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Volumn 1468, Issue 1-2, 2000, Pages 213-230

X-ray studies on the interaction of the antimicrobial peptide gramicidin S with microbial lipid extracts: Evidence for cubic phase formation

Author keywords

Antimicrobial peptide; Gramicidin S; Lipid peptide interaction; Microbial lipid; Non lamellar phase; Phospholipid

Indexed keywords

AMPHOLYTE; GLYCOLIPID; GRAMICIDIN S; MEMBRANE LIPID; MEMBRANE PHOSPHOLIPID;

EID: 0034730576     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(00)00260-1     Document Type: Article
Times cited : (77)

References (70)
  • 1
    • 0001131165 scopus 로고
    • Gramicidin S and its use in the treatment of infected wounds
    • Gause G.F., Brazhnikova M.G. Gramicidin S and its use in the treatment of infected wounds. Nature. 154:1944;703.
    • (1944) Nature , vol.154 , pp. 703
    • Gause, G.F.1    Brazhnikova, M.G.2
  • 3
    • 0003238774 scopus 로고
    • Recent advances in the biotechnology of β-lactams and microbial bioactive peptides
    • in: H. Kleinhaug, H. van Doren (Eds.), de Gruyter, Berlin
    • M. Waki, N. Izumiya, Recent advances in the biotechnology of β-lactams and microbial bioactive peptides, in: H. Kleinhaug, H. van Doren (Eds.), Biochemistry of Peptide Antibiotics, de Gruyter, Berlin, 1990, pp. 205-244.
    • (1990) Biochemistry of Peptide Antibiotics , pp. 205-244
    • Waki, M.1    Izumiya, N.2
  • 5
    • 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., Hodges R.S. 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.S.6
  • 7
    • 0017382706 scopus 로고
    • Conformations of di-N-methylleucine gramicidin S and N-methylleucine gramicidin S compatible with the sidedness hypothesis
    • Kato T., Izumiya N. Conformations of di-N-methylleucine gramicidin S and N-methylleucine gramicidin S compatible with the sidedness hypothesis. Biochim. Biophys. Acta. 493:1977;235-238.
    • (1977) Biochim. Biophys. Acta , vol.493 , pp. 235-238
    • Kato, T.1    Izumiya, N.2
  • 8
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner E.J., Lewis R.N.A.H., McElhaney R.N. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model 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
  • 9
    • 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., Neuman K.C., Gruner S.M., Kondejewski L.H., Hodges R.S., 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    Neuman, K.C.3    Gruner, S.M.4    Kondejewski, L.H.5    Hodges, R.S.6    McElhaney, R.N.7
  • 10
    • 0017902280 scopus 로고
    • 31P Nuclear magnetic resonance and the headgroup structure of phospholipid membranes
    • 31P Nuclear magnetic resonance and the headgroup structure of phospholipid membranes. Biochim. Biophys. Acta. 515:1978;105-140.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 12
    • 0019320887 scopus 로고
    • Lipid and protein composition and thermotropic lipid phase transitions in fatty acid-homogeneous membranes of Acholeplasma laidlawii B
    • Silvius J.R., Mak N., McElhaney R.N. Lipid and protein composition and thermotropic lipid phase transitions in fatty acid-homogeneous membranes of Acholeplasma laidlawii B. Biochim. Biophys. Acta. 597:1980;199-215.
    • (1980) Biochim. Biophys. Acta , vol.597 , pp. 199-215
    • Silvius, J.R.1    Mak, N.2    McElhaney, R.N.3
  • 13
    • 0026977703 scopus 로고
    • SWAX - A dual detector camera for simultaneous small- And wide-angle X-ray diffraction in polymer and liquid crystal research
    • Laggner P., Mio H. SWAX - a dual detector camera for simultaneous small- and wide-angle X-ray diffraction in polymer and liquid crystal research. Nucl. Inst. Methods Phys. Res. A. 323:1992;86-90.
    • (1992) Nucl. Inst. Methods Phys. Res. a , vol.323 , pp. 86-90
    • Laggner, P.1    Mio, H.2
  • 15
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter O. A new method for the evaluation of small-angle scattering data. J. Appl. Crystallogr. 10:1977;415-421.
    • (1977) J. Appl. Crystallogr. , vol.10 , pp. 415-421
    • Glatter, O.1
  • 16
    • 0002417327 scopus 로고
    • Data Treatment
    • in: O. Glatter, O. Kratky (Eds.), Academic Press, London
    • O. Glatter, Data Treatment, in: O. Glatter, O. Kratky (Eds.), Small Angle X-Ray Scattering, Academic Press, London, 1982, pp. 119-166.
    • (1982) Small Angle X-Ray Scattering , pp. 119-166
    • Glatter, O.1
  • 17
    • 0001372919 scopus 로고
    • Interpretation
    • in: O. Glatter, O. Kratky (Eds.), Academic Press, London
    • O. Glatter, Interpretation, in: O. Glatter, O. Kratky (Eds.), Small Angle X-Ray Scattering, Academic Press, London, 1982, pp. 167-196.
    • (1982) Small Angle X-Ray Scattering , pp. 167-196
    • Glatter, O.1
  • 18
    • 0015935391 scopus 로고
    • Structure and polymorphism of the hydrocarbon chains of lipids: A study of lecithin-water phases
    • Tardieu A., Luzatti V., Reman F.C. Structure and polymorphism of the hydrocarbon chains of lipids: a study of lecithin-water phases. J. Mol. Biol. 75:1973;711-733.
    • (1973) J. Mol. Biol. , vol.75 , pp. 711-733
    • Tardieu, A.1    Luzatti, V.2    Reman, F.C.3
  • 19
    • 0027445292 scopus 로고
    • Small angle X-ray scattering: Possibilities and limitations in characterization of vesicles
    • Bouwstra J.A., Gooris G.S., Bras W., Talsma H. Small angle X-ray scattering: possibilities and limitations in characterization of vesicles. Chem. Phys. Lipids. 64:1993;83-98.
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 83-98
    • Bouwstra, J.A.1    Gooris, G.S.2    Bras, W.3    Talsma, H.4
  • 20
    • 0020481078 scopus 로고
    • Evidence of bilayer structure and of membrane interactions from X-ray diffraction analysis
    • Blaurock A.E. Evidence of bilayer structure and of membrane interactions from X-ray diffraction analysis. Biochim. Biophys. Acta. 650:1982;167-207.
    • (1982) Biochim. Biophys. Acta , vol.650 , pp. 167-207
    • Blaurock, A.E.1
  • 21
    • 0025134135 scopus 로고
    • II) phase, and non-lamellar phase transitions of lipids
    • II) phase, and non-lamellar phase transitions of lipids. Biochim. Biophys. Acta. 1031:1990;1-69.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 22
    • 0024291641 scopus 로고
    • X-ray diffraction study of the polymorphic behavior of N-methylated dioleoylphosphatidylethanolamine
    • Gruner S.M., Tate M.W., Kirk G.L., So P.T., Turner D.C., Keane D.T. X-ray diffraction study of the polymorphic behavior of N-methylated dioleoylphosphatidylethanolamine. Biochemistry. 27:1988;2853-2866.
    • (1988) Biochemistry , vol.27 , pp. 2853-2866
    • Gruner, S.M.1    Tate, M.W.2    Kirk, G.L.3    So, P.T.4    Turner, D.C.5    Keane, D.T.6
  • 24
    • 0031848842 scopus 로고    scopus 로고
    • Accelerated formation of cubic phases in phosphatidylethanolamine dispersions
    • Tenchov B., Koynova R., Rapp G. Accelerated formation of cubic phases in phosphatidylethanolamine dispersions. Biophys. J. 75:1998;853-866.
    • (1998) Biophys. J. , vol.75 , pp. 853-866
    • Tenchov, B.1    Koynova, R.2    Rapp, G.3
  • 25
    • 0025005039 scopus 로고
    • Physical properties of glycosyl diacylglycerols. 2. X-ray diffraction studies of a homologous series of 1,2-di-O-acyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerols
    • Sen A., Hui S.W., Mannock D.A., Lewis R.N.A.H., McElhaney R.N. Physical properties of glycosyl diacylglycerols. 2. X-ray diffraction studies of a homologous series of 1,2-di-O-acyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerols. Biochemistry. 29:1990;7799-7804.
    • (1990) Biochemistry , vol.29 , pp. 7799-7804
    • Sen, A.1    Hui, S.W.2    Mannock, D.A.3    Lewis, R.N.A.H.4    McElhaney, R.N.5
  • 26
    • 0031738220 scopus 로고    scopus 로고
    • Total lipids with short and long acyl chains from Acholeplasma form nonlamellar phases
    • Andersson A.-S., Rilfors L., Orädd G., Lindblom G. Total lipids with short and long acyl chains from Acholeplasma form nonlamellar phases. Biophys. J. 75:1998;2877-2887.
    • (1998) Biophys. J. , vol.75 , pp. 2877-2887
    • Andersson, A.-S.1    Rilfors, L.2    Orädd, G.3    Lindblom, G.4
  • 27
    • 0024603546 scopus 로고
    • Cubic phases and isotropic structures formed by membrane lipids - possible biological significance
    • Lindblom G., Rilfors L. Cubic phases and isotropic structures formed by membrane lipids - possible biological significance. Biochim. Biophys. Acta. 988:1989;221-256.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 221-256
    • Lindblom, G.1    Rilfors, L.2
  • 28
  • 29
    • 0025317415 scopus 로고
    • P-31 nuclear magnetic resonance studies of the appearance of an isotropic component in dielaidoylphosphatidylethanolamine
    • Veiro J.A., Khalifah R.G., Rowe E.S. P-31 nuclear magnetic resonance studies of the appearance of an isotropic component in dielaidoylphosphatidylethanolamine. Biophys. J. 57:1990;637-641.
    • (1990) Biophys. J. , vol.57 , pp. 637-641
    • Veiro, J.A.1    Khalifah, R.G.2    Rowe, E.S.3
  • 30
    • 0029975929 scopus 로고    scopus 로고
    • Wild-type Escherichia coli cells regulate the membrane lipid composition in a 'window' between gel and non-lamellar structures
    • Morein S., Andersson A.-S., Rilfors L., Lindblom G. Wild-type Escherichia coli cells regulate the membrane lipid composition in a 'window' between gel and non-lamellar structures. J. Biol. Chem. 271:1996;6801-6809.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6801-6809
    • Morein, S.1    Andersson, A.-S.2    Rilfors, L.3    Lindblom, G.4
  • 31
    • 0001095136 scopus 로고
    • Membrane Fluidity
    • in: M. Kates, L.A. Mason (Eds.), Plenum Press, New York
    • L. Rilfors, G. Lindblom, A. Wieslander, A. Christiansson, Membrane Fluidity, in: M. Kates, L.A. Mason (Eds.), Biomembranes, Vol. 12, Plenum Press, New York, 1984, pp. 205-245.
    • (1984) Biomembranes , vol.12 , pp. 205-245
    • Rilfors, L.1    Lindblom, G.2    Wieslander, A.3    Christiansson, A.4
  • 32
    • 0027346050 scopus 로고
    • Regulation and physicochemical properties of the polar lipids in Acholeplasma laidlawii
    • in: S. Rottem, I. Kahane (Eds.), Plenum Press, New York
    • L. Rilfors, A. Wieslander, G. Lindblom, Regulation and physicochemical properties of the polar lipids in Acholeplasma laidlawii, in: S. Rottem, I. Kahane (Eds.), Subcellular Biochemistry, Vol. 20, Plenum Press, New York, 1993, pp. 109-166.
    • (1993) Subcellular Biochemistry , vol.20 , pp. 109-166
    • Rilfors, L.1    Wieslander, A.2    Lindblom, G.3
  • 33
    • 0028835134 scopus 로고
    • Quantitation of the phase preferences of the major lipids of the Acholeplasma laidlawii B membrane
    • Foht P.J., Tran Q.M., Lewis R.N.A.H., McElhaney R.N. Quantitation of the phase preferences of the major lipids of the Acholeplasma laidlawii B membrane. Biochemistry. 34:1995;13811-13817.
    • (1995) Biochemistry , vol.34 , pp. 13811-13817
    • Foht, P.J.1    Tran, Q.M.2    Lewis, R.N.A.H.3    McElhaney, R.N.4
  • 34
    • 0001223593 scopus 로고
    • in: J. Maniloff, R.N. McElhaney, L.R. Finch, J.B. Baseman (Eds.), American Society for Microbiology, Washington, DC
    • R.N. McElhaney, in: J. Maniloff, R.N. McElhaney, L.R. Finch, J.B. Baseman (Eds.), Mycoplasma: Molecular Biology and Pathogenesis, American Society for Microbiology, Washington, DC, 1992, pp. 113-155.
    • (1992) Mycoplasma: Molecular Biology and Pathogenesis , pp. 113-155
    • McElhaney, R.N.1
  • 35
    • 0024711084 scopus 로고
    • Effects of lipid packing on polymorphic phase behavior and membrane properties
    • Hui S.-W., Sen A. Effects of lipid packing on polymorphic phase behavior and membrane properties. Proc. Natl. Acad. Sci. USA. 86:1989;5825-5829.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5825-5829
    • Hui, S.-W.1    Sen, A.2
  • 36
    • 0002013329 scopus 로고
    • Non-lamellar lipid phases
    • in: P.L. Yeagle (Ed.), CRC Press, Boca Raton, FL
    • S.M. Gruner, Non-lamellar lipid phases, in: P.L. Yeagle (Ed.), Structure of Biological Membranes, CRC Press, Boca Raton, FL, 1992, pp. 211-250.
    • (1992) Structure of Biological Membranes , pp. 211-250
    • Gruner, S.M.1
  • 37
    • 0030586129 scopus 로고    scopus 로고
    • Is the high propensity of ethanolamine plasmalogens to form non-lamellar lipid structures manifested in the properties of biomembranes?
    • Lohner K. Is the high propensity of ethanolamine plasmalogens to form non-lamellar lipid structures manifested in the properties of biomembranes? Chem. Phys. Lipids. 81:1996;167-184.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 167-184
    • Lohner, K.1
  • 39
    • 22644440788 scopus 로고
    • A cubic structure consisting of a lipid bilayer forming an infinite periodic minimum surface of the gyroid type in the glyceromonooleate-water system
    • Hyde S., Andersson S., Ericsson B., Larsson K. A cubic structure consisting of a lipid bilayer forming an infinite periodic minimum surface of the gyroid type in the glyceromonooleate-water system. Z. Krystallogr. 168:1984;213-219.
    • (1984) Z. Krystallogr. , vol.168 , pp. 213-219
    • Hyde, S.1    Andersson, S.2    Ericsson, B.3    Larsson, K.4
  • 40
    • 0030048521 scopus 로고    scopus 로고
    • Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures
    • Keller S.L., Gruner S.M., Gawrisch K. Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures. Biochim. Biophys. Acta. 1127:1996;241-246.
    • (1996) Biochim. Biophys. Acta , vol.1127 , pp. 241-246
    • Keller, S.L.1    Gruner, S.M.2    Gawrisch, K.3
  • 41
    • 0029022547 scopus 로고
    • X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: Diphytanoyl phosphatidylcholine with alamethicin at low concentrations
    • Wu Y., He K., Ludtke S.J., Huang H.W. X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicin at low concentrations. Biophys. J. 68:1995;2361-2369.
    • (1995) Biophys. J. , vol.68 , pp. 2361-2369
    • Wu, Y.1    He, K.2    Ludtke, S.J.3    Huang, H.W.4
  • 42
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He K., Ludtke S.J., Heller W.T., Huang H.W. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71:1996;2669-2897.
    • (1996) Biophys. J. , vol.71 , pp. 2669-2897
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 43
    • 0029594533 scopus 로고
    • Membrane thinning caused by magainin 2
    • Ludtke S.J., He K., Huang H.W. Membrane thinning caused by magainin 2. Biochemistry. 34:1995;16764-16769.
    • (1995) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.J.1    He, K.2    Huang, H.W.3
  • 44
    • 0028010757 scopus 로고
    • Cooperative membrane insertion of magainin correlated with its cytolytic activity
    • Ludtke S.J., He K., Wu Y., Huang H.W. Cooperative membrane insertion of magainin correlated with its cytolytic activity. Biochim. Biophys. Acta. 1190:1994;181-184.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 181-184
    • Ludtke, S.J.1    He, K.2    Wu, Y.3    Huang, H.W.4
  • 46
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand R.M. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta. 1376:1998;353-368.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 47
    • 0032718949 scopus 로고    scopus 로고
    • Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems
    • Lohner K., Prenner E.J. Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems. Biochim. Biophys. Acta. 1462:1999;141-156.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 141-156
    • Lohner, K.1    Prenner, E.J.2
  • 48
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht T., Dathe M., Epand R.M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., Bienert M. Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry. 36:1997;12869-12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 50
    • 0027369494 scopus 로고
    • Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes - cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability
    • Tytler E.M., Segrest J.P., Epand R.M., Nie S.-Q., Epand R.F., Mishra V.K., Venkatachalapathi Y.V., Anantharamaiah G.M. Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes - cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability. J. Biol. Chem. 268:1993;22112-22118.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22112-22118
    • Tytler, E.M.1    Segrest, J.P.2    Epand, R.M.3    Nie, S.-Q.4    Epand, R.F.5    Mishra, V.K.6    Venkatachalapathi, Y.V.7    Anantharamaiah, G.M.8
  • 52
    • 0030041468 scopus 로고    scopus 로고
    • Structural study of the interaction between the SIV fusion peptide and model membranes
    • Colotto A., Martin I., Ruysschaert J., Sen A., Hui S.W., Epand R.M. Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry. 35:1996;980-989.
    • (1996) Biochemistry , vol.35 , pp. 980-989
    • Colotto, A.1    Martin, I.2    Ruysschaert, J.3    Sen, A.4    Hui, S.W.5    Epand, R.M.6
  • 54
    • 0027399966 scopus 로고
    • Cyclic amphipathic peptide-DNA complexes mediate high-efficiency transfection of adherent mammalian cells
    • Legendre J.Y., Szoka F.C. Cyclic amphipathic peptide-DNA complexes mediate high-efficiency transfection of adherent mammalian cells. Proc. Natl. Acad. Sci. USA. 90:1993;893-897.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 893-897
    • Legendre, J.Y.1    Szoka, F.C.2
  • 55
    • 0029562430 scopus 로고
    • Short-chain phospholipids enhance amphipathic peptide-mediated gene transfer
    • Legendre J.Y., Supersaxo A. Short-chain phospholipids enhance amphipathic peptide-mediated gene transfer. Biochem. Biophys. Res. Commun. 217:1995;179-185.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 179-185
    • Legendre, J.Y.1    Supersaxo, A.2
  • 56
    • 0030032075 scopus 로고    scopus 로고
    • Effects of fusogenic and DNA-binding amphiphilic compounds on the receptor-mediated gene transfer into hepatic cells by asialofetuin-labeled liposomes
    • Hara T., Kuwasawa H., Aramaki Y., Takada S., Koike K., Ishidate K., Kato H., Tsuchiya S. Effects of fusogenic and DNA-binding amphiphilic compounds on the receptor-mediated gene transfer into hepatic cells by asialofetuin-labeled liposomes. Biochim. Biophys. Acta. 1278:1996;51-58.
    • (1996) Biochim. Biophys. Acta , vol.1278 , pp. 51-58
    • Hara, T.1    Kuwasawa, H.2    Aramaki, Y.3    Takada, S.4    Koike, K.5    Ishidate, K.6    Kato, H.7    Tsuchiya, S.8
  • 57
    • 0027362739 scopus 로고
    • Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms
    • Siegel D.P. Energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms. Biophys. J. 65:1993;2124-2140.
    • (1993) Biophys. J. , vol.65 , pp. 2124-2140
    • Siegel, D.P.1
  • 58
    • 0032926928 scopus 로고    scopus 로고
    • The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion
    • Siegel D.P. The modified stalk mechanism of lamellar/inverted phase transitions and its implications for membrane fusion. Biophys. J. 76:1999;291-313.
    • (1999) Biophys. J. , vol.76 , pp. 291-313
    • Siegel, D.P.1
  • 60
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner S.M. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. USA. 82:1985;3665-3669.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 61
    • 0022553466 scopus 로고
    • Mode of action of gramicidin S on Escherichia coli membrane
    • Katsu T., Kobayashi H., Fujita Y. Mode of action of gramicidin S on Escherichia coli membrane. Biochim. Biophys. Acta. 860:1986;608-619.
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 608-619
    • Katsu, T.1    Kobayashi, H.2    Fujita, Y.3
  • 64
    • 0028849131 scopus 로고
    • Acholeplasma laidlawii B membranes contain a lipid (glycerylphosphoryldiglucosyldiacylglycerol) which forms micelles rather than lamellar or reversed phases when dispersed in water
    • Lewis R.N.A.H., McElhaney R.N. Acholeplasma laidlawii B membranes contain a lipid (glycerylphosphoryldiglucosyldiacylglycerol) which forms micelles rather than lamellar or reversed phases when dispersed in water. Biochemistry. 34:1995;13818-13824.
    • (1995) Biochemistry , vol.34 , pp. 13818-13824
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 65
    • 0003100631 scopus 로고    scopus 로고
    • Lipids in total extracts from Acholeplasma laidlawii A pack more closely than the individual lipids. Monolayers studied at the air-water interface
    • Andersson A.-S., Demel R.A., Rilfors L., Lindblom G. Lipids in total extracts from Acholeplasma laidlawii A pack more closely than the individual lipids. Monolayers studied at the air-water interface. Biochim. Biophys. Acta. 1369:1998;94-102.
    • (1998) Biochim. Biophys. Acta , vol.1369 , pp. 94-102
    • Andersson, A.-S.1    Demel, R.A.2    Rilfors, L.3    Lindblom, G.4
  • 66
    • 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., 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
  • 67
    • 0033009036 scopus 로고    scopus 로고
    • Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes
    • Prenner E.J., Lewis R.N.A.H., Kondejewski L.H., Hodges R.S., McElhaney R.N. Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes. Biochim. Biophys. Acta. 1417:1999;211-223.
    • (1999) Biochim. Biophys. Acta , vol.1417 , 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
  • 68
    • 0016775558 scopus 로고
    • Conformational states and biological activity of cyclic peptides
    • Ovchinnikov Y.A., Ivanov V.T. Conformational states and biological activity of cyclic peptides. Tetrahedron. 31:1975;2177-2209.
    • (1975) Tetrahedron , vol.31 , pp. 2177-2209
    • Ovchinnikov, Y.A.1    Ivanov, V.T.2
  • 69
    • 0001447789 scopus 로고
    • The cyclic peptides: Structure, conformation, and function
    • in: H. Neurath, R.L. Hill (Eds.), Academic Press, New York
    • Y.A. Ovchinnikov, V.T. Ivanov, The cyclic peptides: structure, conformation, and function, in: H. Neurath, R.L. Hill (Eds.), The Proteins, Vol. V, Academic Press, New York, 1982, pp. 391-398.
    • (1982) The Proteins , vol.5 , pp. 391-398
    • Ovchinnikov, Y.A.1    Ivanov, V.T.2
  • 70
    • 4244107148 scopus 로고    scopus 로고
    • Cholesterol attenuates the interaction of the antimicrobial peptide gramicidin S with phospholipid bilayer membranes
    • submitted for publication
    • E.J. Prenner, R.N.A.H. Lewis, M. Jelokhani-Niaraki, R.S. Hodges, R.N. McElhaney, Cholesterol attenuates the interaction of the antimicrobial peptide gramicidin S with phospholipid bilayer membranes, Biochim. Biophys. Acta, submitted for publication.
    • Biochim. Biophys. Acta
    • Prenner, E.J.1    Lewis, R.N.A.H.2    Jelokhani-Niaraki, M.3    Hodges, R.S.4    McElhaney, R.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.