메뉴 건너뛰기




Volumn 1778, Issue 12, 2008, Pages 2814-2822

The antimicrobial peptide gramicidin S permeabilizes phospholipid bilayer membranes without forming discrete ion channels

Author keywords

Antimicrobial peptide; Gramicidin S; Ion channel; Lipid bilayer membrane; Membrane conductance; Membrane defect

Indexed keywords

AMPHOLYTE; CHOLESTEROL; DIPHYTANOYLLECITHIN; DIPHYTANOYLPHOSPHATIDYLGLYCEROL; GRAMICIDIN S; ION CHANNEL; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 55749104221     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.08.017     Document Type: Article
Times cited : (57)

References (49)
  • 1
    • 0002336563 scopus 로고    scopus 로고
    • Are we on the threshold of the post-antibiotics era?
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, U.K
    • Lohner K., and Staudegger E. Are we on the threshold of the post-antibiotics era?. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, U.K 149-165
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 149-165
    • Lohner, K.1    Staudegger, E.2
  • 2
    • 0003401938 scopus 로고    scopus 로고
    • Origins and evolution of antibiotic and multiple antibiotic resistance in bacteria
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, U.K
    • Hall R.M., and Collis C.M. Origins and evolution of antibiotic and multiple antibiotic resistance in bacteria. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, U.K 1-15
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 1-15
    • Hall, R.M.1    Collis, C.M.2
  • 3
    • 0003160911 scopus 로고    scopus 로고
    • Antimicrobial peptides in innate immunity
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, U.K
    • Grantz T., and Lehrer R.I. Antimicrobial peptides in innate immunity. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, U.K 139-147
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 139-147
    • Grantz, T.1    Lehrer, R.I.2
  • 4
    • 1642495497 scopus 로고    scopus 로고
    • The commercial development of antimicrobial peptide pexiganam
    • Lohner K. (Ed), Horizon Scientific Press, Wymondham, U.K
    • Zasloff M. The commercial development of antimicrobial peptide pexiganam. In: Lohner K. (Ed). Development of Novel Antimicrobial Agents: Emerging Strategies (2001), Horizon Scientific Press, Wymondham, U.K 261-271
    • (2001) Development of Novel Antimicrobial Agents: Emerging Strategies , pp. 261-271
    • Zasloff, M.1
  • 5
    • 0037539998 scopus 로고    scopus 로고
    • Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S
    • Lee D.L., and Hosges R.S. Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S. Biopolymers 71 (2003) 28-48
    • (2003) Biopolymers , vol.71 , pp. 28-48
    • Lee, D.L.1    Hosges, R.S.2
  • 6
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., and Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462 (1999) 11-28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 7
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity
    • Sitaram N., and Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim. Biophys. Acta 1462 (1999) 29-54
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 8
    • 0001131165 scopus 로고
    • Gramicidin S and its use in the treatment of infected wounds
    • Gauge G.G., and Brazhnikova M.G. Gramicidin S and its use in the treatment of infected wounds. Nature 154 (1944) 703
    • (1944) Nature , vol.154 , pp. 703
    • Gauge, G.G.1    Brazhnikova, M.G.2
  • 10
    • 0003238774 scopus 로고
    • Recent advances in the biotechnology of β-lactams and microbial bioactive peptides
    • Kleinhaug H., and van Dohren H. (Eds), Walter de Gruyter Co., Berlin
    • Waki M., and Izumiya N. Recent advances in the biotechnology of β-lactams and microbial bioactive peptides. In: Kleinhaug H., and van Dohren H. (Eds). Biochemistry of Peptide Antibiotics (1990), Walter de Gruyter Co., Berlin 205-240
    • (1990) Biochemistry of Peptide Antibiotics , pp. 205-240
    • Waki, M.1    Izumiya, N.2
  • 11
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs
    • Kondejewski L.H., Farmer S.W., Wishart D.S., Kay C.M., Hancock R.E.W., and Hodges R.H. Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs. J. Biol. Chem. 271 (1996) 25261-25268
    • (1996) J. Biol. Chem. , vol.271 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.W.5    Hodges, R.H.6
  • 12
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondjewski L.H., Jelokhani-Niaraki M., Farmer S.W., Lix B., Kay C.M., Sykes B.D., Hancock R.E.W., and Hodges R.S. Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity. J. Biol. Chem. 274 (1999) 13181-13192
    • (1999) J. Biol. Chem. , vol.274 , pp. 13181-13192
    • Kondjewski, L.H.1    Jelokhani-Niaraki, M.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.W.7    Hodges, R.S.8
  • 13
    • 0034254229 scopus 로고    scopus 로고
    • Diastereoisomeric analogues of gramicidin S: structure, biological activity, and interaction with lipid bilayers
    • Jelokhani-Niaraki M., Kondejewski L.H., Farmer S.W., Hancock R.E.W., Kay C.M., and Hodges R.S. Diastereoisomeric analogues of gramicidin S: structure, biological activity, and interaction with lipid bilayers. Biochem. J. 349 (2000) 747-755
    • (2000) Biochem. J. , vol.349 , pp. 747-755
    • Jelokhani-Niaraki, M.1    Kondejewski, L.H.2    Farmer, S.W.3    Hancock, R.E.W.4    Kay, C.M.5    Hodges, R.S.6
  • 14
    • 0037016737 scopus 로고    scopus 로고
    • Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework
    • Kondjewski L.H., Lee D.L., Jelokhani-Niaraki M., Farmer S.W., Hancock R.E., and Hodges R.S. Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework. J. Biol. Chem. 277 (2002) 67-74
    • (2002) J. Biol. Chem. , vol.277 , pp. 67-74
    • Kondjewski, L.H.1    Lee, D.L.2    Jelokhani-Niaraki, M.3    Farmer, S.W.4    Hancock, R.E.5    Hodges, R.S.6
  • 15
    • 55949121413 scopus 로고    scopus 로고
    • M. Jelokhani-Niaraki, R.S. Hodges, J.E. Meissner, U.E. Hassenstein, L. Wheaton, Interaction of gramicidin S and its aromatic amino acid analogues with phospholipid membranes, Biophys. J. (in press), doi:10.1529/biophysj.108.137471 (BioFAST: July 11, 2008).
    • M. Jelokhani-Niaraki, R.S. Hodges, J.E. Meissner, U.E. Hassenstein, L. Wheaton, Interaction of gramicidin S and its aromatic amino acid analogues with phospholipid membranes, Biophys. J. (in press), doi:10.1529/biophysj.108.137471 (BioFAST: July 11, 2008).
  • 16
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer and biological membranes
    • Prenner E.J., Lewis R.N.A.H., and McElhaney R.N. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer and biological membranes. Biochim. Biophys. Acta 1462 (1999) 201-221
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 17
    • 33645493838 scopus 로고    scopus 로고
    • Biophysical studies of the interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner E.J., Lewis R.N.A.H., and McElhaney R.N. Biophysical studies of the interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Phys. Can. 60 (2004) 121-129
    • (2004) Phys. Can. , vol.60 , pp. 121-129
    • Prenner, E.J.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 18
    • 0033009036 scopus 로고    scopus 로고
    • Diffraction scanning calorimetry study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol bilayer membranes
    • Prenner E.J., Lewis R.N.A.H., Kondejewski L.H., Hodges R.S., and McElhaney R.N. Diffraction scanning calorimetry study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol bilayer membranes. Biochim. Biophys. Acta 147 (2001) 211-223
    • (2001) Biochim. Biophys. Acta , vol.147 , pp. 211-223
    • Prenner, E.J.1    Lewis, R.N.A.H.2    Kondejewski, L.H.3    Hodges, R.S.4    McElhaney, R.N.5
  • 19
    • 0035830596 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptides gramicidin S with dimyristoylphosphatidylcholine membranes: a densitometry and sound velocity study
    • Krivanek R., Rybar P., Prenner E.J., McElhaney R.N., and Hianik T. Interaction of the antimicrobial peptides gramicidin S with dimyristoylphosphatidylcholine membranes: a densitometry and sound velocity study. Biochim. Biophys. Acta 1510 (2001) 452-463
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 452-463
    • Krivanek, R.1    Rybar, P.2    Prenner, E.J.3    McElhaney, R.N.4    Hianik, T.5
  • 20
    • 0030853508 scopus 로고    scopus 로고
    • Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity
    • Prenner E.J., Lewis R.N.A.H., Kondejewski L.H., Hodges R.S., and McElhaney R.N. Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity. Biochemistry 36 (1997) 7906-7916
    • (1997) Biochemistry , vol.36 , pp. 7906-7916
    • Prenner, E.J.1    Lewis, R.N.A.H.2    Kondejewski, L.H.3    Hodges, R.S.4    McElhaney, R.N.5
  • 22
    • 0033576275 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes
    • Lewis R.N.A.H., Prenner E.J., Kondejewski L.H., Flach C.R., Mendelsohn R., Hodges R.S., and McElhaney R.N. Fourier transform infrared spectroscopic studies of the interaction of the antimicrobial peptide gramicidin S with lipid micelles and with lipid monolayer and bilayer membranes. Biochemistry 38 (1999) 15193-15203
    • (1999) Biochemistry , vol.38 , pp. 15193-15203
    • Lewis, R.N.A.H.1    Prenner, E.J.2    Kondejewski, L.H.3    Flach, C.R.4    Mendelsohn, R.5    Hodges, R.S.6    McElhaney, R.N.7
  • 23
    • 0035830591 scopus 로고    scopus 로고
    • Cholesterol attenuates the interaction of antimicrobial peptide gramicidin S with phospholipid bilayer membranes
    • Prenner E.J., Lewis R.N.A.H., Jelokhani-Niaraki M., Hodges R.S., and McElhaney R.N. Cholesterol attenuates the interaction of antimicrobial peptide gramicidin S with phospholipid bilayer membranes. Biochim. Biophys. Acta 1510 (2001) 83-92
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 83-92
    • Prenner, E.J.1    Lewis, R.N.A.H.2    Jelokhani-Niaraki, M.3    Hodges, R.S.4    McElhaney, R.N.5
  • 26
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia Coli
    • Wu M., Maier E., Benz R., and Hancock R.E.W. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia Coli. Biochemistry 38 (1999) 7235-7242
    • (1999) Biochemistry , vol.38 , pp. 7235-7242
    • Wu, M.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4
  • 27
    • 0016794454 scopus 로고
    • Electrical capacity of black lipid films and of lipid bilayers made from monolayers
    • Benz R., Frohlich O., Lauger P., and Montal M. Electrical capacity of black lipid films and of lipid bilayers made from monolayers. Biochim. Biophys. Acta 394 (1975) 323-334
    • (1975) Biochim. Biophys. Acta , vol.394 , pp. 323-334
    • Benz, R.1    Frohlich, O.2    Lauger, P.3    Montal, M.4
  • 28
    • 0000436494 scopus 로고
    • The effects of the macrotetralide actin antibiotics on the electrical properties of phospholipid bilayer membranes
    • Szabo G., EisenMann G., and Ciani S. The effects of the macrotetralide actin antibiotics on the electrical properties of phospholipid bilayer membranes. J. Membr. Biol. 1 (1969) 346-382
    • (1969) J. Membr. Biol. , vol.1 , pp. 346-382
    • Szabo, G.1    EisenMann, G.2    Ciani, S.3
  • 30
    • 0020630895 scopus 로고
    • Ion movement through gramicidin A channels - single-channel measurements at very high potentials
    • Andersen O.S. Ion movement through gramicidin A channels - single-channel measurements at very high potentials. Biophys. J. 41 (1983) 119-133
    • (1983) Biophys. J. , vol.41 , pp. 119-133
    • Andersen, O.S.1
  • 32
    • 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 Bamberg E. 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 1 (1977) 127-141
    • (1977) Biochim. Biophys. Acta , vol.464 , Issue.1 , pp. 127-141
    • Kolb, H.A.1    Bamberg, E.2
  • 33
    • 0030758516 scopus 로고    scopus 로고
    • The conformational preference of gramicidin channels is a function of lipid bilayer thickness
    • Mobasherry N., Nielsen C., and Andersen O.S. The conformational preference of gramicidin channels is a function of lipid bilayer thickness. FEBS Lett 412 1 (1997) 15-20
    • (1997) FEBS Lett , vol.412 , Issue.1 , pp. 15-20
    • Mobasherry, N.1    Nielsen, C.2    Andersen, O.S.3
  • 34
    • 0345254912 scopus 로고    scopus 로고
    • Genistein can modulate channel function by a phosphorylation-independent mechanism: importance of hydrophobic mismatch and bilayer mechanics
    • Hwang T.C., Koeppe II R.E., and Andersen O.S. Genistein can modulate channel function by a phosphorylation-independent mechanism: importance of hydrophobic mismatch and bilayer mechanics. Biochemistry 42 46 (2003) 13646-13658
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13646-13658
    • Hwang, T.C.1    Koeppe II, R.E.2    Andersen, O.S.3
  • 35
    • 0032228033 scopus 로고    scopus 로고
    • Phospholipid chain length alters the equilibrium between pore and channel forms of gramicidin
    • Galbraith T.P., and Wallace B.A. Phospholipid chain length alters the equilibrium between pore and channel forms of gramicidin. Faraday Discuss. 111 (1998) 159-164
    • (1998) Faraday Discuss. , vol.111 , pp. 159-164
    • Galbraith, T.P.1    Wallace, B.A.2
  • 36
    • 23944443237 scopus 로고    scopus 로고
    • Isothermal titration calorimetry studies of the binding of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes
    • Abraham T., Lewis R.N.A.H., Hodges R.S., and McElhaney R.N. Isothermal titration calorimetry studies of the binding of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes. Biochemistry 44 (2005) 11279-11285
    • (2005) Biochemistry , vol.44 , pp. 11279-11285
    • Abraham, T.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 37
    • 0016794454 scopus 로고
    • Electrical capacity of black lipid films and of lipid bilayers made from monolayers
    • Benz R., Fröhlich O., Läuger P., and Montal M. Electrical capacity of black lipid films and of lipid bilayers made from monolayers. Biochim. Biophys. Acta 394 3 (1975) 323-334
    • (1975) Biochim. Biophys. Acta , vol.394 , Issue.3 , pp. 323-334
    • Benz, R.1    Fröhlich, O.2    Läuger, P.3    Montal, M.4
  • 38
    • 0018087411 scopus 로고
    • Formation of "solvent free" black lipid bilayer membrane from glyceryl monooleate dispersed in squalene
    • White S.H. Formation of "solvent free" black lipid bilayer membrane from glyceryl monooleate dispersed in squalene. Biophys. J. 23 (1978) 337-347
    • (1978) Biophys. J. , vol.23 , pp. 337-347
    • White, S.H.1
  • 39
    • 0015760624 scopus 로고
    • The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes
    • Eisenberg M., Hall J.E., and Mead C.A. The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes. J. Membr. Biol. 14 (1973) 143-176
    • (1973) J. Membr. Biol. , vol.14 , pp. 143-176
    • Eisenberg, M.1    Hall, J.E.2    Mead, C.A.3
  • 40
    • 0016697413 scopus 로고
    • Toward a molecular understanding of excitability: alamethicin in black lipid films
    • Hall J.E. Toward a molecular understanding of excitability: alamethicin in black lipid films. Biophys. J. 15 (1975) 934-939
    • (1975) Biophys. J. , vol.15 , pp. 934-939
    • Hall, J.E.1
  • 41
    • 0017872580 scopus 로고
    • Analysis of the multi-pore system of alamethicin in a lipid membrane. II. Autocorrelation analysis and power spectral density
    • Kolb H.A., and Boheim G. Analysis of the multi-pore system of alamethicin in a lipid membrane. II. Autocorrelation analysis and power spectral density. J. Membr. Biol. 38 (1978) 151-191
    • (1978) J. Membr. Biol. , vol.38 , pp. 151-191
    • Kolb, H.A.1    Boheim, G.2
  • 42
    • 0019458461 scopus 로고
    • Voltage-dependent channels in planar lipid bilayer membranes
    • Latorre R., and Alvarez R. 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, R.2
  • 44
    • 0028860483 scopus 로고
    • Two classes of alamethicin transmembrane channels: molecular models from single-channel properties
    • Mak D.O., and Webb W.W. Two classes of alamethicin transmembrane channels: molecular models from single-channel properties. Biophys. J. 69 (1995) 2323-2336
    • (1995) Biophys. J. , vol.69 , pp. 2323-2336
    • Mak, D.O.1    Webb, W.W.2
  • 46
    • 33847037505 scopus 로고    scopus 로고
    • Structure and mechanism of action of the antimicrobial peptide piscidin
    • Campagna S., Saint N., Molle G., and Aumelas A. Structure and mechanism of action of the antimicrobial peptide piscidin. Biochemistry 46 (2007) 1771-1778
    • (2007) Biochemistry , vol.46 , pp. 1771-1778
    • Campagna, S.1    Saint, N.2    Molle, G.3    Aumelas, A.4
  • 47
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He K., Ludtke S.J., and Huang H.W. Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry 36 (1995) 15614-15618
    • (1995) Biochemistry , vol.36 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3
  • 48
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: magainins, secropins, melittin and alamethicin
    • Bechinger B. Structure and functions of channel-forming peptides: magainins, secropins, melittin and alamethicin. J. Membr. Biol. 156 (1997) 197-211
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 49
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462 (1999) 157-183
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.