메뉴 건너뛰기




Volumn 91, Issue 8, 2006, Pages 2919-2927

Poly-L-lysine-induced morphology changes in mixed anionic/zwitterionic and neat zwitterionic-supported phospholipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOLYTE; LIPOSOME; PHOSPHOLIPID; POLYLYSINE;

EID: 33749526302     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.082479     Document Type: Article
Times cited : (20)

References (73)
  • 1
    • 0032763121 scopus 로고    scopus 로고
    • Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: Theory and experiment
    • Murray, D., A. Arbuzova, G. Hangyas-Mihalyne, A. Gambhir, N. Ben-Tal, B. Honig, and S. McLaughlin. 1999. Electrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experiment. Biophys. J. 77:3176-3188.
    • (1999) Biophys. J. , vol.77 , pp. 3176-3188
    • Murray, D.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    Gambhir, A.4    Ben-Tal, N.5    Honig, B.6    McLaughlin, S.7
  • 2
    • 0038476268 scopus 로고    scopus 로고
    • Phospholipid membranes as substrates for polymer adsorption
    • Xie, A. F., and S. Granick. 2002. Phospholipid membranes as substrates for polymer adsorption. Nat. Mater. 1:129-133.
    • (2002) Nat. Mater. , vol.1 , pp. 129-133
    • Xie, A.F.1    Granick, S.2
  • 3
    • 0346634895 scopus 로고    scopus 로고
    • In vitro cytotoxicity testing of polycations: Influence of polymer structure on cell viability and hemolysis
    • Fischer, D., Y. Li, B. Ahlemeyer, J. Krieglstein, and T. Kissel. 2003. In vitro cytotoxicity testing of polycations: influence of polymer structure on cell viability and hemolysis. Biomaterials. 24:1121-1131.
    • (2003) Biomaterials , vol.24 , pp. 1121-1131
    • Fischer, D.1    Li, Y.2    Ahlemeyer, B.3    Krieglstein, J.4    Kissel, T.5
  • 4
    • 7644222023 scopus 로고    scopus 로고
    • Binding and insertion of α-helical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations
    • Kandasamy, S. K., and R. G. Larson. 2004. Binding and insertion of α-helical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations. Chem. Phys. Lipids. 132:113-132.
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 113-132
    • Kandasamy, S.K.1    Larson, R.G.2
  • 5
    • 28444450556 scopus 로고    scopus 로고
    • Coexistence of a two-states organization for a cell-penetrating peptide in lipid bilayer
    • Plenat, T., S. Boichot, P. Dosset, P.-E. Milhiet, and C. Le Grimellec. 2005. Coexistence of a two-states organization for a cell-penetrating peptide in lipid bilayer. Biophys. J. 89:4300-4309.
    • (2005) Biophys. J. , vol.89 , pp. 4300-4309
    • Plenat, T.1    Boichot, S.2    Dosset, P.3    Milhiet, P.-E.4    Le Grimellec, C.5
  • 6
    • 0040291808 scopus 로고    scopus 로고
    • Formation of domains of cationic or anionic lipids in binary lipid mixtures increases the electrostatic coupling strength of water-soluble proteins to supported bilayers
    • Kasbauer, M., and T. M. Bayerl. 1999. Formation of domains of cationic or anionic lipids in binary lipid mixtures increases the electrostatic coupling strength of water-soluble proteins to supported bilayers. Biochemistry. 38:15258-15263.
    • (1999) Biochemistry , vol.38 , pp. 15258-15263
    • Kasbauer, M.1    Bayerl, T.M.2
  • 7
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: Scientific and practical applications
    • Sackmann, E. 1996. Supported membranes: scientific and practical applications. Science. 71:43-48.
    • (1996) Science , vol.71 , pp. 43-48
    • Sackmann, E.1
  • 8
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • Tanaka, M., and E. Sackmann. 2005. Polymer-supported membranes as models of the cell surface. Nature. 437:656-663.
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 9
    • 0034081731 scopus 로고    scopus 로고
    • Two photon fluorescence microscopy of coexisting lipid domains in giant unilamellar vesicles of binary phospholipid mixtures
    • Bagatolli, L. A., and E. Gratton. 2000. Two photon fluorescence microscopy of coexisting lipid domains in giant unilamellar vesicles of binary phospholipid mixtures. Biophys. J. 78:290-305.
    • (2000) Biophys. J. , vol.78 , pp. 290-305
    • Bagatolli, L.A.1    Gratton, E.2
  • 10
    • 0034702838 scopus 로고    scopus 로고
    • Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS
    • Arbuzova, A., L. Wang, J. Wang, G. Hangyas-Mihalyne, D. Murray, B. Honig, and S. McLaughlin. 2000. Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. Biochemistry. 39:10330-10339.
    • (2000) Biochemistry , vol.39 , pp. 10330-10339
    • Arbuzova, A.1    Wang, L.2    Wang, J.3    Hangyas-Mihalyne, G.4    Murray, D.5    Honig, B.6    McLaughlin, S.7
  • 11
    • 0001378233 scopus 로고    scopus 로고
    • Giant vesicles: Imitating the cytological processes of cell membranes
    • Menger, F. M., and M. I. Angelova. 1998. Giant vesicles: imitating the cytological processes of cell membranes. Acc. Chem. Res. 31:789-797.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 789-797
    • Menger, F.M.1    Angelova, M.I.2
  • 12
    • 0032477992 scopus 로고    scopus 로고
    • Asymmetric molecular friction in supported phospholipid bilayers revealed by NMR measurements of lipid diffusion
    • Hetzer, M., S. Heinz, S. Grage, and T. M. Bayerl. 1998. Asymmetric molecular friction in supported phospholipid bilayers revealed by NMR measurements of lipid diffusion. Langmuir. 14:982-984.
    • (1998) Langmuir , vol.14 , pp. 982-984
    • Hetzer, M.1    Heinz, S.2    Grage, S.3    Bayerl, T.M.4
  • 13
    • 0039090584 scopus 로고    scopus 로고
    • Effect of cationic lipids in the formation of asymmetries in supported bilayers
    • Kasbauer, M., M. Junglas, and T. M. Bayerl. 1999. Effect of cationic lipids in the formation of asymmetries in supported bilayers. Biophys. J. 76:2600-2605.
    • (1999) Biophys. J. , vol.76 , pp. 2600-2605
    • Kasbauer, M.1    Junglas, M.2    Bayerl, T.M.3
  • 14
    • 11844273222 scopus 로고    scopus 로고
    • On the effect of the solid support on the interleaflet distribution of lipids in supported lipid bilayers
    • Richter, R. P., N. Maury, and A. R. Brisson. 2005. On the effect of the solid support on the interleaflet distribution of lipids in supported lipid bilayers. Langmuir. 21:299-304.
    • (2005) Langmuir , vol.21 , pp. 299-304
    • Richter, R.P.1    Maury, N.2    Brisson, A.R.3
  • 15
    • 3142714535 scopus 로고    scopus 로고
    • Materials science of the gel to fluid phase transition in a supported phospholipid bilayer
    • Xie, A. F., R. Yamada, A. A. Gewirth, and S. Granick. 2002. Materials science of the gel to fluid phase transition in a supported phospholipid bilayer. Phys. Rev. Lett. 89:246103/246101-246103/246104.
    • (2002) Phys. Rev. Lett. , vol.89
    • Xie, A.F.1    Yamada, R.2    Gewirth, A.A.3    Granick, S.4
  • 16
    • 0035917264 scopus 로고    scopus 로고
    • Location of cholesterol in DMPC membranes. A comparative study by neutron diffraction and molecular mechanics simulation
    • Leonard, A., C. Escrive, M. Laguerre, E. Pebay-Peyroula, W. Neri, T. Pott, J. Katsaras, and E. J. Dufourc. 2001. Location of cholesterol in DMPC membranes. A comparative study by neutron diffraction and molecular mechanics simulation. Langmuir. 17:2019-2030.
    • (2001) Langmuir , vol.17 , pp. 2019-2030
    • Leonard, A.1    Escrive, C.2    Laguerre, M.3    Pebay-Peyroula, E.4    Neri, W.5    Pott, T.6    Katsaras, J.7    Dufourc, E.J.8
  • 18
    • 0036238014 scopus 로고    scopus 로고
    • Chemical control of phospholipid distribution across bilayer membranes
    • Boon, J. M., and B. D. Smith. 2002. Chemical control of phospholipid distribution across bilayer membranes. Med. Res. Rev. 22:251-281.
    • (2002) Med. Res. Rev. , vol.22 , pp. 251-281
    • Boon, J.M.1    Smith, B.D.2
  • 19
    • 0023873894 scopus 로고
    • Studies on sickled erythrocytes provide evidence that the asymmetric distribution of phosphatidylserine in the red cell membrane is maintained by both ATP-dependent translocation and interaction with membrane skeletal proteins
    • Middelkoop, E., B. H. Lubin, E. M. Bevers, J. A. Op den Kamp, P. Comfurius, D. T. Chiu, R. F. Zwaal, L. L. van Deenen, and B. Roelofsen. 1988. Studies on sickled erythrocytes provide evidence that the asymmetric distribution of phosphatidylserine in the red cell membrane is maintained by both ATP-dependent translocation and interaction with membrane skeletal proteins. Biochim. Biophys. Acta. 937:281-288.
    • (1988) Biochim. Biophys. Acta , vol.937 , pp. 281-288
    • Middelkoop, E.1    Lubin, B.H.2    Bevers, E.M.3    Op Den Kamp, J.A.4    Comfurius, P.5    Chiu, D.T.6    Zwaal, R.F.7    Van Deenen, L.L.8    Roelofsen, B.9
  • 20
    • 33646148481 scopus 로고    scopus 로고
    • Lipid asymmetry in DLPC/DSPC-supported lipid bilayers: A combined AFM and fluorescence microscopy study
    • Lin, W.-C., C. D. Blanchette, T. V. Ratto, and M. L. Longo. 2006. Lipid asymmetry in DLPC/DSPC-supported lipid bilayers: a combined AFM and fluorescence microscopy study. Biophys. J. 90:228-237.
    • (2006) Biophys. J. , vol.90 , pp. 228-237
    • Lin, W.-C.1    Blanchette, C.D.2    Ratto, T.V.3    Longo, M.L.4
  • 21
    • 0021185107 scopus 로고
    • Asymmetric lipid fluidity in human erythrocyte membrane: New spin-label evidence
    • Seigneuret, M., A. Zachowski, A. Hermann, and P. F. Devaux. 1984. Asymmetric lipid fluidity in human erythrocyte membrane: new spin-label evidence. Biochemistry. 23:4271-4275.
    • (1984) Biochemistry , vol.23 , pp. 4271-4275
    • Seigneuret, M.1    Zachowski, A.2    Hermann, A.3    Devaux, P.F.4
  • 22
    • 0027396671 scopus 로고
    • Phospholipid transmembrane domains and lateral diffusion in fibroblasts
    • Chahine, J. M. E. H., S. Cribier, and P. F. Devaux. 1993. Phospholipid transmembrane domains and lateral diffusion in fibroblasts. Proc. Natl. Acad. Sci. USA. 90:447-451.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 447-451
    • Chahine, J.M.E.H.1    Cribier, S.2    Devaux, P.F.3
  • 23
    • 1842588912 scopus 로고    scopus 로고
    • Transmembrane asymmetry and lateral domains in biological membranes
    • Devaux, P. F., and R. Morris. 2004. Transmembrane asymmetry and lateral domains in biological membranes. Traffic. 5:241-246.
    • (2004) Traffic , vol.5 , pp. 241-246
    • Devaux, P.F.1    Morris, R.2
  • 24
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • Pike, L. J. 2003. Lipid rafts: bringing order to chaos. J. Lipid Res. 44:655-667.
    • (2003) J. Lipid Res. , vol.44 , pp. 655-667
    • Pike, L.J.1
  • 25
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch, S. L., and S. L. Keller. 2003. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys. J. 85:3074-3083.
    • (2003) Biophys. J. , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 26
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 27
    • 0037429735 scopus 로고    scopus 로고
    • Role of cholesterol in lipid raft formation: Lessons from lipid model systems
    • Silvius, J. R. 2003. Role of cholesterol in lipid raft formation: lessons from lipid model systems. Biochim. Biophys. Acta. 1610:174-183.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 174-183
    • Silvius, J.R.1
  • 28
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 29
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson, K., E. D. Sheets, and R. Simson. 1995. Revisiting the fluid mosaic model of membranes. Science. 268:1441-1442.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 30
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: Different pathways, common approaches
    • McMahon, H. T., and I. G. Mills. 2004. COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr. Opin. Cell Biol. 16:379-391.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 31
    • 28444479505 scopus 로고    scopus 로고
    • Role of cholesterol and lipid organization in disease
    • Maxfield, F. R., and I. Tabas. 2005. Role of cholesterol and lipid organization in disease. Nature. 438:612-621.
    • (2005) Nature , vol.438 , pp. 612-621
    • Maxfield, F.R.1    Tabas, I.2
  • 32
    • 0035799334 scopus 로고    scopus 로고
    • Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif
    • Hinderliter, A., P. F. F. Almeida, C. E. Creutz, and R. L. Biltonen. 2001. Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif. Biochemistry. 40:4181-4191.
    • (2001) Biochemistry , vol.40 , pp. 4181-4191
    • Hinderliter, A.1    Almeida, P.F.F.2    Creutz, C.E.3    Biltonen, R.L.4
  • 33
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons, K., and R. Ehehalt. 2002. Cholesterol, lipid rafts, and disease. J. Clin. Invest. 110:597-603.
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 34
    • 0031927361 scopus 로고    scopus 로고
    • Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: An electrostatic model and experimental results
    • Denisov, G., S. Wanaski, P. Luan, M. Glaser, and S. McLaughlin. 1998. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results. Biophys. J. 74:731-744.
    • (1998) Biophys. J. , vol.74 , pp. 731-744
    • Denisov, G.1    Wanaski, S.2    Luan, P.3    Glaser, M.4    McLaughlin, S.5
  • 35
    • 0034747216 scopus 로고    scopus 로고
    • 2H NMR-observable domains in phosphatidylserine/phosphatidylcholine lipid bilayers
    • 2H NMR-observable domains in phosphatidylserine/phosphatidylcholine lipid bilayers. Biophys. J. 81:3346-3362.
    • (2001) Biophys. J. , vol.81 , pp. 3346-3362
    • Franzin, C.M.1    Macdonald, P.M.2
  • 36
  • 37
    • 0033807597 scopus 로고    scopus 로고
    • Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes
    • May, S., D. Harries, and A. Ben-Shaul. 2000. Lipid demixing and protein-protein interactions in the adsorption of charged proteins on mixed membranes. Biophys. J. 79:1747-1760.
    • (2000) Biophys. J. , vol.79 , pp. 1747-1760
    • May, S.1    Harries, D.2    Ben-Shaul, A.3
  • 39
    • 0037128111 scopus 로고    scopus 로고
    • Reversibility of structural rearrangements in the negative vesicular membrane upon electrostatic adsorption/desorption of the polycation
    • Yaroslavov, A. A., A. A. Efimova, V. I. Lobyshev, and V. A. Kabanov. 2002. Reversibility of structural rearrangements in the negative vesicular membrane upon electrostatic adsorption/desorption of the polycation. Biochim.Biophys. Acta. 1560:14-24.
    • (2002) Biochim. Biophys. Acta , vol.1560 , pp. 14-24
    • Yaroslavov, A.A.1    Efimova, A.A.2    Lobyshev, V.I.3    Kabanov, V.A.4
  • 40
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin, S., and D. Murray. 2005. Plasma membrane phosphoinositide organization by protein electrostatics. Nature. 438:605-611.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 41
    • 7044241296 scopus 로고    scopus 로고
    • Do proteins facilitate the formation of cholesterol-rich domains?
    • Epand, R. M. 2004. Do proteins facilitate the formation of cholesterol-rich domains? Biochim. Biophys. Acta. 1666:227-238.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 227-238
    • Epand, R.M.1
  • 42
    • 2642533608 scopus 로고    scopus 로고
    • Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction
    • Hinderliter, A., R. L. Biltonen, and P. F. F. Almeida. 2004. Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction. Biochemistry. 43:7102-7110.
    • (2004) Biochemistry , vol.43 , pp. 7102-7110
    • Hinderliter, A.1    Biltonen, R.L.2    Almeida, P.F.F.3
  • 43
    • 0024438206 scopus 로고
    • Conformational study of poly(L-lysine) interacting with acidic phospholipid vesicles
    • Fukushima, K., Y. Muraoka, T. Inoue, and R. Shimozawa. 1989. Conformational study of poly(L-lysine) interacting with acidic phospholipid vesicles. Biophys. Chem. 34:83-90.
    • (1989) Biophys. Chem. , vol.34 , pp. 83-90
    • Fukushima, K.1    Muraoka, Y.2    Inoue, T.3    Shimozawa, R.4
  • 44
    • 0014959632 scopus 로고
    • Structure of macromolecular aggregates. II. Construction of model membranes from phospholipids and polypeptides
    • Hammes, G. G., and S. E. Schullery. 1970. Structure of macromolecular aggregates. II. Construction of model membranes from phospholipids and polypeptides. Biochemistry. 9:2555-2563.
    • (1970) Biochemistry , vol.9 , pp. 2555-2563
    • Hammes, G.G.1    Schullery, S.E.2
  • 45
    • 0022500198 scopus 로고
    • Investigation of polylysinedipalmitoylphosphatidylglycerol interactions in model membranes
    • Carrier, D., and M. Pezolet. 1986. Investigation of polylysinedipalmitoylphosphatidylglycerol interactions in model membranes. Biochemistry. 25:4167-4174.
    • (1986) Biochemistry , vol.25 , pp. 4167-4174
    • Carrier, D.1    Pezolet, M.2
  • 46
    • 0023711978 scopus 로고
    • Study of the effect of poly(L-lysine) on phosphatidic acid and phosphatidylcholine/phosphatidic acid bilayers by Raman spectroscopy
    • Laroche, G., D. Carrier, and M. Pezolet. 1988. Study of the effect of poly(L-lysine) on phosphatidic acid and phosphatidylcholine/phosphatidic acid bilayers by Raman spectroscopy. Biochemistry. 27:6220-6228.
    • (1988) Biochemistry , vol.27 , pp. 6220-6228
    • Laroche, G.1    Carrier, D.2    Pezolet, M.3
  • 47
    • 0037162409 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers
    • Liu, F., N. A. H. Lewis Ruthven, S. Hodges Robert, and N. McElhaney Ronald. 2002. Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers. Biochemistry. 41:9197-9207.
    • (2002) Biochemistry , vol.41 , pp. 9197-9207
    • Liu, F.1    Lewis Ruthven, N.A.H.2    Hodges Robert, S.3    McElhaney Ronald, N.4
  • 48
    • 16644377766 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylethanolamine bilayers
    • Liu, F., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 2004. Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylethanolamine bilayers. Biophys. J. 87:2470-2482.
    • (2004) Biophys. J. , vol.87 , pp. 2470-2482
    • Liu, F.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 51
    • 0033880358 scopus 로고    scopus 로고
    • 2+ on the morphology of mixed DPPC-DOPS supported phospholipid bilayers
    • 2+ on the morphology of mixed DPPC-DOPS supported phospholipid bilayers. Langmuir. 16:1473-1477.
    • (2000) Langmuir , vol.16 , pp. 1473-1477
    • Reviakine, I.1    Simon, A.2    Brisson, A.3
  • 52
    • 0242290843 scopus 로고    scopus 로고
    • Pathways of lipid vesicle deposition on solid surfaces: A combined QCM-D and AFM study
    • Richter, R., A. Mukhopadhyay, and A. Brisson. 2003. Pathways of lipid vesicle deposition on solid surfaces: a combined QCM-D and AFM study. Biophys. J. 85:3035-3047.
    • (2003) Biophys. J. , vol.85 , pp. 3035-3047
    • Richter, R.1    Mukhopadhyay, A.2    Brisson, A.3
  • 53
    • 0033639204 scopus 로고    scopus 로고
    • From liposomes to supported, planar bilayer structures on hydrophilic and hydrophobic surfaces: An atomic force microscopy study
    • Jass, J., T. Tjarnhage, and G. Puu. 2000. From liposomes to supported, planar bilayer structures on hydrophilic and hydrophobic surfaces: an atomic force microscopy study. Biophys. J. 79:3153-3163.
    • (2000) Biophys. J. , vol.79 , pp. 3153-3163
    • Jass, J.1    Tjarnhage, T.2    Puu, G.3
  • 54
    • 0022531311 scopus 로고
    • Supported planar membranes in studies of cell-cell recognition in the immune system
    • McConnell, H. M., T. H. Watts, R. M. Weis, and A. A. Brian. 1986. Supported planar membranes in studies of cell-cell recognition in the immune system. Biochim. Biophys. Acta. 864:95-106.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 95-106
    • McConnell, H.M.1    Watts, T.H.2    Weis, R.M.3    Brian, A.A.4
  • 55
    • 21244451188 scopus 로고    scopus 로고
    • Direct visualization of asymmetric behavior in supported lipid bilayers at the gel-fluid phase transition
    • Feng, Z. V., T. A. Spurlin, and A. A. Gewirth. 2005. Direct visualization of asymmetric behavior in supported lipid bilayers at the gel-fluid phase transition. Biophys. J. 88:2154-2164.
    • (2005) Biophys. J. , vol.88 , pp. 2154-2164
    • Feng, Z.V.1    Spurlin, T.A.2    Gewirth, A.A.3
  • 56
    • 18144423564 scopus 로고    scopus 로고
    • Decoupled phase transitions and grain-boundary melting in supported phospholipid bilayers
    • Keller, D., N. B. Larsen, I. M. Moeller, and O. G. Mouritsen. 2005. Decoupled phase transitions and grain-boundary melting in supported phospholipid bilayers. Phys. Rev. Lett. 94:025701/025701-025701/025704.
    • (2005) Phys. Rev. Lett. , vol.94
    • Keller, D.1    Larsen, N.B.2    Moeller, I.M.3    Mouritsen, O.G.4
  • 57
    • 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
  • 59
    • 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. S. 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.S.4    Cramb, D.T.5
  • 60
    • 28444474267 scopus 로고    scopus 로고
    • Effect of temperature on the nanomechanics of lipid bilayers studied by force spectroscopy
    • Garcia-Manyes, S., G. Oncins, and F. Sanz. 2005. Effect of temperature on the nanomechanics of lipid bilayers studied by force spectroscopy. Biophys. J. 89:4261-4274.
    • (2005) Biophys. J. , vol.89 , pp. 4261-4274
    • Garcia-Manyes, S.1    Oncins, G.2    Sanz, F.3
  • 61
    • 23844517491 scopus 로고    scopus 로고
    • Role of lipid charge in organization of water/lipid bilayer interface: Insights via computer simulations
    • Polyansky, A. A., P. E. Volynsky, D. E. Nolde, A. S. Arseniev, and R. G. Efremov. 2005. Role of lipid charge in organization of water/lipid bilayer interface: insights via computer simulations. J. Phys. Chem. B. 109:15052-15059.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15052-15059
    • Polyansky, A.A.1    Volynsky, P.E.2    Nolde, D.E.3    Arseniev, A.S.4    Efremov, R.G.5
  • 62
    • 0032438997 scopus 로고    scopus 로고
    • Nano-deposition of protein molecules using tapping-mode atomic force microscopy: Facts or artifacts
    • You, H., and L. Yu. 1998. Nano-deposition of protein molecules using tapping-mode atomic force microscopy: facts or artifacts. Probe Microscopy. 1:233-237.
    • (1998) Probe Microscopy , vol.1 , pp. 233-237
    • You, H.1    Yu, L.2
  • 63
    • 0037062827 scopus 로고    scopus 로고
    • Lipid phase dependence of DNA-cationic phospholipid bilayer interactions examined using atomic force microscopy
    • Leonenko, Z. V., D. Merkle, S. P. Lees-Miller, and D. T. Cramb. 2002. Lipid phase dependence of DNA-cationic phospholipid bilayer interactions examined using atomic force microscopy. Langmuir. 18:4873-4884.
    • (2002) Langmuir , vol.18 , pp. 4873-4884
    • Leonenko, Z.V.1    Merkle, D.2    Lees-Miller, S.P.3    Cramb, D.T.4
  • 64
    • 0034730471 scopus 로고    scopus 로고
    • Estimations of lipid bilayer geometry in fluid lamellar phases
    • Costigan, S. C., P. J. Booth, and R. H. Templer. 2000. Estimations of lipid bilayer geometry in fluid lamellar phases. Biochim. Biophys. Acta. 1468:41-54.
    • (2000) Biochim. Biophys. Acta , vol.1468 , pp. 41-54
    • Costigan, S.C.1    Booth, P.J.2    Templer, R.H.3
  • 65
    • 16644377766 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine bilayers
    • Liu, F., N. A. H. Lewis Ruthven, S. Hodges Robert, and N. McElhaney Ronald. 2004. Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine bilayers. Biophys. J. 87:2470-2482.
    • (2004) Biophys. J. , vol.87 , pp. 2470-2482
    • Liu, F.1    Lewis Ruthven, N.A.H.2    Hodges Robert, S.3    McElhaney Ronald, N.4
  • 66
    • 25844458511 scopus 로고    scopus 로고
    • Synthetic and natural polycationic polymer nanoparticles interact selectively with fluid-phase domains of DMPC lipid bilayers
    • Mecke, A., D.-K. Lee, A. Ramamoorthy, B. G. Orr, and M. M. Banaszak Holl. 2005. Synthetic and natural polycationic polymer nanoparticles interact selectively with fluid-phase domains of DMPC lipid bilayers. Langmuir. 21:8588-8590.
    • (2005) Langmuir , vol.21 , pp. 8588-8590
    • Mecke, A.1    Lee, D.-K.2    Ramamoorthy, A.3    Orr, B.G.4    Banaszak Holl, M.M.5
  • 67
    • 17844381589 scopus 로고    scopus 로고
    • Following the formation of supported lipid bilayers on mica: A study combining AFM, QCM-D, and ellipsometry
    • Richter, R. P., and A. R. Brisson. 2005. Following the formation of supported lipid bilayers on mica: a study combining AFM, QCM-D, and ellipsometry. Biophys. J. 88:3422-3433.
    • (2005) Biophys. J. , vol.88 , pp. 3422-3433
    • Richter, R.P.1    Brisson, A.R.2
  • 68
    • 1642402920 scopus 로고    scopus 로고
    • Synthetic copoly(Lys/Phe) and poly(Lys) translocate through lipid bilayer membranes
    • Shibata, A., S. Murata, S. Ueno, S. Liu, S. Futaki, and Y. Baba. 2003. Synthetic copoly(Lys/Phe) and poly(Lys) translocate through lipid bilayer membranes. Biochim. Biophys. Acta. 1616:147-155.
    • (2003) Biochim. Biophys. Acta , vol.1616 , pp. 147-155
    • Shibata, A.1    Murata, S.2    Ueno, S.3    Liu, S.4    Futaki, S.5    Baba, Y.6
  • 69
    • 4444329595 scopus 로고    scopus 로고
    • Interaction of poly(L-lysine)-g-poly(ethylene glycol) with supported phospholipid bilayers
    • Rossetti, F. F., I. Reviakine, G. Csucs, F. Assi, J. Voeroes, and M. Textor. 2004. Interaction of poly(L-lysine)-g-poly(ethylene glycol) with supported phospholipid bilayers. Biophys. J. 87:1711-1721.
    • (2004) Biophys. J. , vol.87 , pp. 1711-1721
    • Rossetti, F.F.1    Reviakine, I.2    Csucs, G.3    Assi, F.4    Voeroes, J.5    Textor, M.6
  • 71
    • 0001002410 scopus 로고
    • Phenomenology and kinetics of lipid bilayer spreading on hydrophilic surfaces
    • Raedler, J., H. Strey, and E. Sackmann. 1995. Phenomenology and kinetics of lipid bilayer spreading on hydrophilic surfaces. Langmuir. 11:4539-4548.
    • (1995) Langmuir , vol.11 , pp. 4539-4548
    • Raedler, J.1    Strey, H.2    Sackmann, E.3
  • 72
    • 0029998704 scopus 로고    scopus 로고
    • Impedance analysis of supported lipid bilayer membranes: A scrutiny of different preparation techniques
    • Steinem, C., A. Janshoff, W. P. Ulrich, M. Sieber, and H. J. Galla. 1996. Impedance analysis of supported lipid bilayer membranes: a scrutiny of different preparation techniques. Biochim. Biophys. Acta. 1279:169-180.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 169-180
    • Steinem, C.1    Janshoff, A.2    Ulrich, W.P.3    Sieber, M.4    Galla, H.J.5
  • 73
    • 0032482919 scopus 로고    scopus 로고
    • Influence of polylysine on the rupture of negatively charged membranes
    • Diederich, A., G. Baehr, and M. Winterhalter. 1998. Influence of polylysine on the rupture of negatively charged membranes. Langmuir. 14:4597-4605.
    • (1998) Langmuir , vol.14 , pp. 4597-4605
    • Diederich, A.1    Baehr, G.2    Winterhalter, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.