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Volumn 270, Issue 9, 2003, Pages 2038-2046

Interaction of the P-type cardiotoxin with phospholipid membranes

Author keywords

31P NMR; Cytotoxin II (cardiotoxin); Isotropic phase; Membrane binding mode; Multilamellar phospholipid vesicles

Indexed keywords

AMPHOLYTE; CARDIOTOXIN; CYTOTOXIN; DIPALMITOYLGLYCEROPHOSPHOGLYCEROL; DIPALMITOYLPHOSPHATIDYLCHOLINE; GLYCEROL DERIVATIVE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 0038029876     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03580.x     Document Type: Article
Times cited : (41)

References (49)
  • 2
    • 0023728715 scopus 로고
    • Structure and pharmacology of elapid cytotoxins
    • Dufton, M.J. & Hider, R.C. (1988) Structure and pharmacology of elapid cytotoxins. Pharmacol. Ther. 36, 1-40.
    • (1988) Pharmacol. Ther. , vol.36 , pp. 1-40
    • Dufton, M.J.1    Hider, R.C.2
  • 4
    • 0018100287 scopus 로고
    • Specific binding of a cardiotoxin from Naja mossambica mossambica to charged phospholipids detected by intrinsic fluorescence
    • Dufourcq, J. & Faucon, J.F. (1978) Specific binding of a cardiotoxin from Naja mossambica mossambica to charged phospholipids detected by intrinsic fluorescence. Biochemistry 17, 1170-1176.
    • (1978) Biochemistry , vol.17 , pp. 1170-1176
    • Dufourcq, J.1    Faucon, J.F.2
  • 5
    • 0017838272 scopus 로고
    • Properties of association of cardiotoxin with lipid vesicles and natural membranes. A fluorescence study
    • Vincent, J.P., Balerna, M. & Lazdunski, M. (1978) Properties of association of cardiotoxin with lipid vesicles and natural membranes. A fluorescence study. FEBS Lett. 85, 103-108.
    • (1978) FEBS Lett. , vol.85 , pp. 103-108
    • Vincent, J.P.1    Balerna, M.2    Lazdunski, M.3
  • 6
    • 0028332859 scopus 로고
    • Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions
    • Chien, K.Y., Chiang, C.M., Hseu, Y.C., Vyas, A.A., Rule, G.S. & Wu, W.G. (1994) Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions. J. Biol. Chem. 269, 14473-14483.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14473-14483
    • Chien, K.Y.1    Chiang, C.M.2    Hseu, Y.C.3    Vyas, A.A.4    Rule, G.S.5    Wu, W.G.6
  • 7
    • 0031740077 scopus 로고    scopus 로고
    • Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes
    • Watts, A. (1998) Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes. Biochim. Biophys. Acta 1376, 297-318.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 297-318
    • Watts, A.1
  • 8
    • 0032694324 scopus 로고    scopus 로고
    • The monolayer technique: A potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes
    • Maget-Dana, R. (1999) The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes. Biochim. Biophys. Acta 1462, 109-140.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 109-140
    • Maget-Dana, R.1
  • 10
    • 0019816841 scopus 로고
    • Penetration of phospholipid monolayers by cardiotoxins
    • Bougis, P., Rochat, H., Pieroni, G. & Verger, R. (1981) Penetration of phospholipid monolayers by cardiotoxins. Biochemistry 20, 4915-4920.
    • (1981) Biochemistry , vol.20 , pp. 4915-4920
    • Bougis, P.1    Rochat, H.2    Pieroni, G.3    Verger, R.4
  • 11
    • 0018074077 scopus 로고
    • A possible structural basis for the different modes of action of neurotoxins and cardiotoxins from snake venoms
    • Lauterwein, J. & Wüthrich, K. (1978) A possible structural basis for the different modes of action of neurotoxins and cardiotoxins from snake venoms. FEBS Lett. 93, 181-184.
    • (1978) FEBS Lett. , vol.93 , pp. 181-184
    • Lauterwein, J.1    Wüthrich, K.2
  • 12
    • 0028306665 scopus 로고
    • X-ray structure at 1.55 Å of toxin gamma, a cardiotoxin from Naja nigricollis venom. Crystal packing reveals a model for insertion into membranes
    • Bilwes, A., Rees, B., Moras, D., Menez, R. & Ménez, A. (1994) X-ray structure at 1.55 Å of toxin gamma, a cardiotoxin from Naja nigricollis venom. Crystal packing reveals a model for insertion into membranes. J. Mol. Biol. 239, 122-136.
    • (1994) J. Mol. Biol. , vol.239 , pp. 122-136
    • Bilwes, A.1    Rees, B.2    Moras, D.3    Menez, R.4    Ménez, A.5
  • 13
    • 0030764529 scopus 로고    scopus 로고
    • Action of Taiwan cobra cardiotoxin on membranes: Binding modes of a beta-sheet polypeptide with phosphatidylcholine bilayers
    • Sue, S.C., Rajan, P.K., Chen, T.S., Hsieh, C.H. & Wu, W. (1997) Action of Taiwan cobra cardiotoxin on membranes: binding modes of a beta-sheet polypeptide with phosphatidylcholine bilayers. Biochemistry 36, 9826-9836.
    • (1997) Biochemistry , vol.36 , pp. 9826-9836
    • Sue, S.C.1    Rajan, P.K.2    Chen, T.S.3    Hsieh, C.H.4    Wu, W.5
  • 14
    • 0029013695 scopus 로고
    • An NMR study of the interaction of cardiotoxin gamma from Naja nigricollis with perdeuterated dodecylphosphocholine micelles
    • Dauplais, M., Neumann, J.M., Pinkasfeld, S., Menez, A. & Roumestand, C. (1995) An NMR study of the interaction of cardiotoxin gamma from Naja nigricollis with perdeuterated dodecylphosphocholine micelles. Eur. J. Biochem. 230, 213-220.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 213-220
    • Dauplais, M.1    Neumann, J.M.2    Pinkasfeld, S.3    Menez, A.4    Roumestand, C.5
  • 19
    • 0032586679 scopus 로고    scopus 로고
    • 31P NMR first spectral moment study of the partial magnetic orientation of phospholipid membranes
    • 31P NMR first spectral moment study of the partial magnetic orientation of phospholipid membranes. Biophys. J. 77, 888-902.
    • (1999) Biophys. J. , vol.77 , pp. 888-902
    • Picard, F.1    Paquet, M.J.2    Levesque, J.3    Belanger, A.4    Auger, M.5
  • 21
    • 0033167928 scopus 로고    scopus 로고
    • Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution: Spatial structures with tightly bound water molecules
    • Dementieva, D.V., Bocharov, E.V. & Arseniev, A.S. (1999) Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution: spatial structures with tightly bound water molecules. Eur. J. Biochem. 263, 152-162.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 152-162
    • Dementieva, D.V.1    Bocharov, E.V.2    Arseniev, A.S.3
  • 22
    • 0026951903 scopus 로고
    • Gradient tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenář, V. (1992) Gradient tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenář, V.3
  • 23
    • 2442767079 scopus 로고
    • Obtaining high-fidelity spin 1/2-powder spectra in anisotropic media: Phase cycled Hahn echo spectroscopy
    • Rance, M. & Byrd, R.A. (1983) Obtaining high-fidelity spin 1/2-powder spectra in anisotropic media: phase cycled Hahn echo spectroscopy. J. Magn. Reson. 52, 221-240.
    • (1983) J. Magn. Reson. , vol.52 , pp. 221-240
    • Rance, M.1    Byrd, R.A.2
  • 24
    • 0027464961 scopus 로고
    • Magnetically induced orientation of phosphatidylcholine membranes
    • Qiu, X., Mirau, P.A. & Pidgeon, C. (1993) Magnetically induced orientation of phosphatidylcholine membranes. Biochim. Biophys. Acta 1147, 59-72.
    • (1993) Biochim. Biophys. Acta , vol.1147 , pp. 59-72
    • Qiu, X.1    Mirau, P.A.2    Pidgeon, C.3
  • 25
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billiter, M. & Wütrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billiter, M.2    Wütrich, K.3
  • 26
    • 0024322106 scopus 로고
    • Interaction of the Saccharomyces cerevisiae alpha-factor with phospholipid vesicles as revealed by proton and phosphorus NMR
    • Jelicks, L.A., Broido, M.S., Becker, J.M. & Naider, F.R. (1989) Interaction of the Saccharomyces cerevisiae alpha-factor with phospholipid vesicles as revealed by proton and phosphorus NMR. Biochemistry 28, 4233-4240.
    • (1989) Biochemistry , vol.28 , pp. 4233-4240
    • Jelicks, L.A.1    Broido, M.S.2    Becker, J.M.3    Naider, F.R.4
  • 28
    • 0025801848 scopus 로고
    • Fusion of sphingomyelin vesicles induced by proteins from Taiwan cobra (Naja naja atra) venom. Interactions of zwitterionic phospholipids with cardiotoxin analogues
    • Chien, K.Y., Huang, W.N., Jean, J.H. & Wu, W.G. (1991) Fusion of sphingomyelin vesicles induced by proteins from Taiwan cobra (Naja naja atra) venom. Interactions of zwitterionic phospholipids with cardiotoxin analogues. J. Biol. Chem. 266, 3252-3259.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3252-3259
    • Chien, K.Y.1    Huang, W.N.2    Jean, J.H.3    Wu, W.G.4
  • 29
    • 46549104553 scopus 로고
    • Magnetic ordering of phospholipid membranes
    • Seelig, J., Borle, F. & Cross, T.A. (1985) Magnetic ordering of phospholipid membranes. Biochim. Biophys. Acta. 814, 195-198.
    • (1985) Biochim. Biophys. Acta , vol.814 , pp. 195-198
    • Seelig, J.1    Borle, F.2    Cross, T.A.3
  • 31
    • 0026578843 scopus 로고
    • Macroscopic orientation effects in broadline NMR-spectra of model membranes at high magnetic field strength. A method preventing such effects
    • Brumm, T., Möps, A., Dolainsky, C. & Bayerl, T.M. (1992) Macroscopic orientation effects in broadline NMR-spectra of model membranes at high magnetic field strength. A method preventing such effects. Biophys. J. 61, 1018-1024.
    • (1992) Biophys. J. , vol.61 , pp. 1018-1024
    • Brumm, T.1    Möps, A.2    Dolainsky, C.3    Bayerl, T.M.4
  • 33
    • 0022297833 scopus 로고
    • Deuterium and phosphorus nuclear magnetic resonance studies on the binding of polymyxin B to lipid bilayer-water interfaces
    • Sixl, F. & Watts, A. (1985) Deuterium and phosphorus nuclear magnetic resonance studies on the binding of polymyxin B to lipid bilayer-water interfaces. Biochemistry 24, 7906-7910.
    • (1985) Biochemistry , vol.24 , pp. 7906-7910
    • Sixl, F.1    Watts, A.2
  • 34
    • 0028804445 scopus 로고
    • Modulation of melittin-induced lysis by surface charge density of membranes
    • Monette, M. & Lafleur, M. (1995) Modulation of melittin-induced lysis by surface charge density of membranes. Biophys. J. 68, 187-195.
    • (1995) Biophys. J. , vol.68 , pp. 187-195
    • Monette, M.1    Lafleur, M.2
  • 38
    • 0030890988 scopus 로고    scopus 로고
    • Interactions of thionin from Pyrularia pubera with dipalmitoylphosphatidylglycerol large unilamellar vesicles
    • Huang, W., Vernon, L.P., Hansen, L.D. & Bell, J.D. (1997) Interactions of thionin from Pyrularia pubera with dipalmitoylphosphatidylglycerol large unilamellar vesicles. Biochemistry 36, 2860-2866.
    • (1997) Biochemistry , vol.36 , pp. 2860-2866
    • Huang, W.1    Vernon, L.P.2    Hansen, L.D.3    Bell, J.D.4
  • 39
    • 0025061113 scopus 로고
    • Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes
    • Beschiaschvili, G. & Seelig, J. (1990) Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes. Biochemistry 29, 52-58.
    • (1990) Biochemistry , vol.29 , pp. 52-58
    • Beschiaschvili, G.1    Seelig, J.2
  • 41
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit, E., Boman, A., Boman, H.G. & Shai, Y. (1995) Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34, 11479-11488.
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 43
    • 0031024447 scopus 로고    scopus 로고
    • Crystal structure of cardiotoxin V from Taiwan cobra venom: pH-dependent conformational change and a novel membrane-binding motif identified in the three-finger loops of P-type cardiotoxin
    • Sun, Y.J., Wu, W.G., Chiang, C.M., Hsin, A.Y. & Hsiao, C.D. (1997) Crystal structure of cardiotoxin V from Taiwan cobra venom: pH-dependent conformational change and a novel membrane-binding motif identified in the three-finger loops of P-type cardiotoxin. Biochemistry 36, 2403-2413.
    • (1997) Biochemistry , vol.36 , pp. 2403-2413
    • Sun, Y.J.1    Wu, W.G.2    Chiang, C.M.3    Hsin, A.Y.4    Hsiao, C.D.5
  • 44
    • 0035980233 scopus 로고    scopus 로고
    • Dynamic characterization of the water binding loop in the P-type cardiotoxin: Implication for the role of the bound water molecule
    • Sue, S.C., Jarrell, H.C., Brisson, J.R. & Wu, W.G. (2001) Dynamic characterization of the water binding loop in the P-type cardiotoxin: implication for the role of the bound water molecule. Biochemistry 40, 12782-12794.
    • (2001) Biochemistry , vol.40 , pp. 12782-12794
    • Sue, S.C.1    Jarrell, H.C.2    Brisson, J.R.3    Wu, W.G.4
  • 45
    • 0022339641 scopus 로고
    • Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organization
    • Batenburg, A.M., Bougis, P.E., Rochat, H., Verkleij, A.J. & de Kruijff, B. (1985) Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organization. Biochemistry 24, 7101-7110.
    • (1985) Biochemistry , vol.24 , pp. 7101-7110
    • Batenburg, A.M.1    Bougis, P.E.2    Rochat, H.3    Verkleij, A.J.4    De Kruijff, B.5
  • 46
    • 0031057809 scopus 로고    scopus 로고
    • Cobra venom cytotoxin free of phospholipase A and its effect on model membranes and T leukemia cells
    • Gasanov, S.E., Alsarraj, M.A., Gasanov, N.E. & Rael, E.D. (1997) Cobra venom cytotoxin free of phospholipase A and its effect on model membranes and T leukemia cells. J. Membr. Biol. 155, 133-142.
    • (1997) J. Membr. Biol. , vol.155 , pp. 133-142
    • Gasanov, S.E.1    Alsarraj, M.A.2    Gasanov, N.E.3    Rael, E.D.4
  • 47
    • 0030294854 scopus 로고    scopus 로고
    • Similarities and differences in mechanisms of cardiotoxins, melittin and other myotoxins
    • Fletcher, J.E., Hubert, M., Wieland, S.J., Gong, Q.H. & Jiang, M.S. (1996) Similarities and differences in mechanisms of cardiotoxins, melittin and other myotoxins. Toxicon 34, 1301-1311.
    • (1996) Toxicon , vol.34 , pp. 1301-1311
    • Fletcher, J.E.1    Hubert, M.2    Wieland, S.J.3    Gong, Q.H.4    Jiang, M.S.5
  • 48
    • 0026522092 scopus 로고
    • 2H-NMR, FT-IR, DSC, and neutron scattering study
    • 2H-NMR, FT-IR, DSC, and neutron scattering study. Biophys. J. 61, 1025-1035.
    • (1992) Biophys. J. , vol.61 , pp. 1025-1035
    • Reinl, H.1    Brumm, T.2    Bayerl, T.M.3
  • 49
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo, E., Kloda, A., Cortes, D.M. & Martinac, B. (2002) Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9, 696-703.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4


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