메뉴 건너뛰기




Volumn 89, Issue 4, 2005, Pages 2434-2442

Interaction of alamethicin with ether-linked phospholipid bilayers: Oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies

Author keywords

[No Author keywords available]

Indexed keywords

1 PALMITOYL 2 OLEOYLGLYCEROL 3 PHOSPHATIDYLCHOLINE; 1,2 O DIHEXADECYLGLYCEROL 3 PHOSPHOCHOLINE; ALAMETHICIN; ESTER; ETHER; PHOSPHOLIPID; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 25844513230     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.067678     Document Type: Article
Times cited : (44)

References (61)
  • 2
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Maganins, cecropins, melittin and alamethicin
    • Bechinger, B. 1997. Structure and functions of channel-forming peptides: maganins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:197-211.
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 3
    • 0034667428 scopus 로고    scopus 로고
    • Solid-state NMR investigations on the structure and topological equilibria of polypeptides associated with biological membranes
    • Bechinger, B. 2000. Solid-state NMR investigations on the structure and topological equilibria of polypeptides associated with biological membranes. Phys. Chem. Chem. Phys. 2:4569-4573.
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4569-4573
    • Bechinger, B.1
  • 4
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • He, K., S. J. Ludtke, and H. W. Huang. 1995. Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry. 34:15614-15618.
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3
  • 5
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • He, K., S. J. Ludtke, D. L. Worcester, and H. W. Huang. 1996. Neutron scattering in the plane of membranes: structure of alamethicin pores. Biophys. J. 70:2659-2666.
    • (1996) Biophys. J. , vol.70 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 6
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F., M. Lee, and H. W. Huang. 2002. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82:908-914.
    • (2002) Biophys. J. , vol.82 , pp. 908-914
    • Chen, F.1    Lee, M.2    Huang, H.W.3
  • 7
    • 0025889072 scopus 로고
    • Lipid-alamethicin interactions influence alamethicin orientation
    • Huang, H. W., and Y. Wu. 1991. Lipid-alamethicin interactions influence alamethicin orientation. Biophys. J. 60:1079-1087.
    • (1991) Biophys. J. , vol.60 , pp. 1079-1087
    • Huang, H.W.1    Wu, Y.2
  • 9
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L., T. A. Harroun, T. M. Weiss, L. Ding, and H. W. Huang. 2001. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys. J. 81:1475-1485.
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 10
    • 0034866022 scopus 로고    scopus 로고
    • Conformation of alamethicin in oriented phospholipid bilayers determined by N-15 solid-state nuclear magnetic resonance
    • Bak, M., R. P. Bywateer, M. Hohwy, J. K. Thomsen, K. Adelhorst, H. J. Jakobsen, O. W. Sorensen, and N. C. Nielsen. 2001. Conformation of alamethicin in oriented phospholipid bilayers determined by N-15 solid-state nuclear magnetic resonance. Biophys. J. 81:1684-1698.
    • (2001) Biophys. J. , vol.81 , pp. 1684-1698
    • Bak, M.1    Bywateer, R.P.2    Hohwy, M.3    Thomsen, J.K.4    Adelhorst, K.5    Jakobsen, H.J.6    Sorensen, O.W.7    Nielsen, N.C.8
  • 11
    • 0028010757 scopus 로고
    • Cooperative membrane insertion of magainin correlated with its cytolytic activity
    • Ludtke, S. J., K. He, Y. Wu, and H. W. Huang. 1994. Cooperative membrane insertion of magainin correlated with its cytolytic activity. Biochim. Biophys. Acta. 1190:182-184.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 182-184
    • Ludtke, S.J.1    He, K.2    Wu, Y.3    Huang, H.W.4
  • 12
    • 0029594533 scopus 로고
    • Membrane thinning caused by maganin 2
    • Ludtke, S. J., K. He, and H. W. Huang. 1994. Membrane thinning caused by maganin 2. Biochemistry. 34:16764-16769.
    • (1994) Biochemistry , vol.34 , pp. 16764-16769
    • Ludtke, S.J.1    He, K.2    Huang, H.W.3
  • 13
    • 0032497922 scopus 로고    scopus 로고
    • Multiple states of beta-sheet peptide protegrin in lipid bilayers
    • Heller, W. T., A. J. Waring, R. I. Lehrer, and H. W. Huang. 1998. Multiple states of beta-sheet peptide protegrin in lipid bilayers. Biochemistry. 37:17331-17338.
    • (1998) Biochemistry , vol.37 , pp. 17331-17338
    • Heller, W.T.1    Waring, A.J.2    Lehrer, R.I.3    Huang, H.W.4
  • 14
    • 0036400912 scopus 로고    scopus 로고
    • Changes in lipid mobility associated with alamethicin incorporation into membranes
    • Kikukawa, T., and T. Araiso. 2002. Changes in lipid mobility associated with alamethicin incorporation into membranes. Arch. Biochem. Biophys. 405:214-222.
    • (2002) Arch. Biochem. Biophys. , vol.405 , pp. 214-222
    • Kikukawa, T.1    Araiso, T.2
  • 15
    • 0031006189 scopus 로고    scopus 로고
    • Effect of changing the size of lipid headgroup on peptide insertion into membranes
    • Heller, W. T., K. He, S. J. Ludtke, T. A. Harroun, and H. W. Huang. 1997. Effect of changing the size of lipid headgroup on peptide insertion into membranes. Biophys. J. 73:239-244.
    • (1997) Biophys. J. , vol.73 , pp. 239-244
    • Heller, W.T.1    He, K.2    Ludtke, S.J.3    Harroun, T.A.4    Huang, H.W.5
  • 16
    • 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., K. He, S. J. Ludtke, and H. W. Huang. 1995. X-ray diffraction study of lipid bilayer membranes interacting with amphiphilic helical peptides: diphytanoyl phosphatidylcholine with alamethicin at low concentrations. Biophys. J. 68:2361-2369.
    • (1995) Biophys. J. , vol.68 , pp. 2361-2369
    • Wu, Y.1    He, K.2    Ludtke, S.J.3    Huang, H.W.4
  • 17
    • 0021829331 scopus 로고
    • Comparative study of the gel phases of ether- and ester-linked phosphatidylcholines
    • Ruocco, M. J., D. J. Siminovitch, and R. G. Griffin. 1985. Comparative study of the gel phases of ether- and ester-linked phosphatidylcholines. Biochemistry. 24:2406-2411.
    • (1985) Biochemistry , vol.24 , pp. 2406-2411
    • Ruocco, M.J.1    Siminovitch, D.J.2    Griffin, R.G.3
  • 18
    • 0023357999 scopus 로고
    • Structure and thermodynamics of the dihexadecylphosphatidyl-choline-water system
    • Laggner, P., K. Lohner, G. Degovics, K. Muller, and A. Schuster. 1987. Structure and thermodynamics of the dihexadecylphosphatidyl-choline-water system. Chem. Phys. Lipids. 44:31-60.
    • (1987) Chem. Phys. Lipids , vol.44 , pp. 31-60
    • Laggner, P.1    Lohner, K.2    Degovics, G.3    Muller, K.4    Schuster, A.5
  • 19
    • 0023661103 scopus 로고
    • Gel phase polymorphism in ether-linked dihexadecylphosphatidylcholine bilayers
    • Kim, J. T., J. Mattay, and G. G. Shipley. 1987. Gel phase polymorphism in ether-linked dihexadecylphosphatidylcholine bilayers. Biochemistry. 26:6592-6598.
    • (1987) Biochemistry , vol.26 , pp. 6592-6598
    • Kim, J.T.1    Mattay, J.2    Shipley, G.G.3
  • 20
    • 0028597086 scopus 로고
    • Antitumor ether lipids and alkylphosphocholines
    • Lohmeyer, M., and R. Bittman. 1994. Antitumor ether lipids and alkylphosphocholines. Drugs Future. 19:1021-1037.
    • (1994) Drugs Future , vol.19 , pp. 1021-1037
    • Lohmeyer, M.1    Bittman, R.2
  • 21
    • 77957089159 scopus 로고
    • The evolution of membrane structure and dynamics of membrane
    • R. Lipiwsky and E. Sackman, editors. Elsevier/North Holland, Amsterdam
    • Bloom, M., and O. G. Mouritsen. 1995. The evolution of membrane structure and dynamics of membrane. In Handbook of Biological Physics, Vol. IA. R. Lipiwsky and E. Sackman, editors. Elsevier/North Holland, Amsterdam. 65-95.
    • (1995) Handbook of Biological Physics , vol.1 A , pp. 65-95
    • Bloom, M.1    Mouritsen, O.G.2
  • 22
    • 0036931991 scopus 로고    scopus 로고
    • Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides
    • Yang, J., P. D. Parkanzky, M. L. Bodner, C. A. Duskin, and D. P. Weliky. 2002. Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides. J. Magn. Reson. 159:101-110.
    • (2002) J. Magn. Reson. , vol.159 , pp. 101-110
    • Yang, J.1    Parkanzky, P.D.2    Bodner, M.L.3    Duskin, C.A.4    Weliky, D.P.5
  • 24
    • 0032919273 scopus 로고    scopus 로고
    • Improved low pH bicelle system for orienting macromolecules over a wide temperature range
    • Cavagnero, S., H. J. Dyson, and P. E. Wright. 1999. Improved low pH bicelle system for orienting macromolecules over a wide temperature range. J. Biomol. NMR. 13:387-391.
    • (1999) J. Biomol. NMR , vol.13 , pp. 387-391
    • Cavagnero, S.1    Dyson, H.J.2    Wright, P.E.3
  • 25
    • 0033026167 scopus 로고    scopus 로고
    • Bicelle-based liquid crystals for NMR measurement of dipolar couplings at acidic and basic pH values
    • Ottiger, M., and A. Bax. 1999. Bicelle-based liquid crystals for NMR measurement of dipolar couplings at acidic and basic pH values. J. Biomol. NMR. 13:187-191.
    • (1999) J. Biomol. NMR , vol.13 , pp. 187-191
    • Ottiger, M.1    Bax, A.2
  • 27
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F., M. Lee, and H. W. Huang. 2002. Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin. Biophys. J. 82:908-914.
    • (2002) Biophys. J. , vol.82 , pp. 908-914
    • Chen, F.1    Lee, M.2    Huang, H.W.3
  • 29
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption
    • Hallock, K. J., D. K. Lee, J. Omnaas, H. I. Mosberg, and A. Ramamoorthy. 2002. Membrane composition determines pardaxin's mechanism of lipid bilayer disruption. Biophys. J. 83:1004-1013.
    • (2002) Biophys. J. , vol.83 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, A.5
  • 30
    • 7244257317 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1
    • Mani, R., J. J. Buffy, A. J. Waring, R. I. Lehrer, and M. Hong. 2004. Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1. Biochemistry. 43:13839-13848.
    • (2004) Biochemistry , vol.43 , pp. 13839-13848
    • Mani, R.1    Buffy, J.J.2    Waring, A.J.3    Lehrer, R.I.4    Hong, M.5
  • 32
    • 0017099492 scopus 로고
    • 31P NMR studies of unsonicated aqueous dispersions of neutral and acidic phospholipids. Effects of phase transitions, p2H and divalent cations on the motion in the phosphate region of the polar headgroup
    • 31P NMR studies of unsonicated aqueous dispersions of neutral and acidic phospholipids. Effects of phase transitions, p2H and divalent cations on the motion in the phosphate region of the polar headgroup. Biochim. Biophys. Acta. 436:523-540.
    • (1976) Biochim. Biophys. Acta , vol.436 , pp. 523-540
    • Cullis, P.R.1    De Kruyff, B.2
  • 33
    • 0032740652 scopus 로고    scopus 로고
    • Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids
    • Huang, C., and S. Li. 1999. Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids. Biochim. Biophys. Acta. 1422:273-307.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 273-307
    • Huang, C.1    Li, S.2
  • 34
    • 0021746887 scopus 로고
    • Effect of phase transitions on the interaction of peptides and proteins with phospholipids
    • Epand, R. M., and W. K. Surewicz. 1984. Effect of phase transitions on the interaction of peptides and proteins with phospholipids. Can. J. Biochem. Cell Biol. 62:1167-1173.
    • (1984) Can. J. Biochem. Cell Biol. , vol.62 , pp. 1167-1173
    • Epand, R.M.1    Surewicz, W.K.2
  • 35
    • 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., R. N. Lewis, K. C. Neuman, S. M. Gruner, L. H. Kondejewski, R. S. Hodges, and R. N. McElhaney. 1997. Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity. Biochemistry. 36:7906-7916.
    • (1997) Biochemistry , vol.36 , pp. 7906-7916
    • Prenner, E.J.1    Lewis, R.N.2    Neuman, K.C.3    Gruner, S.M.4    Kondejewski, L.H.5    Hodges, R.S.6    McElhaney, R.N.7
  • 36
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • Henzer-Wildman, K. A., G. V. Martinez, M. F. Brown, and A. Ramamoorthy. 2004. Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37. Biochemistry. 43:8459-8469.
    • (2004) Biochemistry , vol.43 , pp. 8459-8469
    • Henzer-Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4
  • 37
    • 0026623539 scopus 로고
    • Calorimetry of tetraether lipids from Thermoplasma acidophilum: Incorporation of alamethicin, melittin, valinomycin, and nonactin
    • Freisleben, H. J., D. Blocher, and K. Ring. 1992. Calorimetry of tetraether lipids from Thermoplasma acidophilum: incorporation of alamethicin, melittin, valinomycin, and nonactin. Arch. Biochem. Biophys. 294:418-426.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 418-426
    • Freisleben, H.J.1    Blocher, D.2    Ring, K.3
  • 38
    • 0028598299 scopus 로고
    • Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application
    • de Jongh, H. H., E. Goormaghtigh, and J. A. Killian. 1994. Analysis of circular dichroism spectra of oriented protein-lipid complexes: toward a general application. Biochemistry. 33:14521-14528.
    • (1994) Biochemistry , vol.33 , pp. 14521-14528
    • Jongh, H.H.1    Goormaghtigh, E.2    Killian, J.A.3
  • 39
    • 0021103672 scopus 로고
    • Lipid solvation of cytochrome c oxidase. Deuterium, nitrogen-14, and phosphorus-31 nuclear magnetic resonance studies on the phosphocholine head group and on cis-unsaturated fatty acyl chains
    • Tamm, L. K., and J. Seelig. 1983. Lipid solvation of cytochrome c oxidase. Deuterium, nitrogen-14, and phosphorus-31 nuclear magnetic resonance studies on the phosphocholine head group and on cis-unsaturated fatty acyl chains. Biochemistry. 22:1474-1483.
    • (1983) Biochemistry , vol.22 , pp. 1474-1483
    • Tamm, L.K.1    Seelig, J.2
  • 40
    • 0028260185 scopus 로고
    • Lipid specificity in the interaction of cytochrome-c with anionic phospholipids-bilayers revealed by solid-state P-31 NMR
    • Pinheiro, T. J. T., and A. Watts. 1994. Lipid specificity in the interaction of cytochrome-c with anionic phospholipids-bilayers revealed by solid-state P-31 NMR. Biochemistry. 33:2451-2458.
    • (1994) Biochemistry , vol.33 , pp. 2451-2458
    • Pinheiro, T.J.T.1    Watts, A.2
  • 41
    • 0028231733 scopus 로고
    • Resolution of individual lipids in mixed phospholipids membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR
    • Pinheiro, T. J. T., and A. Watts. 1994. Resolution of individual lipids in mixed phospholipids membranes and specific lipid-cytochrome c interactions by magic-angle spinning solid-state phosphorus-31 NMR. Biochemistry 33:2459-2467.
    • (1994) Biochemistry , vol.33 , pp. 2459-2467
    • Pinheiro, T.J.T.1    Watts, A.2
  • 42
    • 0025278431 scopus 로고
    • Method of oriented circular dichroism
    • Wu, Y., H. W. Huang, and G. A. Olah. 1990. Method of oriented circular dichroism. Biophys. J. 57:797-806.
    • (1990) Biophys. J. , vol.57 , pp. 797-806
    • Wu, Y.1    Huang, H.W.2    Olah, G.A.3
  • 43
    • 0029147077 scopus 로고
    • Molecular interactions of ether-linked phospholipids
    • Hing, F. S., and G. G. Shipley. 1995. Molecular interactions of ether-linked phospholipids. Biochemistry. 34:11904-11909.
    • (1995) Biochemistry , vol.34 , pp. 11904-11909
    • Hing, F.S.1    Shipley, G.G.2
  • 45
    • 0034738622 scopus 로고    scopus 로고
    • Order-disorder transition in bilayers of diphytanoyl-phosphatidylcholine
    • Hung, W. C., F. Y. Chen, and H. W. Huang. 2000. Order-disorder transition in bilayers of diphytanoyl-phosphatidylcholine. Biochim. Biophys. Acta. 1467:198-206.
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 198-206
    • Hung, W.C.1    Chen, F.Y.2    Huang, H.W.3
  • 47
    • 0017902280 scopus 로고
    • P-31 nuclear magnetic-resonance and head group structure of phospholipids in membrane
    • Seelig, J. 1978. P-31 nuclear magnetic-resonance and head group structure of phospholipids in membrane. Biochim. Biophys. Acta. 515:105-140.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 48
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner, E. J., R. N. Lewis, and R. N. McElhaney. 1999. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim. Biophys. Acta. 1462:201-221.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.2    McElhaney, R.N.3
  • 49
    • 7644228920 scopus 로고    scopus 로고
    • Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy
    • Pointer-Keenan, C. D., D. K. Lee, K. Hallock, A. M. Tan, R. Zand, and A. Ramamoorthy. 2004. Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy. Chem. Phys. Lipids. 132:47-54.
    • (2004) Chem. Phys. Lipids. , vol.132 , pp. 47-54
    • Pointer-Keenan, C.D.1    Lee, D.K.2    Hallock, K.3    Tan, A.M.4    Zand, R.5    Ramamoorthy, A.6
  • 50
    • 3342900055 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptide RTD-1
    • Buffy, J. J., M. J. McCormick, S. Wi, A. Waring, R. I. Mehrer, and M. Hong. 2004. Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptide RTD-1. Biochemistry. 43:9800-9812.
    • (2004) Biochemistry , vol.43 , pp. 9800-9812
    • Buffy, J.J.1    McCormick, M.J.2    Wi, S.3    Waring, A.4    Mehrer, R.I.5    Hong, M.6
  • 51
    • 0033783447 scopus 로고    scopus 로고
    • 31P solid-state NMR spectroscopy investigation
    • 31P solid-state NMR spectroscopy investigation. Biochemistry. 39:13106-13114.
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 52
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzer-Wildman, K. A., D. K. Lee, and A. Ramamoorthy. 2003. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry. 42:6545-6558.
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzer-Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 53
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock, K. J., D. K. Lee, and A. Ramamoorthy. 2003. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J. 84:3052-3060.
    • (2003) Biophys. J. , vol.84 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 55
    • 0028860483 scopus 로고
    • Two classes of alamethicin transmembrane channels: Molecular models from single-channel properties
    • Mak, D. O., and W. W. Webb. 1995. Two classes of alamethicin transmembrane channels: molecular models from single-channel properties. Biophys. J. 69:2323-2336.
    • (1995) Biophys. J. , vol.69 , pp. 2323-2336
    • Mak, D.O.1    Webb, W.W.2
  • 56
    • 0028841644 scopus 로고
    • Membrane orientation of the N-terminal segment of alamethicin determined by solid-state N-15 NMR
    • North, C. L., M. Barranger-Mathys, and D. S. Cafiso. 1995. Membrane orientation of the N-terminal segment of alamethicin determined by solid-state N-15 NMR. Biophys. J. 69:2392-2397.
    • (1995) Biophys. J. , vol.69 , pp. 2392-2397
    • North, C.L.1    Barranger-Mathys, M.2    Cafiso, D.S.3
  • 57
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols-model ion channels
    • Sansom, M. S. 1993. Alamethicin and related peptaibols-model ion channels. Eur. Biophys. J. 22:105-124.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 105-124
    • Sansom, M.S.1
  • 58
    • 0032951553 scopus 로고    scopus 로고
    • Alamethicin helices in a bilayer and in solution: Molecular dynamics simulations
    • Tieleman, D. P., M. S. P. Sansom, and H. J. C. Berendsen. 1999. Alamethicin helices in a bilayer and in solution: molecular dynamics simulations. Biophys. J. 76:40-49.
    • (1999) Biophys. J. , vol.76 , pp. 40-49
    • Tieleman, D.P.1    Sansom, M.S.P.2    Berendsen, H.J.C.3
  • 59
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: Molecular dynamics simulations
    • Tieleman, D. P., H. J. C. Berendsen, and M. S. P. Sansom. 1999. An alamethicin channel in a lipid bilayer: molecular dynamics simulations. Biophys. J. 76:1757-1769.
    • (1999) Biophys. J. , vol.76 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 60
    • 19444376974 scopus 로고    scopus 로고
    • Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843
    • Thennarasu, S., D. K. Lee, A. Tan, U. Prasad Kari, and A. Ramamoorthy. 2005. Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843. Biochim. Biophys. Acta. 1711:49-58.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 49-58
    • Thennarasu, S.1    Lee, D.K.2    Tan, A.3    Prasad Kari, U.4    Ramamoorthy, A.5
  • 61
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. 1998. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.