, K., Fujimoto, Y., and Kido, N. (1995) Fluorescence studies on the adsorption of octadecylrhodamine B onto a latex surface. Photochem. Photobiol. 62, 674-679
    • (1995) Photochem. Photobiol. , vol.62 , pp. 674-679
    • Nakashima, K.1    Fujimoto, Y.2    Kido, N.3
  • 23
    • 0029841008 scopus 로고    scopus 로고
    • Fluorescence quenching of 1-pyrenemethanol by methylviologen in polystyrene latex dispersions
    • Nakashima, K. and Kido, N. (1996) Fluorescence quenching of 1-pyrenemethanol by methylviologen in polystyrene latex dispersions. Photochem. Photobiol. 64, 296-302
    • (1996) Photochem. Photobiol. , vol.64 , pp. 296-302
    • Nakashima, K.1    Kido, N.2
  • 25
    • 33847798446 scopus 로고
    • Fluorencence quenching of indole and model micelle systems
    • Eftnik, M.R. and Ghiron, C.A. (1976) Fluorencence quenching of indole and model micelle systems. J. Phys. Chem. 80, 486-493
    • (1976) J. Phys. Chem. , vol.80 , pp. 486-493
    • Eftnik, M.R.1    Ghiron, C.A.2
  • 26
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftnik, M.R. and Ghiron, C.A. (1981) Fluorescence quenching studies with proteins. Anal. Biochem. 114, 199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftnik, M.R.1    Ghiron, C.A.2
  • 27
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg D., Schwarz, E., Komaromy, M., and Wall, R. (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 28
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J.-L. and Engelman, D.M. (1990) Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29, 4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 29
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber, C.M. and Li, S.-C. (1995) Peptides in membranes: helicity and hydrophobicity. Biopolymers (Peptide Sci.) 37, 295-318.
    • (1995) Biopolymers (Peptide Sci.) , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.-C.2
  • 30
    • 0029146071 scopus 로고
    • Mechanism for the modulation of membrane bilayer properties by amphipathic helical peptides
    • Epand, R.M., Shai, Y., Segrest, J.P., and Anantharamaiah, G.M. (1995) Mechanism for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers (Peptide Sci.) 37, 319-338
    • (1995) Biopolymers (Peptide Sci.) , vol.37 , pp. 319-338
    • Epand, R.M.1    Shai, Y.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 31
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols-model ion channels
    • Sansom, M.S.P. (1993) Alamethicin and related peptaibols-model ion channels. Eur. Biophys. J. 22, 105-124
    • (1993) Eur. Biophys. J. , vol.22 , pp. 105-124
    • Sansom, M.S.P.1
  • 33
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • De Kroon, A.I.P.M., Soekarjo, M.W., De Gier, J., and De Kruijff, B. (1990) The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 29, 8229-8240
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.P.M.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 34
    • 2642643268 scopus 로고
    • How a short gramicidin Aib analogue can form pores in phospholipid bilayers
    • (Ohno, M., ed.) Protein Research Foundation, Osaka
    • Jelokhani-Niaraki, M., Kodama, H., Ehara, T., and Kondo, M. (1995) How a short gramicidin Aib analogue can form pores in phospholipid bilayers in Peptide Chemistry 1994 (Ohno, M., ed.) pp. 113-116, Protein Research Foundation, Osaka
    • (1995) Peptide Chemistry 1994 , pp. 113-116
    • Jelokhani-Niaraki, M.1    Kodama, H.2    Ehara, T.3    Kondo, M.4


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