메뉴 건너뛰기




Volumn 77, Issue 1, 1999, Pages 299-305

Effect of gramicidin A on the dipole potential of phospholipid membranes

Author keywords

[No Author keywords available]

Indexed keywords

DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPHYTANOYLLECITHIN; DISTEAROYLPHOSPHATIDYLCHOLINE; FLUORESCENT DYE; GRAMICIDIN A; LIPOSOME; N (4 SULFOBUTYL) 4 [4 [4 (DIPENTYLAMINO)PHENYL]BUTANDIENYL]PYRIDINIUM; PHLORETIN; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 0032974758     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76890-6     Document Type: Article
Times cited : (45)

References (42)
  • 1
    • 0028335099 scopus 로고
    • Conformation states of gramicidin A along the pathway to the formation of channels in model membranes determined by 2D NMR and circular dichroism spectroscopy
    • Abdul-Manan, N., and J. F. Hinton. 1994. Conformation states of gramicidin A along the pathway to the formation of channels in model membranes determined by 2D NMR and circular dichroism spectroscopy. Biochemistry. 33:6773-6783.
    • (1994) Biochemistry , vol.33 , pp. 6773-6783
    • Abdul-Manan, N.1    Hinton, J.F.2
  • 2
    • 0001798441 scopus 로고
    • Ion transport across simple membranes
    • G. H. Giebisch and E. F. Purcell, editors. Jociah Macy, Jr., Foundation, New York
    • Andersen, O. S. 1978. Ion transport across simple membranes. In Renal Function. G. H. Giebisch and E. F. Purcell, editors. Jociah Macy, Jr., Foundation, New York. 71-99.
    • (1978) Renal Function , pp. 71-99
    • Andersen, O.S.1
  • 3
    • 0017161652 scopus 로고
    • Effect of phloretin on the permeability of thin lipid membranes
    • Andersen, O. S., A. Finkelstein, and I. Kate. 1976. Effect of phloretin on the permeability of thin lipid membranes. J. Gen. Physiol. 67:749-771.
    • (1976) J. Gen. Physiol. , vol.67 , pp. 749-771
    • Andersen, O.S.1    Finkelstein, A.2    Kate, I.3
  • 4
    • 0000346708 scopus 로고
    • Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR spectroscopy and energy refinement
    • Arseniev, A. S., A. L. Lomize, I. L. Barsukov, and V. F. Bystrov. 1986. Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR spectroscopy and energy refinement. Biol. Membr. 3:1077-1103.
    • (1986) Biol. Membr. , vol.3 , pp. 1077-1103
    • Arseniev, A.S.1    Lomize, A.L.2    Barsukov, I.L.3    Bystrov, V.F.4
  • 5
    • 0025721931 scopus 로고
    • Amino acid sequence modulation of gramicidin channel function: Effects of tryptophan-to-phenylalanine substitutions on the single-channel conductance and duration
    • Becker, M. D., D. V. Greathouse, R. E. Koeppe, II, and O. S. Andersen. 1991. Amino acid sequence modulation of gramicidin channel function: effects of tryptophan-to-phenylalanine substitutions on the single-channel conductance and duration. Biochemistry. 30:8830-8839.
    • (1991) Biochemistry , vol.30 , pp. 8830-8839
    • Becker, M.D.1    Greathouse, D.V.2    Koeppe R.E. II3    Andersen, O.S.4
  • 6
    • 0027142557 scopus 로고
    • Solvent history dependence of gramicidin-lipid interactions: A Raman and infrared spectroscopic study
    • Bouchard, M., and M. Auger. 1993. Solvent history dependence of gramicidin-lipid interactions: a Raman and infrared spectroscopic study. Biophys. J. 65:2484-2492.
    • (1993) Biophys. J. , vol.65 , pp. 2484-2492
    • Bouchard, M.1    Auger, M.2
  • 7
    • 0027982642 scopus 로고
    • Dipole potential of lipid membranes
    • Brockman, H. 1994. Dipole potential of lipid membranes. Chem. Phys. Lipids. 73:57-79.
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 57-79
    • Brockman, H.1
  • 8
    • 0027533833 scopus 로고
    • The use of physical methods in determining gramicidin channel structure and function
    • Busath, D. D. 1993. The use of physical methods in determining gramicidin channel structure and function. Annu. Rev. Physiol. 55:473-501.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 473-501
    • Busath, D.D.1
  • 10
    • 0031958516 scopus 로고    scopus 로고
    • Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide
    • Cladera, J., and P. O'Shea. 1998. Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide. Biophys. J. 74:2434-2442.
    • (1998) Biophys. J. , vol.74 , pp. 2434-2442
    • Cladera, J.1    O'Shea, P.2
  • 11
    • 0030757379 scopus 로고    scopus 로고
    • Effect of lipid structure on the dipole potential of phosphatidylcholine bilayers
    • Clarke, R. J. 1997. Effect of lipid structure on the dipole potential of phosphatidylcholine bilayers. Biochim. Biophys. Acta. 1327:269-278.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 269-278
    • Clarke, R.J.1
  • 12
    • 0031012421 scopus 로고    scopus 로고
    • Optical detection of membrane dipole potential: Avoidance of fluidity and dye-induced effects
    • Clarke, R. J., and D. J. Kane. 1997. Optical detection of membrane dipole potential: avoidance of fluidity and dye-induced effects. Biochim. Biophys. Acta. 1323:223-239.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 223-239
    • Clarke, R.J.1    Kane, D.J.2
  • 13
    • 0031910472 scopus 로고    scopus 로고
    • The adsorption of phloretin to lipid monolayers and bilayers cannot be explained by langmuir adsorption isotherms alone
    • Cseh, R., and R. Benz. 1998. The adsorption of phloretin to lipid monolayers and bilayers cannot be explained by Langmuir adsorption isotherms alone. Biophys. J. 74:1399-1408.
    • (1998) Biophys. J. , vol.74 , pp. 1399-1408
    • Cseh, R.1    Benz, R.2
  • 14
    • 0027177939 scopus 로고
    • Internal electrostatic potentials in bilayers - Measuring and controlling dipole potentials in lipid vesicles
    • Franklin, J. C., and D. S. Cafiso. 1993. Internal electrostatic potentials in bilayers - measuring and controlling dipole potentials in lipid vesicles. Biophys. J. 65:289-299.
    • (1993) Biophys. J. , vol.65 , pp. 289-299
    • Franklin, J.C.1    Cafiso, D.S.2
  • 16
    • 0028284842 scopus 로고
    • Dual-wavelength ratio-metric fluorescence measurement of the membrane dipole potential
    • Gross, E., R. S. Bedlack, and L. M. Loew. 1994. Dual-wavelength ratio-metric fluorescence measurement of the membrane dipole potential. Biophys. J. 67:208-216.
    • (1994) Biophys. J. , vol.67 , pp. 208-216
    • Gross, E.1    Bedlack, R.S.2    Loew, L.M.3
  • 18
    • 0031835569 scopus 로고    scopus 로고
    • Submicron structure in L-α-dipalmitoylphosphatidylcholine monolayers and bilayers probed with confocal, atomic force, and near-field microscopy
    • Hollars, C. W., and R. C. Dunn. 1998. Submicron structure in L-α-dipalmitoylphosphatidylcholine monolayers and bilayers probed with confocal, atomic force, and near-field microscopy. Biophys. J. 75: 342-353.
    • (1998) Biophys. J. , vol.75 , pp. 342-353
    • Hollars, C.W.1    Dunn, R.C.2
  • 19
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel
    • Hu, W., K. C. Lee, and T. A. Cross. 1993. Tryptophans in membrane proteins: indole ring orientations and functional implications in the gramicidin channel. Biochemistry. 32:7035-7047.
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.C.2    Cross, T.A.3
  • 20
    • 0028787147 scopus 로고
    • Tryptophan hydrogen bonding and electric dipole moments: Functional roles in the gramicidin channel and implications for membrane proteins
    • Hu, W., and T. A. Cross. 1995. Tryptophan hydrogen bonding and electric dipole moments: functional roles in the gramicidin channel and implications for membrane proteins. Biochemistry. 34:14147-14155.
    • (1995) Biochemistry , vol.34 , pp. 14147-14155
    • Hu, W.1    Cross, T.A.2
  • 21
    • 0028842124 scopus 로고
    • The structure and stability of phospholipid bilayers by atomic force microscopy
    • Hui, S. W., R. Viswanathan, J. A. Zasadzinski, and J. N. Israelachvili. 1995. The structure and stability of phospholipid bilayers by atomic force microscopy. Biophys. J. 68:171-178.
    • (1995) Biophys. J. , vol.68 , pp. 171-178
    • Hui, S.W.1    Viswanathan, R.2    Zasadzinski, J.A.3    Israelachvili, J.N.4
  • 22
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem, R. R., W. Hu, and T. A. Cross. 1993. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science. 261:1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 23
    • 0026473040 scopus 로고
    • Gramicidin and gramicidin-lipid interactions
    • Killian, J. A. 1992. Gramicidin and gramicidin-lipid interactions. Biochim. Biophys. Acta. 1113:391-425.
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 391-425
    • Killian, J.A.1
  • 25
    • 0017369257 scopus 로고
    • Influence of membrane thickness and ion concentration on the properties of the gramicidin A channel. Autocorrelation, spectral power density, relaxation and single-channel studies
    • Kolb, H. A., and E. Bamberg. 1977. Influence of membrane thickness and ion concentration on the properties of the gramicidin A channel. Autocorrelation, spectral power density, relaxation and single-channel studies. Biochim. Biophys. Acta. 464:127-141.
    • (1977) Biochim. Biophys. Acta , vol.464 , pp. 127-141
    • Kolb, H.A.1    Bamberg, E.2
  • 27
    • 0006081918 scopus 로고
    • Permeability of biomolecular phospholipid membranes for fat-soluble ions
    • Liberman, E. A., and V. P. Topaly. 1969. Permeability of biomolecular phospholipid membranes for fat-soluble ions. Biophysics. 14:477-487.
    • (1969) Biophysics , vol.14 , pp. 477-487
    • Liberman, E.A.1    Topaly, V.P.2
  • 28
    • 0023353671 scopus 로고
    • Lipid monolayer states and their relationships to bilayers
    • MacDonald, R. C., and S. A. Simon. 1987. Lipid monolayer states and their relationships to bilayers. Proc. Natl. Acad. Sci. USA. 84:4089-4093.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4089-4093
    • MacDonald, R.C.1    Simon, S.A.2
  • 29
    • 0017357683 scopus 로고
    • Phloretin-induced changes in ion transport across lipid bilayer membranes
    • Melnik, E., R. Latorre, J. E. Hall, and D. C. Tosteson. 1977. Phloretin-induced changes in ion transport across lipid bilayer membranes. J. Gen. Physiol. 69:243-257.
    • (1977) J. Gen. Physiol. , vol.69 , pp. 243-257
    • Melnik, E.1    Latorre, R.2    Hall, J.E.3    Tosteson, D.C.4
  • 30
    • 0030012156 scopus 로고    scopus 로고
    • Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers
    • Mou, J. X., D. M. Czajkowsky, and Z. F. Shao. 1996. Gramicidin A aggregation in supported gel state phosphatidylcholine bilayers. Biochemistry. 35:3222-3226.
    • (1996) Biochemistry , vol.35 , pp. 3222-3226
    • Mou, J.X.1    Czajkowsky, D.M.2    Shao, Z.F.3
  • 31
    • 0030572286 scopus 로고    scopus 로고
    • Three-capacitor model for surface potential of insoluble monolayers
    • Petrov, J. G., Polymeropoulos, E. E., and H. Moehwald. 1996. Three-capacitor model for surface potential of insoluble monolayers. J. Phys. Chem. 100:9860-9869.
    • (1996) J. Phys. Chem. , vol.100 , pp. 9860-9869
    • Petrov, J.G.1    Polymeropoulos, E.E.2    Moehwald, H.3
  • 32
    • 0031022072 scopus 로고    scopus 로고
    • Permeation of phloretin across bilayer lipid membranes monitored by dipole potential and microelectrode measurements
    • Pohl, P., T. I. Rokitskaya, E. E. Pohl, and S. M. Saparov. 1997. Permeation of phloretin across bilayer lipid membranes monitored by dipole potential and microelectrode measurements. Biochim. Biophys. Acta. 1323:163-172.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 163-172
    • Pohl, P.1    Rokitskaya, T.I.2    Pohl, E.E.3    Saparov, S.M.4
  • 34
    • 0020584454 scopus 로고
    • Phloretin and phloretin analogues: Mode of action in planar lipid bilayers and monolayers
    • Reyes, J., F. Greco, R. Montals, and R. Latorre. 1983. Phloretin and phloretin analogues: mode of action in planar lipid bilayers and monolayers. J. Membr. Biol. 72:93-103.
    • (1983) J. Membr. Biol. , vol.72 , pp. 93-103
    • Reyes, J.1    Greco, F.2    Montals, R.3    Latorre, R.4
  • 35
    • 0030851433 scopus 로고    scopus 로고
    • Effect of the dipole potential of a bilayer lipid membrane on gramicidin channel dissociation kinetics
    • Rokitskaya, T. I., Y. N. Antonenko, and E. A. Kotova. 1997. Effect of the dipole potential of a bilayer lipid membrane on gramicidin channel dissociation kinetics. Biophys. J. 73:850-854.
    • (1997) Biophys. J. , vol.73 , pp. 850-854
    • Rokitskaya, T.I.1    Antonenko, Y.N.2    Kotova, E.A.3
  • 36
    • 0024453540 scopus 로고
    • Reversible binding of substance P to artificial lipid membranes studied by capacitance minimization techniques
    • Sargent, D. F., J. W. Bean, and R. Schwyzer. 1989. Reversible binding of substance P to artificial lipid membranes studied by capacitance minimization techniques. Biophys. Chem. 34:103-114.
    • (1989) Biophys. Chem. , vol.34 , pp. 103-114
    • Sargent, D.F.1    Bean, J.W.2    Schwyzer, R.3
  • 37
    • 0029053366 scopus 로고
    • Gramicidin tryptophans mediate formamidinium-induced channel stabilization
    • Seoh, S. A., and D. Busath. 1995. Gramicidin tryptophans mediate formamidinium-induced channel stabilization. Biophys. J. 68:2271-2279.
    • (1995) Biophys. J. , vol.68 , pp. 2271-2279
    • Seoh, S.A.1    Busath, D.2
  • 38
    • 0031551413 scopus 로고    scopus 로고
    • Interaction of hydrophobic ions with a Langmuir monolayer of dioctadecyldimethylammonium bromide
    • Shapovalov, V., and A. Tronin. 1998. Interaction of hydrophobic ions with a Langmuir monolayer of dioctadecyldimethylammonium bromide. Langmuir. 13:4870-4875.
    • (1998) Langmuir. , vol.13 , pp. 4870-4875
    • Shapovalov, V.1    Tronin, A.2
  • 40
    • 0023707816 scopus 로고
    • Mixed monolayers of linear gramicidins and phospholipid. Surface pressure and surface potential studies
    • Van Mau, N., Y. Trudelle, P. Daumas, and F. Heitz. 1988. Mixed monolayers of linear gramicidins and phospholipid. Surface pressure and surface potential studies. Biophys. J. 54:563-567.
    • (1988) Biophys. J. , vol.54 , pp. 563-567
    • Van Mau, N.1    Trudelle, Y.2    Daumas, P.3    Heitz, F.4
  • 41
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Woolf, T. B., and B. Roux. 1996. Structure, energetics, and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins. 24:92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 42
    • 0029914156 scopus 로고    scopus 로고
    • + channels in growth cones versus somata of neuroblastoma N1E-115 cells
    • + channels in growth cones versus somata of neuroblastoma N1E-115 cells, Biophys. J. 71:2501-2508.
    • (1996) Biophys. J. , vol.71 , pp. 2501-2508
    • Zhang, J.1    Loew, L.M.2    Davidson, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.