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Volumn 89, Issue 3, 2005, Pages 1812-1826

Effect of ion-binding and chemical phospholipid structure on the nanomechanics of lipid bilayers studied by force spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

1 PALMITOYL 2 OLEOYL 3 PHOSPHOETHANOLAMINE; DILAUROYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIOLEOYLPHOSPHATIDYLSERINE; DIPALMITOYLPHOSPHATIDYLCHOLINE; LIPID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 24144502022     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.064030     Document Type: Article
Times cited : (211)

References (51)
  • 1
    • 0025052304 scopus 로고
    • Membrane electrostatics
    • Cevc, G. 1990. Membrane electrostatics. Biochim. Biophys. Acta. 1031:311-382.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 311-382
    • Cevc, G.1
  • 2
    • 0036275087 scopus 로고    scopus 로고
    • The effect of metal cations on the phase behavior and hydration characteristics of phospholipid membranes
    • Binder, H., and O. Zschornig. 2002. The effect of metal cations on the phase behavior and hydration characteristics of phospholipid membranes. Chem. Phys. Lipids. 115:39-61.
    • (2002) Chem. Phys. Lipids , vol.115 , pp. 39-61
    • Binder, H.1    Zschornig, O.2
  • 3
    • 0020492209 scopus 로고
    • Phospholipid vesicle aggregation: Effect of monovalent and divalent ions
    • Ohki, S., N. Duzgunes, and K. Leonards. 1982. Phospholipid vesicle aggregation: effect of monovalent and divalent ions. Biochemistry. 21:2127-2133.
    • (1982) Biochemistry , vol.21 , pp. 2127-2133
    • Ohki, S.1    Duzgunes, N.2    Leonards, K.3
  • 4
    • 0021744932 scopus 로고
    • Monovalent cation-induced phospholipid vesicle aggregation: Effect of ion binding
    • Ohki, S., S. Roy, H. Ohshima, and K. Leonards. 1984. Monovalent cation-induced phospholipid vesicle aggregation: effect of ion binding. Biochemistry. 23:6126-6132.
    • (1984) Biochemistry , vol.23 , pp. 6126-6132
    • Ohki, S.1    Roy, S.2    Ohshima, H.3    Leonards, K.4
  • 5
    • 0018789682 scopus 로고
    • Adsorption of monovalent cations to bilayer membranes containing negative phospholipids
    • Eisenberg, M., T. Gresalfi, T. Riccio, and S. McLaughlin. 1979. Adsorption of monovalent cations to bilayer membranes containing negative phospholipids. Biochemistry. 18:5213-5223.
    • (1979) Biochemistry , vol.18 , pp. 5213-5223
    • Eisenberg, M.1    Gresalfi, T.2    Riccio, T.3    McLaughlin, S.4
  • 6
    • 0026000817 scopus 로고
    • Temperature- and ionic strength-induced conformational changes in the lipid head group region of liposomes as suggested by zeta potential data
    • Makino, K., T. Yamada, M. Kimura, T. Oka, H. Ohshima, and T. Kondo. 1991. Temperature- and ionic strength-induced conformational changes in the lipid head group region of liposomes as suggested by zeta potential data. Biophys. Chem. 41:175-183.
    • (1991) Biophys. Chem. , vol.41 , pp. 175-183
    • Makino, K.1    Yamada, T.2    Kimura, M.3    Oka, T.4    Ohshima, H.5    Kondo, T.6
  • 7
    • 0037678992 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl
    • Pandit, S. A., D. Bostick, and M. L. Berkowitz. 2003. Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl. Biophys. J. 84:3743-3750.
    • (2003) Biophys. J. , vol.84 , pp. 3743-3750
    • Pandit, S.A.1    Bostick, D.2    Berkowitz, M.L.3
  • 8
    • 0242290834 scopus 로고    scopus 로고
    • Mixed bilayer containing dipalmitoylphosphatidylcholine and dipalmitoylphosphati-dylserine: Lipid complexation, ion binding, and electrostatics
    • Pandit, S. A., D. Bostick, and M. L. Berkowitz. 2003. Mixed bilayer containing dipalmitoylphosphatidylcholine and dipalmitoylphosphati-dylserine: lipid complexation, ion binding, and electrostatics. Biophys. J. 85:3120-3131.
    • (2003) Biophys. J. , vol.85 , pp. 3120-3131
    • Pandit, S.A.1    Bostick, D.2    Berkowitz, M.L.3
  • 10
    • 0034694971 scopus 로고    scopus 로고
    • Supported planar bilayer formation by vesicle fusion: The interaction of phospholipid vesicles with surfaces and the effect of gramicidin on bilayer properties using atomic force microscopy
    • Leonenko, Z. V., A. Carnini, and D. T. Cramb. 2000. Supported planar bilayer formation by vesicle fusion: the interaction of phospholipid vesicles with surfaces and the effect of gramicidin on bilayer properties using atomic force microscopy. Biochim. Biophys. Acta. 1509:131-147.
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 131-147
    • Leonenko, Z.V.1    Carnini, A.2    Cramb, D.T.3
  • 11
    • 1142286435 scopus 로고    scopus 로고
    • Correlation of AFM and SFA measurements concerning the stability of supported lipid bilayers
    • Benz, M., T. Gutsmann, N. Chen, R. Tadmor, and J. Israelachvili. 2004. Correlation of AFM and SFA measurements concerning the stability of supported lipid bilayers. Biophys. J. 86:870-879.
    • (2004) Biophys. J. , vol.86 , pp. 870-879
    • Benz, M.1    Gutsmann, T.2    Chen, N.3    Tadmor, R.4    Israelachvili, J.5
  • 12
    • 0000769301 scopus 로고    scopus 로고
    • Adsorption of membrane-associated proteins to lipid bilayers studied with an atomic force microscope: Myelin basic protein and cytochrome c
    • Mueller, H., H. J. Butt, and E. Bamberg. 2000. Adsorption of membrane-associated proteins to lipid bilayers studied with an atomic force microscope: myelin basic protein and cytochrome c. J. Phys. Chem. B. 104:4552-4559.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4552-4559
    • Mueller, H.1    Butt, H.J.2    Bamberg, E.3
  • 13
    • 0036106315 scopus 로고    scopus 로고
    • Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy
    • Desmeules, P., M. Grandbois, V. A. Bondarenko, A. Yamazaki, and C. Salesse. 2002. Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy. Biophys. J. 82:3343-3350.
    • (2002) Biophys. J. , vol.82 , pp. 3343-3350
    • Desmeules, P.1    Grandbois, M.2    Bondarenko, V.A.3    Yamazaki, A.4    Salesse, C.5
  • 15
    • 0036419090 scopus 로고    scopus 로고
    • Single molecule imaging of supported planar lipid bilayer-reconstituted human insulin receptors by in situ scanning probe microscopy
    • Slade, A., J. Luh, S. Ho, and C. M. Yip. 2002. Single molecule imaging of supported planar lipid bilayer-reconstituted human insulin receptors by in situ scanning probe microscopy. J. Struct. Biol. 137:283-291.
    • (2002) J. Struct. Biol. , vol.137 , pp. 283-291
    • Slade, A.1    Luh, J.2    Ho, S.3    Yip, C.M.4
  • 16
    • 0037418463 scopus 로고    scopus 로고
    • Nanometer scale surface properties of supported lipid bilayers measured with hydrophobic and hydrophilic atomic force microscope probes
    • Schneider, J., W. Barger, and G. U. Lee. 2003. Nanometer scale surface properties of supported lipid bilayers measured with hydrophobic and hydrophilic atomic force microscope probes. Langmuir. 19:1899-1907.
    • (2003) Langmuir , vol.19 , pp. 1899-1907
    • Schneider, J.1    Barger, W.2    Lee, G.U.3
  • 17
    • 0842265937 scopus 로고    scopus 로고
    • In situ investigations of the formation of mixed supported lipid bilayers close to the phase transition temperature
    • Scantier, B., C. Breffa, O. Felix, and G. Decher. 2004. In situ investigations of the formation of mixed supported lipid bilayers close to the phase transition temperature. Nano Lett. 4:5-10.
    • (2004) Nano Lett. , vol.4 , pp. 5-10
    • Scantier, B.1    Breffa, C.2    Felix, O.3    Decher, G.4
  • 18
    • 0000832504 scopus 로고    scopus 로고
    • Anomalous plastic deformation at surfaces: Nanoindentation of gold single crystals
    • Corcoran, S. G., R. J. Colton, E. T. Lilleodden, and W. W. Gerberich. 1997. Anomalous plastic deformation at surfaces: nanoindentation of gold single crystals. Phys. Rev. B. 55:16057-16060.
    • (1997) Phys. Rev. B , vol.55 , pp. 16057-16060
    • Corcoran, S.G.1    Colton, R.J.2    Lilleodden, E.T.3    Gerberich, W.W.4
  • 20
    • 2442572104 scopus 로고    scopus 로고
    • Toward mechanical manipulations of cell membranes and membrane proteins using an atomic force microscope: An invited review
    • Ikai, A., and R. Afrin. 2003. Toward mechanical manipulations of cell membranes and membrane proteins using an atomic force microscope: an invited review. Cell Biochem. Biophys. 39:257-277.
    • (2003) Cell Biochem. Biophys. , vol.39 , pp. 257-277
    • Ikai, A.1    Afrin, R.2
  • 21
    • 0037149092 scopus 로고    scopus 로고
    • Confined liquids: Solvation forces in liquid alcohols between solid surfaces
    • Franz, V., and H. J. Butt. 2002. Confined liquids: solvation forces in liquid alcohols between solid surfaces. J. Phys. Chem. B. 106:1703-1708.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1703-1708
    • Franz, V.1    Butt, H.J.2
  • 22
    • 0032120573 scopus 로고    scopus 로고
    • Atomic force microscopy at solid-liquid interfaces
    • O'Shea, S. J., and M. E. Weiland. 1998. Atomic force microscopy at solid-liquid interfaces. Langmuir. 14:4186-4197.
    • (1998) Langmuir , vol.14 , pp. 4186-4197
    • O'Shea, S.J.1    Weiland, M.E.2
  • 23
    • 0030889693 scopus 로고    scopus 로고
    • Force titrations and ionization state sensitive imaging of functional groups in aqueous solutions by chemical force microscopy
    • Vezenov, D. V., A. Noy, L. F. Rozsnyai, and C. M. Lieber. 1997. Force titrations and ionization state sensitive imaging of functional groups in aqueous solutions by chemical force microscopy. J. Am. Chem. Soc. 119:2006-2015.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2006-2015
    • Vezenov, D.V.1    Noy, A.2    Rozsnyai, L.F.3    Lieber, C.M.4
  • 24
    • 0037059164 scopus 로고    scopus 로고
    • Probing microbial cell surface charges by atomic force microscopy
    • Ahimou, F., F. A. Denis, A. Touhami, and Y. F. Dufrene. 2002. Probing microbial cell surface charges by atomic force microscopy. Langmuir. 18:9937-9941.
    • (2002) Langmuir , vol.18 , pp. 9937-9941
    • Ahimou, F.1    Denis, F.A.2    Touhami, A.3    Dufrene, Y.F.4
  • 25
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 26
    • 2442448427 scopus 로고    scopus 로고
    • The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
    • Schlierf, M., H. Li, and J. M. Fernandez. 2004. The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques. Proc. Natl. Acad. Sci. USA. 101:7299-7304.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.2    Fernandez, J.M.3
  • 27
    • 2542577767 scopus 로고    scopus 로고
    • Characterization of the physical properties of model biomembranes at the nanometer scale with the atomic force microscope
    • Dufrene, Y. F., T. Boland, J. W. Schneider, W. R. Barger, and G. U. Lee. 1998. Characterization of the physical properties of model biomembranes at the nanometer scale with the atomic force microscope. Faraday Discuss. 111:79-94.
    • (1998) Faraday Discuss. , vol.111 , pp. 79-94
    • Dufrene, Y.F.1    Boland, T.2    Schneider, J.W.3    Barger, W.R.4    Lee, G.U.5
  • 28
    • 0037418479 scopus 로고    scopus 로고
    • Characterization of lipid bilayers and protein assemblies supported on rough surfaces by atomic force microscopy
    • Richter, R. P., and A. Brisson. 2003. Characterization of lipid bilayers and protein assemblies supported on rough surfaces by atomic force microscopy. Langmuir. 19:1632-1640.
    • (2003) Langmuir , vol.19 , pp. 1632-1640
    • Richter, R.P.1    Brisson, A.2
  • 30
    • 2942668382 scopus 로고    scopus 로고
    • Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy
    • Leonenko, Z. V., E. Finot, H. Ma, T. E. Dahms, and D. T. Cramb. 2004. Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy. Biophys. J. 86:3783-3793.
    • (2004) Biophys. J. , vol.86 , pp. 3783-3793
    • Leonenko, Z.V.1    Finot, E.2    Ma, H.3    Dahms, T.E.4    Cramb, D.T.5
  • 31
    • 33646984182 scopus 로고    scopus 로고
    • Rupture of molecular thin films observed in atomic force microscopy. II
    • Loi, S., G. Sun, V. Franz, and H. J. Butt. 2002. Rupture of molecular thin films observed in atomic force microscopy. II. Experiment. Phys. Rev. E: 66:031602/1-031602/7.
    • (2002) Experiment. Phys. Rev. E , vol.66
    • Loi, S.1    Sun, G.2    Franz, V.3    Butt, H.J.4
  • 32
    • 41349108634 scopus 로고    scopus 로고
    • Rupture of molecular thin films observed in atomic force microscopy. I. Theory
    • Butt, H. J., and V. Franz. 2002. Rupture of molecular thin films observed in atomic force microscopy. I. Theory. Phys. Rev. E. 66: 031601/1-031601/9.
    • (2002) Phys. Rev. E , vol.66
    • Butt, H.J.1    Franz, V.2
  • 34
    • 0037418429 scopus 로고    scopus 로고
    • Effect of ionic strength on two-dimensional streptavidin crystallization
    • Ratanabanangkoon, P., and A. P. Gast. 2003. Effect of ionic strength on two-dimensional streptavidin crystallization. Langmuir. 19:1794-1801.
    • (2003) Langmuir , vol.19 , pp. 1794-1801
    • Ratanabanangkoon, P.1    Gast, A.P.2
  • 35
    • 4544290164 scopus 로고    scopus 로고
    • Multistep binding of divalent cations to phospholipid bilayers: A molecular dynamics study
    • Bockmann, R. A., and H. Grubmuller, 2004. Multistep binding of divalent cations to phospholipid bilayers: a molecular dynamics study. Angew. Chem. Int. Ed. Engl. 43:1021-1024.
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 1021-1024
    • Bockmann, R.A.1    Grubmuller, H.2
  • 36
    • 0019122765 scopus 로고
    • Solubilization and reconstitution of the lactose transport system from Escherichia coli
    • Newman, M. J., and T. H. Wilson. 1980. Solubilization and reconstitution of the lactose transport system from Escherichia coli. J. Biol. Chem. 255:10583-10586.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10583-10586
    • Newman, M.J.1    Wilson, T.H.2
  • 38
    • 4544257551 scopus 로고    scopus 로고
    • Finite optical spot size and position corrections in thermal spring constant calibration
    • Proksch, R., T. E. Schaffer, J. P. Cleveland, R. C. Callahan, and M. B. Viani. 2004. Finite optical spot size and position corrections in thermal spring constant calibration. Nanotechnology. 15:1344-1350.
    • (2004) Nanotechnology , vol.15 , pp. 1344-1350
    • Proksch, R.1    Schaffer, T.E.2    Cleveland, J.P.3    Callahan, R.C.4    Viani, M.B.5
  • 39
    • 0034247718 scopus 로고    scopus 로고
    • The main phase transition of mica-supported phosphatidylcholine membranes
    • Yang, J., and J. Appleyard. 2000. The main phase transition of mica-supported phosphatidylcholine membranes. J. Phys. Chem. B. 104:8097-8100.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 8097-8100
    • Yang, J.1    Appleyard, J.2
  • 40
    • 0033514855 scopus 로고    scopus 로고
    • Liposome adhesion on mica surface studied by atomic force microscopy
    • Egawa, H., and K. Furusawa. 1999. Liposome adhesion on mica surface studied by atomic force microscopy. Langmuir. 15:1660-1666.
    • (1999) Langmuir , vol.15 , pp. 1660-1666
    • Egawa, H.1    Furusawa, K.2
  • 42
    • 16644362025 scopus 로고    scopus 로고
    • Using the atomic force microscope to study the interaction between two solid supported lipid bilayers and the influence of synapsin I
    • Pera, I., R. Stark, M. Kappl, H. J. Butt, and F. Benfenati. 2004. Using the atomic force microscope to study the interaction between two solid supported lipid bilayers and the influence of synapsin I. Biophys. J. 87:2446-2455.
    • (2004) Biophys. J. , vol.87 , pp. 2446-2455
    • Pera, I.1    Stark, R.2    Kappl, M.3    Butt, H.J.4    Benfenati, F.5
  • 43
    • 0026038548 scopus 로고
    • Electrostatic interaction in atomic force microscopy
    • Butt, H. J. 1991. Electrostatic interaction in atomic force microscopy. Biophys. J. 60:777-785.
    • (1991) Biophys. J. , vol.60 , pp. 777-785
    • Butt, H.J.1
  • 44
    • 0000065270 scopus 로고    scopus 로고
    • Hydrogen bonding of water to phosphatidylcholine in the membrane as studied by a molecular dynamics simulation: Location, geometry, and lipid-lipid bridging via hydrogen-bonded water
    • Pasenkiewicz-Gierula, M., Y. Takaoka, H. Miyagawa, K. Kitamura, and A. Kusumi. 1997. Hydrogen bonding of water to phosphatidylcholine in the membrane as studied by a molecular dynamics simulation: location, geometry, and lipid-lipid bridging via hydrogen-bonded water. J. Phys. Chem. A. 101:3677-3691.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3677-3691
    • Pasenkiewicz-Gierula, M.1    Takaoka, Y.2    Miyagawa, H.3    Kitamura, K.4    Kusumi, A.5
  • 45
    • 0033015372 scopus 로고    scopus 로고
    • Charge pairing of headgroups in phosphatidylcholine membranes: A molecular dynamics simulation study
    • Pasenkiewicz-Gierula, M., Y. Takaoka, H. Miyagawa, K. Kitamura, and A. Kusumi. 1999. Charge pairing of headgroups in phosphatidylcholine membranes: a molecular dynamics simulation study. Biophys. J. 76:1228-1240.
    • (1999) Biophys. J. , vol.76 , pp. 1228-1240
    • Pasenkiewicz-Gierula, M.1    Takaoka, Y.2    Miyagawa, H.3    Kitamura, K.4    Kusumi, A.5
  • 47
    • 0021972793 scopus 로고
    • Direct measurements of forces between phosphatidylcholine and phosphatidylethanolamine bilayers in aqueous electrolyte solutions
    • Marra, J., and J. Israelachvili. 1985. Direct measurements of forces between phosphatidylcholine and phosphatidylethanolamine bilayers in aqueous electrolyte solutions. Biochemistry. 24:4608-4618.
    • (1985) Biochemistry , vol.24 , pp. 4608-4618
    • Marra, J.1    Israelachvili, J.2
  • 48
    • 0036923942 scopus 로고    scopus 로고
    • Structure of gel phase DMPC determined by x-ray diffraction
    • Tristram-Nagle, S., Y. Liu, J. Legleiter, and J. F. Nagle. 2002. Structure of gel phase DMPC determined by x-ray diffraction. Biophys. J. 83:3324-3335.
    • (2002) Biophys. J. , vol.83 , pp. 3324-3335
    • Tristram-Nagle, S.1    Liu, Y.2    Legleiter, J.3    Nagle, J.F.4
  • 49
    • 0030881877 scopus 로고    scopus 로고
    • Effect of n-alkanols on lipid bilayer hydration
    • Ho, C., and C. D. Stubbs. 1997. Effect of n-alkanols on lipid bilayer hydration. Biochemistry. 36:10630-10637.
    • (1997) Biochemistry , vol.36 , pp. 10630-10637
    • Ho, C.1    Stubbs, C.D.2
  • 50
    • 85040875608 scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Johnson, K. L. 1985. Contact Mechanics. Cambridge University Press, Cambridge, UK.
    • (1985) Contact Mechanics
    • Johnson, K.L.1
  • 51
    • 0036212691 scopus 로고    scopus 로고
    • Molecular dynamics simulation of dipalmitoylphosphatidylserine bilayer with Na+ counterions
    • Pandit, S. A., and M. L. Berkowitz. 2002. Molecular dynamics simulation of dipalmitoylphosphatidylserine bilayer with Na+ counterions. Biophys. J. 82:1818-1827.
    • (2002) Biophys. J. , vol.82 , pp. 1818-1827
    • Pandit, S.A.1    Berkowitz, M.L.2


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