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Volumn 1758, Issue 4, 2006, Pages 545-551

High-resolution electrophysiology on a chip: Transient dynamics of alamethicin channel formation

Author keywords

Alamethicin; Electrophysiology; Glass microstructure; Lipid bilayer; Patch clamp chip

Indexed keywords

ALAMETHICIN; SOLVENT;

EID: 33646759936     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.03.023     Document Type: Article
Times cited : (59)

References (40)
  • 1
    • 0003996053 scopus 로고
    • Sakman B., and Neher E. (Eds), Plenum Press, New York
    • In: Sakman B., and Neher E. (Eds). Single-Channel Recordings (1983), Plenum Press, New York
    • (1983) Single-Channel Recordings
  • 2
    • 0036106307 scopus 로고    scopus 로고
    • Whole cell patch clamp recording performed on a planar glass chip
    • Fertig N., Blick R.H., and Behrends J.C. Whole cell patch clamp recording performed on a planar glass chip. Biophys. J. 82 (2002) 3056-3062
    • (2002) Biophys. J. , vol.82 , pp. 3056-3062
    • Fertig, N.1    Blick, R.H.2    Behrends, J.C.3
  • 3
    • 17444400816 scopus 로고    scopus 로고
    • An air-molding technique for fabricating pdms planar patch-clamp electrodes
    • Klemic K.G., Klemic J.F., and Sigworth F.J. An air-molding technique for fabricating pdms planar patch-clamp electrodes. Pflugers Arch. 449 (2005) 564-752
    • (2005) Pflugers Arch. , vol.449 , pp. 564-752
    • Klemic, K.G.1    Klemic, J.F.2    Sigworth, F.J.3
  • 4
    • 0037449319 scopus 로고    scopus 로고
    • Activity of single ion channel proteins detected with a planar microstructure
    • Fertig N., Klau M., George M., Blick R.H., and Behrends J.C. Activity of single ion channel proteins detected with a planar microstructure. Appl. Phys. Lett. 81 (2002) 4865-4867
    • (2002) Appl. Phys. Lett. , vol.81 , pp. 4865-4867
    • Fertig, N.1    Klau, M.2    George, M.3    Blick, R.H.4    Behrends, J.C.5
  • 5
    • 0034805579 scopus 로고    scopus 로고
    • Bilayer reconstitution of voltage-dependent ion channels using a microfabricated silicon chip
    • Pantoja R., Sigg D., Blunck R., Bezanilla F., and Heath J.R. Bilayer reconstitution of voltage-dependent ion channels using a microfabricated silicon chip. Biophys. J. 81 (2001) 2389-2394
    • (2001) Biophys. J. , vol.81 , pp. 2389-2394
    • Pantoja, R.1    Sigg, D.2    Blunck, R.3    Bezanilla, F.4    Heath, J.R.5
  • 6
    • 0141819130 scopus 로고    scopus 로고
    • Microfabricated teflon membranes for low-noise recordings of ion channels in planar lipid bilayers
    • Mayer M., Kriebel J.K., Tosteson M.T., and Whitesides G.M. Microfabricated teflon membranes for low-noise recordings of ion channels in planar lipid bilayers. Biophys. J. 85 (2003) 2684-2695
    • (2003) Biophys. J. , vol.85 , pp. 2684-2695
    • Mayer, M.1    Kriebel, J.K.2    Tosteson, M.T.3    Whitesides, G.M.4
  • 7
    • 0034283554 scopus 로고    scopus 로고
    • A chip-based biosensor for the functional analysis of single ion channels
    • Schmidt C., Mayer M., and Vogel H. A chip-based biosensor for the functional analysis of single ion channels. Angew. Chem., Int. Ed. 39 (2000) 3137-3140
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 3137-3140
    • Schmidt, C.1    Mayer, M.2    Vogel, H.3
  • 9
    • 0032319506 scopus 로고    scopus 로고
    • Low-noise patch-clamp techniques
    • Levis R.A., and Rae J.L. Low-noise patch-clamp techniques. Methods Enzymol. 293 (1998) 218-266
    • (1998) Methods Enzymol. , vol.293 , pp. 218-266
    • Levis, R.A.1    Rae, J.L.2
  • 11
    • 0016584343 scopus 로고
    • Membrane excitation through voltage-induced aggregation of channel precursors
    • Mueller P. Membrane excitation through voltage-induced aggregation of channel precursors. Ann. N. Y. Acad. Sci. 264 (1975) 247-264
    • (1975) Ann. N. Y. Acad. Sci. , vol.264 , pp. 247-264
    • Mueller, P.1
  • 12
    • 0020697109 scopus 로고
    • Alamethicin pore formation: voltage-dependent flip-flop of α-helix dipoles
    • Boheim G., Hanke W., and Jung G. Alamethicin pore formation: voltage-dependent flip-flop of α-helix dipoles. Biophys. Struct. Mech. 9 (1983) 181-191
    • (1983) Biophys. Struct. Mech. , vol.9 , pp. 181-191
    • Boheim, G.1    Hanke, W.2    Jung, G.3
  • 13
    • 0025897469 scopus 로고
    • "Reversed" alamethicin conductance in lipid bilayers
    • Taylor R.J., and de Levie R. "Reversed" alamethicin conductance in lipid bilayers. Biophys. J. 59 (1991) 873-879
    • (1991) Biophys. J. , vol.59 , pp. 873-879
    • Taylor, R.J.1    de Levie, R.2
  • 14
    • 0023492725 scopus 로고
    • Open channel noise. iii. high-resolution recordings show rapid current fluctuations in gramicidin a and four chemical analogues
    • Sigworth F.J., Urry D.W., and Prasad K.U. Open channel noise. iii. high-resolution recordings show rapid current fluctuations in gramicidin a and four chemical analogues. Biophys. J. 52 (1987) 1055-1064
    • (1987) Biophys. J. , vol.52 , pp. 1055-1064
    • Sigworth, F.J.1    Urry, D.W.2    Prasad, K.U.3
  • 16
    • 0002340491 scopus 로고    scopus 로고
    • Liposome electroformation
    • Luisi P.L., and Walde P. (Eds), John Wiley and Sons Ltd, Chichester
    • Angelova M.I. Liposome electroformation. In: Luisi P.L., and Walde P. (Eds). Giant Vesicles (2000), John Wiley and Sons Ltd, Chichester 27-36
    • (2000) Giant Vesicles , pp. 27-36
    • Angelova, M.I.1
  • 18
    • 0019458461 scopus 로고
    • Voltage-dependent channels in planar lipid bilayer membranes
    • Latorre R., and Alvarez O. Voltage-dependent channels in planar lipid bilayer membranes. Physiol. Rev. 61 (1981) 77-150
    • (1981) Physiol. Rev. , vol.61 , pp. 77-150
    • Latorre, R.1    Alvarez, O.2
  • 19
    • 0026754487 scopus 로고
    • Model ion channels: gramicidin and alamethicin
    • Woolley G.A., and Wallace B.A. Model ion channels: gramicidin and alamethicin. Membr. Biol. 192 (1992) 109-136
    • (1992) Membr. Biol. , vol.192 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 20
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • Duclohier H., and Wróblewski H. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184 (2001) 1-12
    • (2001) J. Membr. Biol. , vol.184 , pp. 1-12
    • Duclohier, H.1    Wróblewski, H.2
  • 21
    • 0014428197 scopus 로고
    • Action potentials induced in biomolecular lipid membranes
    • Mueller P., and Rudin D.O. Action potentials induced in biomolecular lipid membranes. Nature 217 (1968) 713-719
    • (1968) Nature , vol.217 , pp. 713-719
    • Mueller, P.1    Rudin, D.O.2
  • 22
    • 0015442260 scopus 로고
    • Time-variant conductance of bilayer membranes treated with monazomycin and alamethicin
    • Mauro A., Nanavati R.P., and Heyer E. Time-variant conductance of bilayer membranes treated with monazomycin and alamethicin. Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 3742-3744
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 3742-3744
    • Mauro, A.1    Nanavati, R.P.2    Heyer, E.3
  • 23
    • 0016910373 scopus 로고
    • Molecular aspects of electrical excitation in lipid bilayers and cell membranes
    • Mueller P. Molecular aspects of electrical excitation in lipid bilayers and cell membranes. Horiz. Biochem. Biophys. 2 (1976) 230-284
    • (1976) Horiz. Biochem. Biophys. , vol.2 , pp. 230-284
    • Mueller, P.1
  • 24
    • 0017869782 scopus 로고
    • Analysis of the multi-pore system of alamethicin in a lipid membrane
    • Boheim G., and Kolb H.-A. Analysis of the multi-pore system of alamethicin in a lipid membrane. J. Membr. Biol. 38 (1978) 99-150
    • (1978) J. Membr. Biol. , vol.38 , pp. 99-150
    • Boheim, G.1    Kolb, H.-A.2
  • 25
    • 0020041631 scopus 로고
    • Calcium-induced inactivation of alamethicin in asymmetric lipid bilayers
    • Hall J.E., and Cahalan M.D. Calcium-induced inactivation of alamethicin in asymmetric lipid bilayers. J. Gen. Physiol. 79 (1982) 387-409
    • (1982) J. Gen. Physiol. , vol.79 , pp. 387-409
    • Hall, J.E.1    Cahalan, M.D.2
  • 26
    • 0021056837 scopus 로고
    • Pressure effects on alamethicin conductance in bilayer membranes
    • Bruner L.J., and Hall J.E. Pressure effects on alamethicin conductance in bilayer membranes. Biophys. J. 44 (1983) 39-47
    • (1983) Biophys. J. , vol.44 , pp. 39-47
    • Bruner, L.J.1    Hall, J.E.2
  • 27
    • 0032513080 scopus 로고    scopus 로고
    • Self-assembled α-hemolysin pores in an s-layer-supported lipid bilayer
    • Schuster B., Pum D., Braha O., Bayley H., and Sleytr U.B. Self-assembled α-hemolysin pores in an s-layer-supported lipid bilayer. Biochim. Biophys. Acta 1370 (1998) 280-288
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 280-288
    • Schuster, B.1    Pum, D.2    Braha, O.3    Bayley, H.4    Sleytr, U.B.5
  • 28
    • 0001774017 scopus 로고
    • Fitting and statistical analysis of single-channel records
    • Sakmann B., and Neher E. (Eds), Plenum Press, New York
    • Colquhoun D., and Sigworth F.J. Fitting and statistical analysis of single-channel records. In: Sakmann B., and Neher E. (Eds). Single-Channel Recording (1995), Plenum Press, New York 483-587
    • (1995) Single-Channel Recording , pp. 483-587
    • Colquhoun, D.1    Sigworth, F.J.2
  • 29
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • Boheim G. Statistical analysis of alamethicin channels in black lipid membranes. J. Membr. Biol. 19 (1974) 277-303
    • (1974) J. Membr. Biol. , vol.19 , pp. 277-303
    • Boheim, G.1
  • 30
    • 0019323459 scopus 로고
    • The lowest conductance state of the alamethicin pore
    • Hanke W., and Boheim G. The lowest conductance state of the alamethicin pore. Biochim. Biophys. Acta 596 (1980) 456-462
    • (1980) Biochim. Biophys. Acta , vol.596 , pp. 456-462
    • Hanke, W.1    Boheim, G.2
  • 32
    • 0028243907 scopus 로고
    • Automatic detection of spontaneous synaptic responses in central neurons
    • Ankri N., Legendre P., Faber D., and Korn H. Automatic detection of spontaneous synaptic responses in central neurons. J. Neurosci. Methods 52 (1994) 87-100
    • (1994) J. Neurosci. Methods , vol.52 , pp. 87-100
    • Ankri, N.1    Legendre, P.2    Faber, D.3    Korn, H.4
  • 33
    • 0032191369 scopus 로고    scopus 로고
    • Single channel currents at six microsecond resolution elicited by acetylcholine in mouse myoballs
    • Parzefall F., Wilhelm R., Heckmann M., and Dudel J. Single channel currents at six microsecond resolution elicited by acetylcholine in mouse myoballs. J. Physiol. 512 (1998) 181-188
    • (1998) J. Physiol. , vol.512 , pp. 181-188
    • Parzefall, F.1    Wilhelm, R.2    Heckmann, M.3    Dudel, J.4
  • 34
    • 3843113235 scopus 로고    scopus 로고
    • Gating transitions in bacterial ion channels measured at 3 μs resolution
    • Shapovalov G., and Lester H.A. Gating transitions in bacterial ion channels measured at 3 μs resolution. J. Gen. Physiol. 124 (2004) 151-161
    • (2004) J. Gen. Physiol. , vol.124 , pp. 151-161
    • Shapovalov, G.1    Lester, H.A.2
  • 35
    • 0025062857 scopus 로고
    • Optimizing planar lipid bilayer single-channel recordings for high resolution with rapid voltage steps
    • Wonderlin W.F., Finkel A., and French R.J. Optimizing planar lipid bilayer single-channel recordings for high resolution with rapid voltage steps. Biophys. J. 58 (1990) 289-297
    • (1990) Biophys. J. , vol.58 , pp. 289-297
    • Wonderlin, W.F.1    Finkel, A.2    French, R.J.3
  • 36
    • 0032762996 scopus 로고    scopus 로고
    • Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single rna molecules
    • Akeson M., Branton D., Kasianowicz J.J., Brandin E., and Deamer D.W. Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single rna molecules. Biophys. J. 77 (1999) 3227-3233
    • (1999) Biophys. J. , vol.77 , pp. 3227-3233
    • Akeson, M.1    Branton, D.2    Kasianowicz, J.J.3    Brandin, E.4    Deamer, D.W.5
  • 37
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • Baumann G., and Mueller P. A molecular model of membrane excitability. J. Supramol. Struct. 2 (1974) 538-557
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 38
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
    • Fox R.O., and Richards F.M. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution. Nature 300 (1982) 325-330
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox, R.O.1    Richards, F.M.2
  • 40
    • 0023251067 scopus 로고
    • Alamethicin incorporation in lipid bilayers: a thermodynamic study
    • Rizzo V., Stankowski S., and Schwarz G. Alamethicin incorporation in lipid bilayers: a thermodynamic study. Biochemistry 26 (1987) 2751-2759
    • (1987) Biochemistry , vol.26 , pp. 2751-2759
    • Rizzo, V.1    Stankowski, S.2    Schwarz, G.3


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