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Volumn 71, Issue 6, 1996, Pages 3288-3301

Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH-sensitive peptide

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; GLYCEROPHOSPHORYLCHOLINE; LIPOSOME; SYNTHETIC PEPTIDE;

EID: 0029731358     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79521-8     Document Type: Article
Times cited : (70)

References (53)
  • 1
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 2
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • Baumann, G., and P. Mueller. 1974. A molecular model of membrane excitability. J. Supramol. Struct. 2:538-557.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 3
    • 0029042292 scopus 로고
    • Study of vesicle leakage induced by melittin
    • Benachir, T., and M. Lafleur. 1995. Study of vesicle leakage induced by melittin. Biochim. Biophys. Acta. 1235:452-460.
    • (1995) Biochim. Biophys. Acta , vol.1235 , pp. 452-460
    • Benachir, T.1    Lafleur, M.2
  • 4
    • 0019546646 scopus 로고
    • Aggregation of colloidal particles modeled as a dynamical process
    • Bentz, J., and S. Nir. 1981. Aggregation of colloidal particles modeled as a dynamical process. Proc. Natl. Acad. Sci. U.S.A. 78:1634-1637.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 1634-1637
    • Bentz, J.1    Nir, S.2
  • 5
    • 0023707810 scopus 로고
    • Mass action kinetics of virus-cell aggregation and fusion
    • Bentz, J., S. Nir. and D. G. Covell. 1988. Mass action kinetics of virus-cell aggregation and fusion. Biophys. J. 54:449-462.
    • (1988) Biophys. J. , vol.54 , pp. 449-462
    • Bentz, J.1    Nir, S.2    Covell, D.G.3
  • 6
    • 5344219744 scopus 로고
    • Note on the kinetics of systems manifesting simultaneous polymerization-depolymerization phenomena
    • Blatz, P. J., and A. V. Tobolski. 1945. Note on the kinetics of systems manifesting simultaneous polymerization-depolymerization phenomena. J. Phys. Chem. 49:77-80.
    • (1945) J. Phys. Chem. , vol.49 , pp. 77-80
    • Blatz, P.J.1    Tobolski, A.V.2
  • 7
    • 0028001501 scopus 로고
    • The effects of membrane physical properties on the fusion of Sendai virus with human erythrocyte ghosts and liposomes. Analysis of kinetics and extent of fusion
    • Cheetham, J. J., S. Nir, E. Johnson, T. D. Flanagan, and R. M. Epand. 1994. The effects of membrane physical properties on the fusion of Sendai virus with human erythrocyte ghosts and liposomes. Analysis of kinetics and extent of fusion. J. Biol. Chem. 269:5467-5472.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5467-5472
    • Cheetham, J.J.1    Nir, S.2    Johnson, E.3    Flanagan, T.D.4    Epand, R.M.5
  • 8
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen, B., J. Fink, R. B. Merrifield, and D. Mauzerall. 1988. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. U.S.A. 85:5072-5076.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 9
    • 0020025608 scopus 로고
    • Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue
    • DeGrado, W. F., G. F. Musso, M. Lieber, E. T. Kaiser, and F. J. Kezdy. 1982. Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue. Biophys. J. 37:329-338.
    • (1982) Biophys. J. , vol.37 , pp. 329-338
    • DeGrado, W.F.1    Musso, G.F.2    Lieber, M.3    Kaiser, E.T.4    Kezdy, F.J.5
  • 10
    • 0024285006 scopus 로고
    • Solute partitioning into bilayer membranes
    • De Young, L. R., and K. A. Dill. 1988. Solute partitioning into bilayer membranes. Biochemistry. 27:5281-5289.
    • (1988) Biochemistry , vol.27 , pp. 5281-5289
    • De Young, L.R.1    Dill, K.A.2
  • 11
    • 0017377209 scopus 로고
    • Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesicles
    • Dufourcq, J., and J. F. Faucon. 1977. Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesicles. Biochim. Biophys. Acta. 467:1-11.
    • (1977) Biochim. Biophys. Acta , vol.467 , pp. 1-11
    • Dufourcq, J.1    Faucon, J.F.2
  • 12
    • 0026645243 scopus 로고
    • Membrane destabilization by N-terminal peptides of viral envelope proteins
    • Düzgünes, N., and S. A. Shavnin. 1992. Membrane destabilization by N-terminal peptides of viral envelope proteins. J. Membr. Biol. 128: 71-80.
    • (1992) J. Membr. Biol. , vol.128 , pp. 71-80
    • Düzgünes, N.1    Shavnin, S.A.2
  • 14
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G., and H. Lecar. 1977. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10:1-34.
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 15
    • 0021340434 scopus 로고
    • pH-induced destabilization of phosphatidylethanolamine-containing liposomes: Role of bilayer contact
    • Ellens, H., J. Bentz, and F. C. Szoka, Jr. 1984. pH-induced destabilization of phosphatidylethanolamine-containing liposomes: role of bilayer contact. Biochemistry. 23:1532-1538.
    • (1984) Biochemistry , vol.23 , pp. 1532-1538
    • Ellens, H.1    Bentz, J.2    Szoka Jr., F.C.3
  • 16
    • 0028178521 scopus 로고
    • Pore-forming peptides induce rapid phospholipid flip-flop in membranes
    • Fattal, E., S. Nir, R. A. Parente, and F. C. Szoka, Jr. 1994. Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry. 33:6721-6731.
    • (1994) Biochemistry , vol.33 , pp. 6721-6731
    • Fattal, E.1    Nir, S.2    Parente, R.A.3    Szoka Jr., F.C.4
  • 17
    • 33947443854 scopus 로고
    • Kinetics of polyesterification: A study of the effects of molecular weight and viscosity on reaction rate
    • Flory, P. J. 1939. Kinetics of polyesterification: a study of the effects of molecular weight and viscosity on reaction rate. J. Am. Chem. Soc. 61:3334-3340.
    • (1939) J. Am. Chem. Soc. , vol.61 , pp. 3334-3340
    • Flory, P.J.1
  • 18
    • 0025647096 scopus 로고
    • Membrane insertion and lateral diffusion of fluorescence-labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers
    • Frey, S., and L. K. Tamm. 1990. Membrane insertion and lateral diffusion of fluorescence-labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers. Biochem. J. 272: 713-719.
    • (1990) Biochem. J. , vol.272 , pp. 713-719
    • Frey, S.1    Tamm, L.K.2
  • 19
    • 0027336342 scopus 로고
    • A carboxy-terminal fragment of colicin la forms ion channels
    • Ghosh, P., S. F. Mel, and R. M. Stroud. 1993. A carboxy-terminal fragment of colicin la forms ion channels. J. Membr. Biol. 134:85-92.
    • (1993) J. Membr. Biol. , vol.134 , pp. 85-92
    • Ghosh, P.1    Mel, S.F.2    Stroud, R.M.3
  • 20
    • 0027655718 scopus 로고
    • Polyamidoamine cascade polymers mediate efficient transfection of cells in culture
    • Haensler, J., and F. C. Szoka, Jr. 1993. Polyamidoamine cascade polymers mediate efficient transfection of cells in culture. Bioconjugate Chem. 4:372-379.
    • (1993) Bioconjugate Chem. , vol.4 , pp. 372-379
    • Haensler, J.1    Szoka Jr., F.C.2
  • 21
    • 0024465666 scopus 로고
    • Staphylococcal alpha-toxin: A study of membrane penetration and pore formation
    • Harshman, S., P. Boquet, E. Duflot, J. E. Alouf, C. Montecucco, and E. Papini. 1989. Staphylococcal alpha-toxin: a study of membrane penetration and pore formation. J. Biol. Chem. 264:14978-14984.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14978-14984
    • Harshman, S.1    Boquet, P.2    Duflot, E.3    Alouf, J.E.4    Montecucco, C.5    Papini, E.6
  • 23
    • 0028883407 scopus 로고
    • Leakage of membrane vesicle contents: Determination of mechanism using fluores-cence requenching
    • Ladokhin, A. S., W. C. Wimley, and S. H. White. 1995. Leakage of membrane vesicle contents: determination of mechanism using fluores-cence requenching. Biophys. J. 69:1964-1971.
    • (1995) Biophys. J. , vol.69 , pp. 1964-1971
    • Ladokhin, A.S.1    Wimley, W.C.2    White, S.H.3
  • 24
    • 0017795661 scopus 로고
    • Model lipid bilayer membranes as targets for antibody-dependent, cellular- and complement-mediated immune attack
    • Lewis, J. T., and H. M. McConnell. 1978. Model lipid bilayer membranes as targets for antibody-dependent, cellular- and complement-mediated immune attack. Ann. N. Y. Acad. Sci. 308:124-138.
    • (1978) Ann. N. Y. Acad. Sci. , vol.308 , pp. 124-138
    • Lewis, J.T.1    McConnell, H.M.2
  • 25
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • Matsuzaki, K., K. Sugishita, N. Fujii, and K. Miyajima. 1995a. Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. Biochemistry. 34:3423-3429.
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 26
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1995b. Translocation of a channel-forming antimicrobial peptide, magainin 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
  • 27
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva, J. L., S. Nir, A. Muga, F. M. Goni, and J. Wilschut. 1994. Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry. 33:3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 29
    • 0022497957 scopus 로고
    • Kinetics and extent of fusion between Sendai virus and erythrocyte ghosts: Application of a mass action kinetic model
    • Nir, S., K. Klappe, and D. Hoekstra, 1986. Kinetics and extent of fusion between Sendai virus and erythrocyte ghosts: application of a mass action kinetic model. Biochemistry. 25:2155-2161.
    • (1986) Biochemistry , vol.25 , pp. 2155-2161
    • Nir, S.1    Klappe, K.2    Hoekstra, D.3
  • 30
    • 0028496741 scopus 로고
    • Analysis of particle uptake by cells: Binding to several receptors, equilibration time, endocytosis
    • Nir, S., R. Peled, and K. Lee. 1994. Analysis of particle uptake by cells: binding to several receptors, equilibration time, endocytosis. Colloids Surf. 89:45-57.
    • (1994) Colloids Surf. , vol.89 , pp. 45-57
    • Nir, S.1    Peled, R.2    Lee, K.3
  • 32
    • 0023883581 scopus 로고
    • pH-dependent fusion of phosphatidylcholine small vesicles. Induction by a synthetic amphipathic peptide
    • Parente, R. A., S. Nir, and F. C. Szoka, Jr. 1988. pH-dependent fusion of phosphatidylcholine small vesicles. Induction by a synthetic amphipathic peptide. J. Biol. Chem. 263:4724-4730.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4724-4730
    • Parente, R.A.1    Nir, S.2    Szoka Jr., F.C.3
  • 33
    • 0025042733 scopus 로고
    • Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA
    • Parente, R. A., S. Nir, and F. C. Szoka, Jr. 1990. Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA. Biochemistry. 29:8720-8728.
    • (1990) Biochemistry , vol.29 , pp. 8720-8728
    • Parente, R.A.1    Nir, S.2    Szoka Jr., F.C.3
  • 34
    • 0029209119 scopus 로고
    • Time of equilibration in reversible aggregation of particles
    • Peled, C. R., G. Braun, and S. Nir. 1995. Time of equilibration in reversible aggregation of particles. J Colloid Interface Sci. 169:204-213.
    • (1995) J Colloid Interface Sci. , vol.169 , pp. 204-213
    • Peled, C.R.1    Braun, G.2    Nir, S.3
  • 35
    • 0028199067 scopus 로고
    • The influence of endosome-disruptive peptides on gene transfer using syn-thetic virus-like gene transfer systems
    • Plank, C., B. Oberhauser, K. Mechtler, C. Koch, and E. Wagner. 1994. The influence of endosome-disruptive peptides on gene transfer using syn-thetic virus-like gene transfer systems. J. Biol. Chem. 269: 12918-12924.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12918-12924
    • Plank, C.1    Oberhauser, B.2    Mechtler, K.3    Koch, C.4    Wagner, E.5
  • 36
    • 0027946064 scopus 로고
    • Capacities of pardaxin analogues to induce fusion and leakage of negatively charged phospholipid vesicles are not necessarily correlated
    • Rapaport, D., S. Nir, and Y. Shai. 1994. Capacities of pardaxin analogues to induce fusion and leakage of negatively charged phospholipid vesicles are not necessarily correlated. Biochemistry. 33:12615-12624.
    • (1994) Biochemistry , vol.33 , pp. 12615-12624
    • Rapaport, D.1    Nir, S.2    Shai, Y.3
  • 37
    • 0030025781 scopus 로고    scopus 로고
    • Reversible surface aggregation in pore formation by pardaxin
    • Rapaport. D., R. Peled, S. Nir, and Y. Shai. 1996. Reversible surface aggregation in pore formation by pardaxin. Biophys. J. 70:2503-2512.
    • (1996) Biophys. J. , vol.70 , pp. 2503-2512
    • Rapaport, D.1    Peled, R.2    Nir, S.3    Shai, Y.4
  • 38
    • 0023441012 scopus 로고
    • Incorporation kinetics in a membrane, studied with the pore-forming peptide alamethicin
    • Schwarz, G., H. Gerke, V. Rizzo, and S. Stankowski. 1987. Incorporation kinetics in a membrane, studied with the pore-forming peptide alamethicin. Biophys. J. 52:685-692.
    • (1987) Biophys. J. , vol.52 , pp. 685-692
    • Schwarz, G.1    Gerke, H.2    Rizzo, V.3    Stankowski, S.4
  • 39
    • 0025113653 scopus 로고
    • Pore formation kinetics in membranes, determined from the release of marker molecules out of liposomes or cells
    • Schwarz, G., and C. H. Robert. 1990. Pore formation kinetics in membranes, determined from the release of marker molecules out of liposomes or cells. Biophys. J. 58:577-583.
    • (1990) Biophys. J. , vol.58 , pp. 577-583
    • Schwarz, G.1    Robert, C.H.2
  • 40
    • 0026607062 scopus 로고
    • Kinetics of pore-mediated release of marker molecules from liposomes or cells
    • Schwarz, G., and C. H. Robert. 1992. Kinetics of pore-mediated release of marker molecules from liposomes or cells. Biophys. Chem. 42:291-296.
    • (1992) Biophys. Chem. , vol.42 , pp. 291-296
    • Schwarz, G.1    Robert, C.H.2
  • 41
    • 0028221653 scopus 로고
    • Pardaxin: Channel formation by a shark repellant peptide from fish
    • Shai, Y. 1994. Pardaxin: channel formation by a shark repellant peptide from fish. Toxicology. 87:109-129.
    • (1994) Toxicology , vol.87 , pp. 109-129
    • Shai, Y.1
  • 43
    • 0024331657 scopus 로고
    • Patch clamp studies of single cell-fusion events mediated by a viral fusion protein
    • Spruce, A. E., A. Iwata, J. M. White, and W. Almers. 1989. Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature. 342:555-558.
    • (1989) Nature , vol.342 , pp. 555-558
    • Spruce, A.E.1    Iwata, A.2    White, J.M.3    Almers, W.4
  • 44
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., D. Hoekstra, and R. E. Pagano. 1981. Use of resonance energy transfer to monitor membrane fusion. Biochemistry. 20: 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 46
    • 0006847485 scopus 로고
    • Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation
    • Szoka, F. C., Jr., and D. Papahadjopoulos. 1978. Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation. Proc. Natl. Acad. Sci. U.S.A. 75:4194-4198.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4194-4198
    • Szoka Jr., F.C.1    Papahadjopoulos, D.2
  • 49
    • 0026655684 scopus 로고
    • Influenza virus hemagglutinin HA-2 N-terminal fusogenic peptides augment gene transfer by transferrin-polylysine-DNA complexes: Toward a synthetic virus-like gene-transfer vehicle
    • Wagner, E., C. Plank, K. Zatloukal, M. Cotten, and M. L. Birnstiel. 1992. Influenza virus hemagglutinin HA-2 N-terminal fusogenic peptides augment gene transfer by transferrin-polylysine-DNA complexes: toward a synthetic virus-like gene-transfer vehicle. Proc. Natl. Acad. Sci. U.S.A. 89:7934-7938.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7934-7938
    • Wagner, E.1    Plank, C.2    Zatloukal, K.3    Cotten, M.4    Birnstiel, M.L.5
  • 50
    • 0019871607 scopus 로고
    • Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins
    • Weinstein, J. N., R. D. Klausner, T. Innerarity, E. Ralston, and R. Blumenthal. 1981. Phase transition release, a new approach to the interaction of proteins with lipid vesicles. Application to lipoproteins. Biochim. Biophys. Acta. 647:270-284.
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 270-284
    • Weinstein, J.N.1    Klausner, R.D.2    Innerarity, T.3    Ralston, E.4    Blumenthal, R.5
  • 51
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. 1992. Membrane fusion. Science. 258:917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 52
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C, M. E. Selsted, and S. H. White. 1994. Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Sci. 3:1362-1373.
    • (1994) Protein Sci. , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 53
    • 0026785278 scopus 로고
    • Localized mutagenesis defines regions of the Bacillus thuringiensis delta-endotoxin involved in toxicity and specificity
    • Wu, D., and A. I. Aronson. 1992. Localized mutagenesis defines regions of the Bacillus thuringiensis delta-endotoxin involved in toxicity and specificity. J. Biol. Chem. 267:2311-2317.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2311-2317
    • Wu, D.1    Aronson, A.I.2


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