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Volumn 8, Issue 3, 1999, Pages 214-229

Interaction of Gd(III) MRI contrast agents with membranes: A review of recent EPR studies

Author keywords

EPR; Membranes; MRI contrast agents; Spin labeling

Indexed keywords

CONTRAST MEDIUM; GADOLINIUM; PENTETIC ACID DERIVATIVE;

EID: 0032850878     PISSN: 13528661     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1352-8661(99)00031-9     Document Type: Conference Paper
Times cited : (8)

References (59)
  • 4
    • 0002513979 scopus 로고
    • High-pressure 2D NOESY experiments on phospholipid vesicles
    • Jonas J., Winter R., Grandinetti P.J., Driscoll D. High-pressure 2D NOESY experiments on phospholipid vesicles. J Magn Reson. 87:1990;536-547.
    • (1990) J Magn Reson , vol.87 , pp. 536-547
    • Jonas, J.1    Winter, R.2    Grandinetti, P.J.3    Driscoll, D.4
  • 5
    • 0000055690 scopus 로고
    • Phase-transition behavior of saturated, symmetric chain phospholipid bilayer dispersions determined by raman spectroscopy: Correlation between spectral and thermodynamic parameters
    • Huang C., Lapides J.R., Levin I.W. Phase-transition behavior of saturated, symmetric chain phospholipid bilayer dispersions determined by raman spectroscopy: correlation between spectral and thermodynamic parameters. J Am Chem Soc. 104:1982;5926-5930.
    • (1982) J Am Chem Soc , vol.104 , pp. 5926-5930
    • Huang, C.1    Lapides, J.R.2    Levin, I.W.3
  • 6
    • 0017695894 scopus 로고
    • Hydrocarbon chain disorder in lipid bilayers. Temperature dependent Raman spectra of 1,2-diacylphosphatidylcholine-water cells
    • Yellin N., Levin I.W. Hydrocarbon chain disorder in lipid bilayers. Temperature dependent Raman spectra of 1,2-diacylphosphatidylcholine-water cells. Biochem Biophys Acta. 489:1977;177-190.
    • (1977) Biochem Biophys Acta , vol.489 , pp. 177-190
    • Yellin, N.1    Levin, I.W.2
  • 7
    • 0017742567 scopus 로고
    • Comment on the carbon-hydrogen stretching region of vibrational Raman spectra of phospholipids
    • Bunow M.R., Levin I.W. Comment on the carbon-hydrogen stretching region of vibrational Raman spectra of phospholipids. Biochem Biophys Acta. 489:1977;191-206.
    • (1977) Biochem Biophys Acta , vol.489 , pp. 191-206
    • Bunow, M.R.1    Levin, I.W.2
  • 8
    • 0018084142 scopus 로고
    • Laser Raman studies of molecular interactions with phosphatidylcholine multilayers. II. Effects of mono- and divalent ions on bilayer structure
    • Loshchilova E., Karvaly B. Laser Raman studies of molecular interactions with phosphatidylcholine multilayers. II. Effects of mono- and divalent ions on bilayer structure. Biochem Biophys Acta. 514:1978;274-285.
    • (1978) Biochem Biophys Acta , vol.514 , pp. 274-285
    • Loshchilova, E.1    Karvaly, B.2
  • 9
    • 4243199532 scopus 로고    scopus 로고
    • 2D NMR and FT-Raman spectroscopic studies on the interaction of lanthanide ions and Ln-DTPA with phospholipid bilayers
    • Chunbo Y., Daqing Z, Bing Z., Yijie W., Juzheng L., Jiazuan N. 2D NMR and FT-Raman spectroscopic studies on the interaction of lanthanide ions and Ln-DTPA with phospholipid bilayers. Langmuir. 12:1996;5375-5378.
    • (1996) Langmuir , vol.12 , pp. 5375-5378
    • Chunbo, Y.1    Daqing, Z.2    Bing, Z.3    Yijie, W.4    Juzheng, L.5    Jiazuan, N.6
  • 12
    • 0026697075 scopus 로고
    • Distance measurements using paramagnetic ion-induced relaxation in the saturation transfer electron spin resonance of spin-labeled biomolecules
    • Pàli T., Bartucci R., Horvàth L.I., Marsh D. Distance measurements using paramagnetic ion-induced relaxation in the saturation transfer electron spin resonance of spin-labeled biomolecules. Biophys J. 61:1992;1595-1602.
    • (1992) Biophys J , vol.61 , pp. 1595-1602
    • Pàli, T.1    Bartucci, R.2    Horvàth, L.I.3    Marsh, D.4
  • 13
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin
    • Altenbach C., Greenhalgh D.A., Khorana H.G., Hubbell W.L. A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc Natl Acad Sci USA. 91:1994;1667-1671.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 14
    • 0342354043 scopus 로고
    • Lateral phase separation in membrane lipids and the mechanism of sugar transport in Escherichia coli
    • Linden C.D., Wright K.L., McConnell H.M., Fox C.F. Lateral phase separation in membrane lipids and the mechanism of sugar transport in Escherichia coli. Proc Natl Acad Sci USA. 70:1973;2271-2275.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2271-2275
    • Linden, C.D.1    Wright, K.L.2    McConnell, H.M.3    Fox, C.F.4
  • 15
    • 0016614466 scopus 로고
    • Phase separation in phospholipid membranes
    • Wu S.H., McConnell H.M. Phase separation in phospholipid membranes. Biochemistry. 14:1975;847-854.
    • (1975) Biochemistry , vol.14 , pp. 847-854
    • Wu, S.H.1    McConnell, H.M.2
  • 16
    • 33947094307 scopus 로고
    • Analysis of the factors determining the EPR spectra of spin probes that partition between aqueous and lipid phases
    • Polnaszek C.F., Schreier S., Butler K.W., Smith I.C.P. Analysis of the factors determining the EPR spectra of spin probes that partition between aqueous and lipid phases. J Am Chem Soc. 100:1978;8223-8231.
    • (1978) J Am Chem Soc , vol.100 , pp. 8223-8231
    • Polnaszek, C.F.1    Schreier, S.2    Butler, K.W.3    Smith, I.C.P.4
  • 17
    • 0029054719 scopus 로고
    • Very high frequency electron paramagnetic resonance of 2,2,6,6-tetramethyl-1-piperidinyloxy in 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine liposomes: Partitioning and molecular dynamics
    • Smirnov A.I., Smirnova T.I., Morse II P.D. Very high frequency electron paramagnetic resonance of 2,2,6,6-tetramethyl-1-piperidinyloxy in 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine liposomes: partitioning and molecular dynamics. Biophys J. 68:1995;2350.
    • (1995) Biophys J , vol.68 , pp. 2350
    • Smirnov, A.I.1    Smirnova, T.I.2    Morse P.D. II3
  • 18
    • 33751386100 scopus 로고
    • Full determination of the rotational diffusion tensor by electron paramagnetic resonance at 250 GHz
    • Budil D.E., Earle K.A., Freed J.H. Full determination of the rotational diffusion tensor by electron paramagnetic resonance at 250 GHz. J Phys Chem. 97:1993;1294-1303.
    • (1993) J Phys Chem , vol.97 , pp. 1294-1303
    • Budil, D.E.1    Earle, K.A.2    Freed, J.H.3
  • 20
    • 0031137466 scopus 로고    scopus 로고
    • Interaction of MRI gadolinium contrast agents with phospholipid bilayers as studied by 95 GHz EPR
    • Smirnova T.I., Smirnov A.I., Belford R.L., Clarkson R.L. Interaction of MRI gadolinium contrast agents with phospholipid bilayers as studied by 95 GHz EPR. Scand Chem Acta. 51:1997;562-566.
    • (1997) Scand Chem Acta , vol.51 , pp. 562-566
    • Smirnova, T.I.1    Smirnov, A.I.2    Belford, R.L.3    Clarkson, R.L.4
  • 21
    • 0001253053 scopus 로고
    • Oxygen permeability of phosphatidylcholine-cholesterol membranes
    • Subczynski W.K., Hyde J.S., Kusumi A. Oxygen permeability of phosphatidylcholine-cholesterol membranes. Proc Natl Acad Sci USA. 86:1989;4474-4478.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4474-4478
    • Subczynski, W.K.1    Hyde, J.S.2    Kusumi, A.3
  • 22
    • 0026701965 scopus 로고
    • Oxygen diffusion-concentration product in rhodopsin as observed by a pulse ESR spin labeling method
    • Subczynski W.K., Renk G.E., Crouch R.K., Hyde J.S., Kusumi A. Oxygen diffusion-concentration product in rhodopsin as observed by a pulse ESR spin labeling method. Biophys J. 63(2):1992;573-577.
    • (1992) Biophys J , vol.63 , Issue.2 , pp. 573-577
    • Subczynski, W.K.1    Renk, G.E.2    Crouch, R.K.3    Hyde, J.S.4    Kusumi, A.5
  • 23
    • 0028343033 scopus 로고
    • Molecular organisation and dynamics in bacteriorhodopsin-rich reconstructed membranes - Discrimination of lipid environments by the oxygen transport parameter using pulse ESR spin-labeling technique
    • Ashikawa I., Yin J.-J., Subczynsli W.K., Kouyama T., Hyde J.S., Kusumi A. Molecular organisation and dynamics in bacteriorhodopsin-rich reconstructed membranes - discrimination of lipid environments by the oxygen transport parameter using pulse ESR spin-labeling technique. Biochemistry. 33:1994;4947-4952.
    • (1994) Biochemistry , vol.33 , pp. 4947-4952
    • Ashikawa, I.1    Yin, J.-J.2    Subczynsli, W.K.3    Kouyama, T.4    Hyde, J.S.5    Kusumi, A.6
  • 24
    • 0030139747 scopus 로고    scopus 로고
    • 2) method to measure oxygen permeability of phospholipid bilayers and its use to study the effects of low ethanol concentrations
    • 2) method to measure oxygen permeability of phospholipid bilayers and its use to study the effects of low ethanol concentrations. J Magn Reson B. 111:1996;149-157.
    • (1996) J Magn Reson B , vol.111 , pp. 149-157
    • Smirnov, A.I.1    Clarkson, R.B.2    Belford, R.L.3
  • 25
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach C., Marti T., Khorana H.G., Hubbell W.L. Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science. 248:1990;1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 26
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • Altenbach C., Flitsch S.L., Khorana H.B., Hubbell W.L. Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. Biochemistry. 28:1989;7806-7812.
    • (1989) Biochemistry , vol.28 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Khorana, H.B.3    Hubbell, W.L.4
  • 27
    • 0028108981 scopus 로고
    • Investigation of structure and dynamics in membrane proteins using site-directed spin labeling
    • Hubbell W.L., Altenbach C. Investigation of structure and dynamics in membrane proteins using site-directed spin labeling. Curr Opin Struct Biol. 4:1994;566-573.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 566-573
    • Hubbell, W.L.1    Altenbach, C.2
  • 28
    • 58149212601 scopus 로고
    • Rapid quantitation from inhomogeneously broadened EPR spectra by a fast convolution algorithm
    • Smirnov A.I., Belford R.L. Rapid quantitation from inhomogeneously broadened EPR spectra by a fast convolution algorithm. J Magn Reson A. 113:1995;65-73.
    • (1995) J Magn Reson a , vol.113 , pp. 65-73
    • Smirnov, A.I.1    Belford, R.L.2
  • 30
    • 0000996670 scopus 로고
    • Electron spin relaxation in aqueous solutions of gadolinium (III). aquo, cacodylate, and bovine serum albumin complexes
    • Reuben J.J. Electron spin relaxation in aqueous solutions of gadolinium (III). aquo, cacodylate, and bovine serum albumin complexes. J Phys Chem. 75:1971;3164-3167.
    • (1971) J Phys Chem , vol.75 , pp. 3164-3167
    • Reuben, J.J.1
  • 34
    • 0037617781 scopus 로고
    • Oxygen transport parameter in membranes as deduced by saturation recovery measurements of spin-lattice relaxation times of spin labels
    • Kusumi A., Subczynski W.K., Hyde J.S. Oxygen transport parameter in membranes as deduced by saturation recovery measurements of spin-lattice relaxation times of spin labels. Proc Natl Acad Sci USA. 79:1982;1854-1858.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1854-1858
    • Kusumi, A.1    Subczynski, W.K.2    Hyde, J.S.3
  • 35
    • 0000288058 scopus 로고
    • Electrostatic effects on lipid phase transitions: Membrane structure and ionic environment
    • Träube H., Eibl H. Electrostatic effects on lipid phase transitions: membrane structure and ionic environment. Proc Natl Acad Sci USA. 71:1974;214-219.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 214-219
    • Träube, H.1    Eibl, H.2
  • 36
    • 0028358508 scopus 로고
    • The effect of temperature on the respiration of cultured neural cells as studied by a novel electron paramagnetic resonance technique
    • Smirnov A.I., Norby S.-W., Weyhenmeyer J.A., Clarkson R.B. The effect of temperature on the respiration of cultured neural cells as studied by a novel electron paramagnetic resonance technique. Biochim Biophys Acta. 1200:1994;205-214.
    • (1994) Biochim Biophys Acta , vol.1200 , pp. 205-214
    • Smirnov, A.I.1    Norby, S.-W.2    Weyhenmeyer, J.A.3    Clarkson, R.B.4
  • 37
    • 0032572062 scopus 로고    scopus 로고
    • Lipid magnetic resonance imaging contrast agent interactions: A spin-labeling and multifrequency EPR study
    • Smirnova T.I., Smirnov A.I., Belford R.L., Clarkson R.B. Lipid magnetic resonance imaging contrast agent interactions: a spin-labeling and multifrequency EPR study. J Am Chem Soc. 120(20):1998;5060-5072.
    • (1998) J Am Chem Soc , vol.120 , Issue.20 , pp. 5060-5072
    • Smirnova, T.I.1    Smirnov, A.I.2    Belford, R.L.3    Clarkson, R.B.4
  • 39
    • 0000726737 scopus 로고
    • W-band (95 GHz) EPR spectroscopy of nitroxide radicals with complex proton hyperfine structures: Fast motion
    • Smirnova T.I., Smirnov A.I., Clarkson R.B., Belford R.L. W-band (95 GHz) EPR spectroscopy of nitroxide radicals with complex proton hyperfine structures: fast motion. J Phys Chem. 99:1995;9008-9016.
    • (1995) J Phys Chem , vol.99 , pp. 9008-9016
    • Smirnova, T.I.1    Smirnov, A.I.2    Clarkson, R.B.3    Belford, R.L.4
  • 41
    • 0001634199 scopus 로고    scopus 로고
    • Aqueous sample holders for high frequency electron spin resonance
    • Barnes J.P., Freed J.H. Aqueous sample holders for high frequency electron spin resonance. Rev Sci Instrum. 68:1997;2838-2846.
    • (1997) Rev Sci Instrum , vol.68 , pp. 2838-2846
    • Barnes, J.P.1    Freed, J.H.2
  • 44
    • 0019324356 scopus 로고
    • The diffusion-solubility of oxygen in lipid bilayers
    • Windrem D.A., Plachy W.Z. The diffusion-solubility of oxygen in lipid bilayers. Biochim Biophys Acta. 600:1980;655-665.
    • (1980) Biochim Biophys Acta , vol.600 , pp. 655-665
    • Windrem, D.A.1    Plachy, W.Z.2
  • 45
    • 0017253370 scopus 로고
    • Monitoring the permeability profile of lipid membranes with spin probes
    • Schreier-Muccillo S., Marsh D., Smith I.P.C. Monitoring the permeability profile of lipid membranes with spin probes. Arch Biochem Biophys. 172:1976;1-11.
    • (1976) Arch Biochem Biophys , vol.172 , pp. 1-11
    • Schreier-Muccillo, S.1    Marsh, D.2    Smith, I.P.C.3
  • 47
    • 36849112090 scopus 로고
    • ESR Rigid-Lattice Line Shape in a System of Two Interacting Spins
    • Leigh J.S. ESR Rigid-Lattice Line Shape in a System of Two Interacting Spins. J Chem Phys. 52:1970;2608-2612.
    • (1970) J Chem Phys , vol.52 , pp. 2608-2612
    • Leigh, J.S.1
  • 48
    • 0029559771 scopus 로고
    • A method for distance determination in proteins using a designated methal ion binding site and side-directed spin labeling: Evaluation with T4 lyisozyme
    • Voss J., Salwinski L., Kaback H.R., Hubbell W.L. A method for distance determination in proteins using a designated methal ion binding site and side-directed spin labeling: evaluation with T4 lyisozyme. Proc Natl Acad Sci USA. 92:1995;12295-12299.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12295-12299
    • Voss, J.1    Salwinski, L.2    Kaback, H.R.3    Hubbell, W.L.4
  • 49
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme.in solution-hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • Mchaourab H.S., Oh K.J., Fang C.J., Hubbell W.L. Conformation of T4 lysozyme.in solution-hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry. 36:1996;307-316.
    • (1996) Biochemistry , vol.36 , pp. 307-316
    • Mchaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 50
    • 0000717350 scopus 로고
    • Solvent effects on the g-value of di-t-butyl nitric oxide
    • Kawamura T., Matsunami S., Yonezawa T. Solvent effects on the g-value of di-t-butyl nitric oxide. Bull Chem Soc Jpn. 40:1967;1111-1115.
    • (1967) Bull Chem Soc Jpn , vol.40 , pp. 1111-1115
    • Kawamura, T.1    Matsunami, S.2    Yonezawa, T.3
  • 51
    • 0028281769 scopus 로고
    • 250-GHz electron spin resonance studies of polarity gradients along the aliphatic chains in phospholipid membranes
    • Earle K.A., Moscicki J.K., Ge M., Budil D.E., Freed J.H. 250-GHz electron spin resonance studies of polarity gradients along the aliphatic chains in phospholipid membranes. Biophys J. 66:1994;1213-1221.
    • (1994) Biophys J , vol.66 , pp. 1213-1221
    • Earle, K.A.1    Moscicki, J.K.2    Ge, M.3    Budil, D.E.4    Freed, J.H.5
  • 54
    • 0012959821 scopus 로고
    • 2O)] in aqueous solution - A variable pressure, temperature and magnetic field O-17 NMR study
    • 2O)] in aqueous solution - a variable pressure, temperature and magnetic field O-17 NMR study. J Phys Chem. 98:1994;53-59.
    • (1994) J Phys Chem , vol.98 , pp. 53-59
    • González, G.1    Powell, D.H.2    Tissières, V.3    Merbach, A.E.4
  • 57
    • 0001507242 scopus 로고
    • Novel contrast agent for magnetic resonance imaging - Synthesis and characterization of the ligand BOPTA and its Ln(III) complexes
    • Uggeri F., Aime S., Anelli P.L., Botta M., Brocchetta M., de Haën C., Ermondi G., Grandi M., Paoli P. Novel contrast agent for magnetic resonance imaging - synthesis and characterization of the ligand BOPTA and its Ln(III) complexes. Inorg Chem. 34:1995;633-642.
    • (1995) Inorg Chem , vol.34 , pp. 633-642
    • Uggeri, F.1    Aime, S.2    Anelli, P.L.3    Botta, M.4    Brocchetta, M.5    De Haën, C.6    Ermondi, G.7    Grandi, M.8    Paoli, P.9
  • 58
    • 0000683465 scopus 로고    scopus 로고
    • Multifreqency EPR determination of zero field splitting of high spin species in liquids: Gd(III) chelates in water
    • Clarkson R.B., Smirnov A.I., Smirnova T.I., Kang H., Belford R.L., Earle K., Freed J.H. Multifreqency EPR determination of zero field splitting of high spin species in liquids: Gd(III) chelates in water. Mol Phys. 95(6):1998;1325-1332.
    • (1998) Mol Phys , vol.95 , Issue.6 , pp. 1325-1332
    • Clarkson, R.B.1    Smirnov, A.I.2    Smirnova, T.I.3    Kang, H.4    Belford, R.L.5    Earle, K.6    Freed, J.H.7


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