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Volumn 74, Issue 6, 1998, Pages 3023-3030

Structural features that modulate the transmembrane migration of a hydrophobic peptide in lipid vesicles

Author keywords

[No Author keywords available]

Indexed keywords

ALAMETHICIN; PEPTIDE;

EID: 0031835795     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)78010-5     Document Type: Article
Times cited : (21)

References (37)
  • 1
    • 0025832273 scopus 로고
    • Dynamics and aggregation of the peptide ion channel alamethicin
    • Archer, S. J., J. F. Ellena, and D. S. Cafiso. 1991. Dynamics and aggregation of the peptide ion channel alamethicin. Biophys. J. 60:389-398.
    • (1991) Biophys. J. , vol.60 , pp. 389-398
    • Archer, S.J.1    Ellena, J.F.2    Cafiso, D.S.3
  • 2
    • 0030024628 scopus 로고    scopus 로고
    • Membrane structure of voltage-gated channel forming peptides revealed by site-directed spin labeling
    • Barranger-Mathys, M., and D. S. Cafiso. 1996. Membrane structure of voltage-gated channel forming peptides revealed by site-directed spin labeling. Biochemistry. 35:498-505.
    • (1996) Biochemistry , vol.35 , pp. 498-505
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 3
    • 0029669955 scopus 로고    scopus 로고
    • Free-energy determinants of α-helix insertion into lipid bilayers
    • Ben-Tal, N., A. Ben-Shaul, A. Nicholls, and B. Honig. 1996. Free-energy determinants of α-helix insertion into lipid bilayers. Biophys. J. 70: 1803-1812.
    • (1996) Biophys. J. , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Ben-Shaul, A.2    Nicholls, A.3    Honig, B.4
  • 4
    • 0028226051 scopus 로고
    • Alamethicin: A peptide model for voltage-gating and protein membrane electrostatic interactions
    • Cafiso, D. S. 1994. Alamethicin: a peptide model for voltage-gating and protein membrane electrostatic interactions. Annu. Rev. Biophys. Biomol. Struct. 23:141-165.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 5
    • 0018073336 scopus 로고
    • Estimation of transmembrane pH gradients from phase equilibria of spin-labeled amines
    • Cafiso, D. S., and W. L. Hubbell. 1978. Estimation of transmembrane pH gradients from phase equilibria of spin-labeled amines. Biochemistry. 17:3871-3877.
    • (1978) Biochemistry , vol.17 , pp. 3871-3877
    • Cafiso, D.S.1    Hubbell, W.L.2
  • 7
    • 0020373002 scopus 로고
    • Transmembrane electrical currents of spin-labeled hydrophobic ions
    • Cafiso, D. S., and W. L. Hubbell. 1982. Transmembrane electrical currents of spin-labeled hydrophobic ions. Biophys. J. 39:263-272.
    • (1982) Biophys. J. , vol.39 , pp. 263-272
    • Cafiso, D.S.1    Hubbell, W.L.2
  • 8
    • 0017182089 scopus 로고
    • Estimation of membrane surface potential and charge density from the phase equilibrium of a paramagnetic amphiphile
    • Castle, J. D., and W. L. Hubbell. 1976. Estimation of membrane surface potential and charge density from the phase equilibrium of a paramagnetic amphiphile. Biochemistry. 15:4818-4831.
    • (1976) Biochemistry , vol.15 , pp. 4818-4831
    • Castle, J.D.1    Hubbell, W.L.2
  • 9
    • 0000745176 scopus 로고
    • Quadrupolar echo deuterium magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis, J. H., K. R. Jeffrey, M. Bloom, M. I. Valic, and T. P. Higgs. 1976. Quadrupolar echo deuterium magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42:390-394.
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 10
    • 0026019283 scopus 로고
    • The membrane interaction of amphiphilic model peptides affects phosphatidylserine headgroup and acyl chain order and dynamics. Application of the "phospholipid headgroup electrometer" concept to phosphatidylserine
    • de Kroon, A., J. A. Killian, J. de Geir, and D. Kruijff. 1991. The membrane interaction of amphiphilic model peptides affects phosphatidylserine headgroup and acyl chain order and dynamics. Application of the "phospholipid headgroup electrometer" concept to phosphatidylserine. Biochemistry. 30:1155-1162.
    • (1991) Biochemistry , vol.30 , pp. 1155-1162
    • De Kroon, A.1    Killian, J.A.2    De Geir, J.3    Kruijff, D.4
  • 11
    • 0023887910 scopus 로고
    • Localizing the nitroxide group of fatty acid and voltage sensitive spin-labels in phospholipid bilayers
    • Ellena, J. F., S. J. Archer, R. N. Dominey, B. D. Hill, and D. S. Cafiso. 1988. Localizing the nitroxide group of fatty acid and voltage sensitive spin-labels in phospholipid bilayers. Biochim. Biophys. Acta. 940:63-70.
    • (1988) Biochim. Biophys. Acta , vol.940 , pp. 63-70
    • Ellena, J.F.1    Archer, S.J.2    Dominey, R.N.3    Hill, B.D.4    Cafiso, D.S.5
  • 12
    • 0022510143 scopus 로고
    • Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins
    • Engleman, D. M., T. A. Steitz, and A. Goldman. 1986. Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15:321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engleman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 15
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He, K., S. J. Ludtke, W. T. Heller, and H. W. Huang. 1996. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71:2669-2679.
    • (1996) Biophys. J. , vol.71 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 16
    • 0000972361 scopus 로고
    • Geometric packing constraints in egg phosphatidylcholine vesicles
    • Huang, C., and J. T. Mason. 1978. Geometric packing constraints in egg phosphatidylcholine vesicles. Proc. Natl. Acad. Sci. USA. 75:308-310.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 308-310
    • Huang, C.1    Mason, J.T.2
  • 17
    • 0025889072 scopus 로고
    • Lipid-alamethicin interactions influence alamethicin orientation
    • Huang, H. W., and Y. Wu. 1991. Lipid-alamethicin interactions influence alamethicin orientation. Biophys. J. 60:1079-1087.
    • (1991) Biophys. J. , vol.60 , pp. 1079-1087
    • Huang, H.W.1    Wu, Y.2
  • 18
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • Keller, S. L., S. M. Bezrukov, S. M. Gruner, M. W. Tate, I. Vodyanoy, and V. A. Parsegian. 1993. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys. J. 65:23-27.
    • (1993) Biophys. J. , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 19
    • 0030048521 scopus 로고    scopus 로고
    • Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures
    • Keller, S. L., S. M. Gruner, and K. Gawrisch. 1996. Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures. Biochim. Biophys. Acta. 1278:241-246.
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 241-246
    • Keller, S.L.1    Gruner, S.M.2    Gawrisch, K.3
  • 20
    • 0026772321 scopus 로고
    • 13C NMR: Implications for the mechanism of gating of a voltage-dependent channel
    • 13C NMR: implications for the mechanism of gating of a voltage-dependent channel. Biochemistry. 31:5136-5144.
    • (1992) Biochemistry , vol.31 , pp. 5136-5144
    • Kelsh, L.P.1    Ellena, J.F.2    Cafiso, D.S.3
  • 21
    • 0019458461 scopus 로고
    • Voltage-dependent channels in planar lipid bilayer membranes
    • Latorre, R., and O. Alvarez. 1981. Voltage-dependent channels in planar lipid bilayer membranes. Physiol. Rev. 61:77-150.
    • (1981) Physiol. Rev. , vol.61 , pp. 77-150
    • Latorre, R.1    Alvarez, O.2
  • 22
    • 0027287709 scopus 로고
    • Import of a mitochondrial presequence into protein-free phospholipid vesicles
    • Maduke, M., and D. Roise. 1993. Import of a mitochondrial presequence into protein-free phospholipid vesicles. Nature. 260:364-367.
    • (1993) Nature , vol.260 , pp. 364-367
    • Maduke, M.1    Roise, D.2
  • 23
    • 0027385040 scopus 로고
    • Resolving the two monolayers of a lipid bilayer in giant unilamellar vesicles using deuterium magnetic resonance
    • Marassi, F. M., R. R. Shivers, and P. M. Macdonald. 1993. Resolving the two monolayers of a lipid bilayer in giant unilamellar vesicles using deuterium magnetic resonance. Biochemistry. 32:9936-9943.
    • (1993) Biochemistry , vol.32 , pp. 9936-9943
    • Marassi, F.M.1    Shivers, R.R.2    Macdonald, P.M.3
  • 24
    • 0020630619 scopus 로고
    • Alamethicin and related membrane channel forming polypeptides
    • Mathew, M. K., and P. Balaram. 1983. Alamethicin and related membrane channel forming polypeptides. Mol. Cell. Biochem. 50:47-64.
    • (1983) Mol. Cell. Biochem. , vol.50 , pp. 47-64
    • Mathew, M.K.1    Balaram, P.2
  • 25
    • 0029065501 scopus 로고
    • Translocation of a channel forming antimicrobial peptide, maganin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1995. Translocation of a channel forming antimicrobial peptide, maganin 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
  • 26
    • 0024500209 scopus 로고
    • Design and conformation of non-Aib synthetic peptides enjoying alamethicin-like ionophore activity
    • Molle, G., H. Duclohier, J. Y. Dugast, and G. Spach. 1989. Design and conformation of non-Aib synthetic peptides enjoying alamethicin-like ionophore activity. Biopolymers. 28:273-283.
    • (1989) Biopolymers , vol.28 , pp. 273-283
    • Molle, G.1    Duclohier, H.2    Dugast, J.Y.3    Spach, G.4
  • 27
    • 0343945189 scopus 로고
    • The use of spin labels for studying the structure and function of enzymes
    • Academic Press, New York
    • Morrisett, J. D. 1976. The use of spin labels for studying the structure and function of enzymes. In Spin Labeling, Theory and Applications. Academic Press, New York. 273-338.
    • (1976) Spin Labeling, Theory and Applications , pp. 273-338
    • Morrisett, J.D.1
  • 29
    • 2442767079 scopus 로고
    • Obtaining high-fidelity spin-1/2 powder spectra in anisotropic media: Phase-cycled Hahn echo spectroscopy
    • Rance, H., and A. Byrd. 1983. Obtaining high-fidelity spin-1/2 powder spectra in anisotropic media: phase-cycled Hahn echo spectroscopy. J. Magn. Reson. 52:221-240.
    • (1983) J. Magn. Reson. , vol.52 , pp. 221-240
    • Rance, H.1    Byrd, A.2
  • 30
    • 0023251067 scopus 로고
    • Alamethicin incorporation in lipid bilayers: A thermodynamic analysis
    • Rizzo, V., S. Stankowski, and G. Schwarz. 1987. Alamethicin incorporation in lipid bilayers: a thermodynamic analysis. Biochemistry. 26: 2751-2759.
    • (1987) Biochemistry , vol.26 , pp. 2751-2759
    • Rizzo, V.1    Stankowski, S.2    Schwarz, G.3
  • 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
  • 32
    • 0023056958 scopus 로고
    • Thermodynamic analysis of incorporation and aggregation in a membrane: Application to the pore forming peptide alamethicin
    • Schwarz, G., S. Stankowski, and V. Rizzo. 1986. Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore forming peptide alamethicin. Biochim. Biophys. Acta. 861:141-151.
    • (1986) Biochim. Biophys. Acta , vol.861 , pp. 141-151
    • Schwarz, G.1    Stankowski, S.2    Rizzo, V.3
  • 33
    • 0024335155 scopus 로고
    • Lipid dependence of peptide-membrane interactions. Bilayer affinity and aggregation of the peptide alamethicin
    • Stankowski, S., and G. Schwarz. 1989. Lipid dependence of peptide-membrane interactions. Bilayer affinity and aggregation of the peptide alamethicin. FEBS Lett. 250:556-560.
    • (1989) FEBS Lett. , vol.250 , pp. 556-560
    • Stankowski, S.1    Schwarz, G.2
  • 34
    • 0020586620 scopus 로고
    • Alamethicin-induced current-voltage curve asymmetry in lipid bilayers
    • Vodyanoy, I., J. E. Hall, and T. M. Balasubramanian. 1983. Alamethicin-induced current-voltage curve asymmetry in lipid bilayers. Biophys. J. 42:71-82.
    • (1983) Biophys. J. , vol.42 , pp. 71-82
    • Vodyanoy, I.1    Hall, J.E.2    Balasubramanian, T.M.3
  • 35
    • 0028013531 scopus 로고
    • Peptides in lipid bilayers: Structural and thermodynamic basis for partitioning and folding
    • White, S., and W. C. Wimley. 1994. Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding. Curr. Opin. Struct. Biol. 4:79-86.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 79-86
    • White, S.1    Wimley, W.C.2
  • 36
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • Woolley, G. A., and B. A. Wallace. 1992. Model ion channels: gramicidin and alamethicin. J. Membr. Biol. 129:109-136.
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 37
    • 0022622852 scopus 로고
    • 1H nuclear magnetic resonance cross-relaxation spectroscopy
    • 1H nuclear magnetic resonance cross-relaxation spectroscopy. Biophys. J. 49:799-783.
    • (1986) Biophys. J. , vol.49 , pp. 799-1783
    • Xu, Z.-C.1    Cafiso, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.