메뉴 건너뛰기




Volumn 78, Issue 1, 2000, Pages 267-280

Kinetics of amphiphile association with two-phase lipid bilayer vesicles

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOPHILE; PHOSPHATIDYLCHOLINE;

EID: 0034030262     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76590-8     Document Type: Article
Times cited : (23)

References (51)
  • 1
    • 0032996357 scopus 로고    scopus 로고
    • Lipid transfer between vesicles: effect of high vesicle concentration
    • P.F.F. Almeida Lipid transfer between vesicles: effect of high vesicle concentration Biophys. J. 76 1999 1922 1928
    • (1999) Biophys. J. , vol.76 , pp. 1922-1928
    • Almeida, P.F.F.1
  • 2
    • 0026767199 scopus 로고
    • Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers: a free volume analysis
    • P.F.F. Almeida W.L.C. Vaz T.E. Thompson Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers: a free volume analysis Biochemistry 31 1992 6739 6747
    • (1992) Biochemistry , vol.31 , pp. 6739-6747
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 3
    • 0026658542 scopus 로고
    • Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer
    • P.F.F. Almeida W.L.C. Vaz T.E. Thompson Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer Biochemistry 31 1992 7198 7210
    • (1992) Biochemistry , vol.31 , pp. 7198-7210
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 4
    • 0007781972 scopus 로고
    • Theory of the kinetics of micellar equilibria and quantitative interpretation of chemical relaxation studies of micellar solutions of ionic surfactants
    • E.A.G. Aniansson S.H. Wall M. Almgren H. Hoffman I. Kielmann W. Ulbricht R. Zana J. Lang C. Tondre Theory of the kinetics of micellar equilibria and quantitative interpretation of chemical relaxation studies of micellar solutions of ionic surfactants J. Phys. Chem. 80 1976 905 922
    • (1976) J. Phys. Chem. , vol.80 , pp. 905-922
    • Aniansson, E.A.G.1    Wall, S.H.2    Almgren, M.3    Hoffman, H.4    Kielmann, I.5    Ulbricht, W.6    Zana, R.7    Lang, J.8    Tondre, C.9
  • 5
    • 0025789799 scopus 로고
    • Interaction of charged and uncharged calcium channel antagonists with phospholipid membranes. Binding equilibrium, binding enthalpy, and membrane location
    • H.-D. Bäuerle J. Seelig Interaction of charged and uncharged calcium channel antagonists with phospholipid membranes. Binding equilibrium, binding enthalpy, and membrane location Biochemistry 30 1991 7203 7211
    • (1991) Biochemistry , vol.30 , pp. 7203-7211
    • Bäuerle, H.-D.1    Seelig, J.2
  • 6
    • 3943103200 scopus 로고
    • Standard thermodynamics of transfer. Uses and misuses
    • A. Ben-Naim Standard thermodynamics of transfer. Uses and misuses J. Phys. Chem. 82 1978 792 803
    • (1978) J. Phys. Chem. , vol.82 , pp. 792-803
    • Ben-Naim, A.1
  • 7
    • 85120096958 scopus 로고
    • Linear equations, vectors, matrices, and determinants, Chap. 3, and Coordinate transformations, tensor analysis, Chap. 10
    • M.L. Boas Linear equations, vectors, matrices, and determinants, Chap. 3, and Coordinate transformations, tensor analysis, Chap. 10 2nd Ed. Mathematical Methods in the Physical Sciences 81–144 1983 John Wiley and Sons New York 407–455
    • (1983)
    • Boas, M.L.1
  • 8
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • D. Brown J.K. Rose Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface Cell 68 1992 533 544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.1    Rose, J.K.2
  • 9
    • 0001401604 scopus 로고
    • Translational diffusion of proteins and lipids in artificial lipid bilayer membranes. A comparison of experiment with theory
    • R.M. Clegg W.L.C. Vaz Translational diffusion of proteins and lipids in artificial lipid bilayer membranes. A comparison of experiment with theory A. Watts J.J.H.H.M. DePont Progress in Protein-Lipid Interactions 1 1985 Elsevier Amsterdam 173 229
    • (1985) , pp. 173-229
    • Clegg, R.M.1    Vaz, W.L.C.2
  • 10
    • 0029024469 scopus 로고
    • Permeability of dimyristoylphosphatidylcholine/dipalmitoylphosphatidylcholine bilayer membranes with coexisting gel and liquid-crystalline phases
    • S. Clerc T.E. Thompson Permeability of dimyristoylphosphatidylcholine/dipalmitoylphosphatidylcholine bilayer membranes with coexisting gel and liquid-crystalline phases Biophys. J. 68 1995 2333 2341
    • (1995) Biophys. J. , vol.68 , pp. 2333-2341
    • Clerc, S.1    Thompson, T.E.2
  • 11
    • 0026780558 scopus 로고
    • The permeability and the effect of acyl-chain length for phospholipid bilayers containing cholesterol: theory and experiment
    • E. Corvera O.G. Mouritsen M.A. Singer M.J. Zuckermann The permeability and the effect of acyl-chain length for phospholipid bilayers containing cholesterol: theory and experiment Biochim. Biophys. Acta 1107 1992 261 270
    • (1992) Biochim. Biophys. Acta , vol.1107 , pp. 261-270
    • Corvera, E.1    Mouritsen, O.G.2    Singer, M.A.3    Zuckermann, M.J.4
  • 12
    • 0023722226 scopus 로고
    • Passive ion permeability of lipid membranes modelled via lipid-domain interfacial area
    • L. Cruzeiro-Hansson O.G. Mouritson Passive ion permeability of lipid membranes modelled via lipid-domain interfacial area Biochim. Biophys. Acta 944 1988 63 72
    • (1988) Biochim. Biophys. Acta , vol.944 , pp. 63-72
    • Cruzeiro-Hansson, L.1    Mouritson, O.G.2
  • 13
    • 0002747562 scopus 로고
    • Physical properties and functional roles of lipids in membranes
    • P.R. Cullis M.J. Hope Physical properties and functional roles of lipids in membranes D.E. Vance J.E. Vance Biochemistry of Lipids and Membranes 1985 Benjamin/Cummings Menlo Park, CA 28 33
    • (1985) , pp. 28-33
    • Cullis, P.R.1    Hope, M.J.2
  • 14
    • 0024285006 scopus 로고
    • Solute partitioning into lipid bilayer membranes
    • L.R. DeYoung K.A. Dill Solute partitioning into lipid bilayer membranes Biochemistry 27 1988 5281 5289
    • (1988) Biochemistry , vol.27 , pp. 5281-5289
    • DeYoung, L.R.1    Dill, K.A.2
  • 16
    • 0030822255 scopus 로고    scopus 로고
    • Lipid microdomains in cell surface membranes
    • M. Edidin Lipid microdomains in cell surface membranes Curr. Opin. Struct. Biol. 7 1997 528 532
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 528-532
    • Edidin, M.1
  • 17
    • 0040724178 scopus 로고
    • Spontaneous transfer of sphingomyelin between phospholipid bilayers
    • A. Frank Y. Barenholz D. Lichtenberg T.E. Thompson Spontaneous transfer of sphingomyelin between phospholipid bilayers Biochemistry 22 1983 5647 5651[[page end]]
    • (1983) Biochemistry , vol.22 , pp. 5647-5651[[page end]]
    • Frank, A.1    Barenholz, Y.2    Lichtenberg, D.3    Thompson, T.E.4
  • 18
    • 0003985009 scopus 로고
    • Kinetics for the Life Sciences. Receptors, Transmitters and Catalysts
    • H. Gutfreund Kinetics for the Life Sciences. Receptors, Transmitters and Catalysts 1995 Cambridge University Press Cambridge 112–118
    • (1995)
    • Gutfreund, H.1
  • 19
    • 0015528115 scopus 로고
    • Interactions of phosphatidylcholine vesicles with 2-p-toluidinylnaphthalene-6-sulfonate
    • C.-H. Huang J.P. Charlton Interactions of phosphatidylcholine vesicles with 2- p -toluidinylnaphthalene-6-sulfonate Biochemistry 11 1972 735 740
    • (1972) Biochemistry , vol.11 , pp. 735-740
    • Huang, C.-H.1    Charlton, J.P.2
  • 20
    • 0031956655 scopus 로고    scopus 로고
    • Domains in cell plasma membranes investigated by near-field scanning optical microscopy
    • J. Hwang L.A. Gheber L. Margolis M. Edidin Domains in cell plasma membranes investigated by near-field scanning optical microscopy Biophys. J. 74 1998 2184 2190
    • (1998) Biophys. J. , vol.74 , pp. 2184-2190
    • Hwang, J.1    Gheber, L.A.2    Margolis, L.3    Edidin, M.4
  • 22
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices
    • R.E. Jacobs S.H. White The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices Biochemistry 28 1989 3421 3427
    • (1989) Biochemistry , vol.28 , pp. 3421-3427
    • Jacobs, R.E.1    White, S.H.2
  • 23
    • 0025162276 scopus 로고
    • Mechanism of spontaneous, concentration-dependent phospholipid transfer between bilayers
    • J.D. Jones T.E. Thompson Mechanism of spontaneous, concentration-dependent phospholipid transfer between bilayers Biochemistry 29 1990 1593 1600
    • (1990) Biochemistry , vol.29 , pp. 1593-1600
    • Jones, J.D.1    Thompson, T.E.2
  • 24
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • W. Kauzmann Some factors in the interpretation of protein denaturation Adv. Protein Chem. 14 1959 1 63
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 25
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of 100Å using imaging fluorescence resonance energy transfer
    • A.K. Kenworthy M. Edidin Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of 100 Å using imaging fluorescence resonance energy transfer J. Cell Biol. 142 1998 69 84
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 26
    • 0027452422 scopus 로고
    • Probing biomembrane interfacial potential and pH profiles with a new type of float-like fluorophores positioned at varying distance from the membrane surface
    • R. Kraayenhof G.J. Sterk H.W. Wong Fong Sang Probing biomembrane interfacial potential and pH profiles with a new type of float-like fluorophores positioned at varying distance from the membrane surface Biochemistry 32 1993 10057 10066
    • (1993) Biochemistry , vol.32 , pp. 10057-10066
    • Kraayenhof, R.1    Sterk, G.J.2    Wong Fong Sang, H.W.3
  • 27
    • 0028933450 scopus 로고
    • Guilt by insolubility—does a protein’s detergent insolubility reflect a caveolar location?
    • T.V. Kurzchalia E. Hartmann P. Dupree Guilt by insolubility—does a protein’s detergent insolubility reflect a caveolar location? Trends Cell Biol. 5 1995 187 189
    • (1995) Trends Cell Biol. , vol.5 , pp. 187-189
    • Kurzchalia, T.V.1    Hartmann, E.2    Dupree, P.3
  • 29
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis
    • M.P. Lisanti P.E. Scherer Z. Tang M. Sargiacomo Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis Trends Cell Biol. 4 1994 231 235
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.3    Sargiacomo, M.4
  • 30
    • 0017195938 scopus 로고
    • Evidence for phase boundary lipid. Permeability of Tempo-choline into dimyristoylphosphatidylcholine vesicles at the phase transition
    • D. Marsh A. Watts P.F. Knowles Evidence for phase boundary lipid. Permeability of Tempo-choline into dimyristoylphosphatidylcholine vesicles at the phase transition Biochemistry 15 1976 3570 3578
    • (1976) Biochemistry , vol.15 , pp. 3570-3578
    • Marsh, D.1    Watts, A.2    Knowles, P.F.3
  • 31
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • S. Mayor F.R. Maxfield Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment Mol. Biol. Cell 6 1995 929 944
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 32
    • 0027104985 scopus 로고
    • Effects of domain connection and disconnection on the yields of in-plane bimolecular reactions in membranes
    • E.C. Melo I.M. Lourtie M.B. Sankaram T.E. Thompson W.L.C. Vaz Effects of domain connection and disconnection on the yields of in-plane bimolecular reactions in membranes Biophys. J. 63 1992 1506 1512
    • (1992) Biophys. J. , vol.63 , pp. 1506-1512
    • Melo, E.C.1    Lourtie, I.M.2    Sankaram, M.B.3    Thompson, T.E.4    Vaz, W.L.C.5
  • 33
    • 0022357345 scopus 로고
    • Thermodynamics and kinetics of phospholipid monomer-vesicle interaction
    • J.W. Nichols Thermodynamics and kinetics of phospholipid monomer-vesicle interaction Biochemistry 24 1985 6390 6398
    • (1985) Biochemistry , vol.24 , pp. 6390-6398
    • Nichols, J.W.1
  • 34
    • 0015795402 scopus 로고
    • Phase transitions in phospholipid vesicles. Fluorescence polarization and permeability measurements concerning the effect of temperature and cholesterol
    • D. Papahadjopoulos K. Jacobson S. Nir T. Isac Phase transitions in phospholipid vesicles. Fluorescence polarization and permeability measurements concerning the effect of temperature and cholesterol Biochim. Biophys. Acta 311 1973 330 348
    • (1973) Biochim. Biophys. Acta , vol.311 , pp. 330-348
    • Papahadjopoulos, D.1    Jacobson, K.2    Nir, S.3    Isac, T.4
  • 35
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • M.B. Sankaram T.E. Thompson Interaction of cholesterol with various glycerophospholipids and sphingomyelin Biochemistry 29 1990 10670 10675
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 37
    • 0025996974 scopus 로고
    • Nonclassical hydrophobic effect in membrane binding equilibria
    • J. Seelig P. Ganz Nonclassical hydrophobic effect in membrane binding equilibria Biochemistry 30 1991 9354 9359
    • (1991) Biochemistry , vol.30 , pp. 9354-9359
    • Seelig, J.1    Ganz, P.2
  • 38
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 39
    • 0000267310 scopus 로고
    • Versuch einer mathematischen Theorie der Koagulationskinetik kolloider Lösungen
    • M. Smoluchowski Versuch einer mathematischen Theorie der Koagulationskinetik kolloider Lösungen Z. Physik. Chem. Leipzig. 92 1917 129 168
    • (1917) Z. Physik. Chem. Leipzig. , vol.92 , pp. 129-168
    • Smoluchowski, M.1
  • 41
    • 0028293086 scopus 로고
    • Diffusion and chemical reactions in phase-separated membranes
    • W.L.C. Vaz Diffusion and chemical reactions in phase-separated membranes Biophys. Chem. 50 1994 139 145
    • (1994) Biophys. Chem. , vol.50 , pp. 139-145
    • Vaz, W.L.C.1
  • 42
    • 0029182997 scopus 로고
    • Percolation properties of two-component, two-phase phospholipid bilayers
    • W.L.C. Vaz Percolation properties of two-component, two-phase phospholipid bilayers Mol. Membr. Biol. 12 1995 39 43
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 39-43
    • Vaz, W.L.C.1
  • 43
    • 0003155927 scopus 로고    scopus 로고
    • Consequences of phase separations in membranes
    • W.L.C. Vaz Consequences of phase separations in membranes Y. Barenholz D. Lasic Non-Medical Applications of Liposomes, Models for Biological Phenomena 2 1996 CRC Press Boca Raton, FL 51 60
    • (1996) , pp. 51-60
    • Vaz, W.L.C.1
  • 44
    • 0027180191 scopus 로고
    • Phase topology and percolation in multi-phase lipid bilayers: is the biological membrane a domain mosaic?
    • W.L.C. Vaz P.F.F. Almeida Phase topology and percolation in multi-phase lipid bilayers: is the biological membrane a domain mosaic? Curr. Opin. Struct. Biol. 3 1993 482 488
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 482-488
    • Vaz, W.L.C.1    Almeida, P.F.F.2
  • 45
    • 0025128695 scopus 로고
    • Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H nuclear magnetic resonance and differential scanning calorimetry
    • 2H nuclear magnetic resonance and differential scanning calorimetry Biochemistry 29 1990 451 464
    • (1990) Biochemistry , vol.29 , pp. 451-464
    • Vist, M.R.1    Davis, J.H.2
  • 46
    • 0027941253 scopus 로고
    • Lipid domains in model and biological membranes
    • R. Welti M. Glaser Lipid domains in model and biological membranes Chem. Phys. Lipids 73 1994 121 137
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 121-137
    • Welti, R.1    Glaser, M.2
  • 47
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: determining energetics of peptide-bilayer interactions
    • S. White W.C. Wimley A.S. Ladokhin K. Hristova Protein folding in membranes: determining energetics of peptide-bilayer interactions Methods Enzymol. 295 1998 63 87
    • (1998) Methods Enzymol. , vol.295 , pp. 63-87
    • White, S.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 48
    • 0025060910 scopus 로고
    • Exchange and flip-flop of dimyristoylphosphatidylcholine in liquid-crystalline, gel, and two-component, two-phase large unilamellar vesicles
    • W.C. Wimley T.E. Thompson Exchange and flip-flop of dimyristoylphosphatidylcholine in liquid-crystalline, gel, and two-component, two-phase large unilamellar vesicles Biochemistry 29 1990 1296 1303
    • (1990) Biochemistry , vol.29 , pp. 1296-1303
    • Wimley, W.C.1    Thompson, T.E.2
  • 49
    • 0025906293 scopus 로고
    • Transbilayer and interbilayer phospholipid exchange in dimyristoylphosphatidylcholine/dimyristoylphosphatidylethanolamine large unilamellar vesicles
    • W.C. Wimley T.E. Thompson Transbilayer and interbilayer phospholipid exchange in dimyristoylphosphatidylcholine/dimyristoylphosphatidylethanolamine large unilamellar vesicles Biochemistry 30 1991 1702 1709
    • (1991) Biochemistry , vol.30 , pp. 1702-1709
    • Wimley, W.C.1    Thompson, T.E.2
  • 50
    • 0016614466 scopus 로고
    • Phase separations in phospholipid membranes
    • H.S. Wu H.M. McConnell Phase separations in phospholipid membranes Biochemistry 14 1975 847 854
    • (1975) Biochemistry , vol.14 , pp. 847-854
    • Wu, H.S.1    McConnell, H.M.2
  • 51
    • 0032489637 scopus 로고    scopus 로고
    • Phase structures of binary lipid bilayers as revealed by permeability of small molecules
    • T.-X. Xiang B.D. Anderson Phase structures of binary lipid bilayers as revealed by permeability of small molecules Biochim. Biophys. Acta 1370 1998 64 76
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 64-76
    • Xiang, T.-X.1    Anderson, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.