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Volumn 95, Issue 10, 2008, Pages 4748-4755

The activity of the amphipathic peptide δ-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DELTA HEMOLYSIN PROTEIN, STAPHYLOCOCCUS AUREUS; HEMOLYSIN; PHOSPHOLIPID; SURFACTANT; UNCLASSIFIED DRUG;

EID: 58149286266     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.138701     Document Type: Article
Times cited : (27)

References (64)
  • 1
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel, W. 2003. The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur. J. Biochem. 270:2109-2119.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 2
    • 33845810639 scopus 로고    scopus 로고
    • 2nd Ed, U. Langel, editor. CRC, Boca Raton, FL
    • Handbook of Cell-Penetrating Peptides, 2nd Ed. 2006. U. Langel, editor. CRC, Boca Raton, FL.
    • (2006) Handbook of Cell-Penetrating Peptides
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature. 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G., and H. Lecar. 1977. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10:1-34.
    • (1977) Q. Rev. Biophys , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 6
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1996. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry. 35:11361-11368.
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 7
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, a-helical peptides
    • Pokorny, A., and P. F. F. Almeida. 2004. Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, a-helical peptides. Biochemistry. 43:8846-8857.
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 9
    • 40149107726 scopus 로고    scopus 로고
    • A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide Cecropin A
    • Gregory, S. M., A. C. Cavenaugh, V. Journigan, A. Pokorny, and P. F. F. Almeida. 2008. A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide Cecropin A. Biophys. J. 94:1667-1680.
    • (2008) Biophys. J , vol.94 , pp. 1667-1680
    • Gregory, S.M.1    Cavenaugh, A.C.2    Journigan, V.3    Pokorny, A.4    Almeida, P.F.F.5
  • 10
    • 40149084042 scopus 로고    scopus 로고
    • Small changes in the primary structure of Transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles
    • Yandek, L. E., A. Pokorny, and P. F. F. Almeida. 2008. Small changes in the primary structure of Transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles. Biochemistry. 47:3051-3060.
    • (2008) Biochemistry , vol.47 , pp. 3051-3060
    • Yandek, L.E.1    Pokorny, A.2    Almeida, P.F.F.3
  • 11
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. 2002. Mode of action of membrane active antimicrobial peptides. Biopolymers. 66:236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 13
    • 0023082885 scopus 로고
    • Nuclear magnetic resonance investigation of the conformation of d-hemolysin bound to dodecylphosphocholine micelles
    • Lee, K. H., J. E. Fitton, and K. Wüthrich. 1987. Nuclear magnetic resonance investigation of the conformation of d-hemolysin bound to dodecylphosphocholine micelles. Biochim. Biophys. Acta. 911:144-153.
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 144-153
    • Lee, K.H.1    Fitton, J.E.2    Wüthrich, K.3
  • 14
    • 0025963949 scopus 로고
    • The amphiphilic α-helix concept. Consequences on the structure of staphylococcal δ-toxin in solution and bound to lipids
    • Thiaudière, E., O. Siffert, J. C. Talbot, J. Bolard, J. E. Alouf, and J. Dufourcq. 1991. The amphiphilic α-helix concept. Consequences on the structure of staphylococcal δ-toxin in solution and bound to lipids. Eur. J. Biochem. 195:203-213.
    • (1991) Eur. J. Biochem , vol.195 , pp. 203-213
    • Thiaudière, E.1    Siffert, O.2    Talbot, J.C.3    Bolard, J.4    Alouf, J.E.5    Dufourcq, J.6
  • 16
    • 21844443548 scopus 로고    scopus 로고
    • Permeabilization of raft-containing lipid vesicles by δ-lysin: A mechanism for cell sensitivity to cytotoxic peptides
    • Pokorny, A., and P. F. F. Almeida. 2005. Permeabilization of raft-containing lipid vesicles by δ-lysin: a mechanism for cell sensitivity to cytotoxic peptides. Biochemistry. 44:9538-9544.
    • (2005) Biochemistry , vol.44 , pp. 9538-9544
    • Pokorny, A.1    Almeida, P.F.F.2
  • 17
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of d-lysin interaction with phospholipid vesicles
    • Pokorny, A., T. H. Birkbeck, and P. F. F. Almeida. 2002. Mechanism and kinetics of d-lysin interaction with phospholipid vesicles. Biochemistry. 41:11044-11056.
    • (2002) Biochemistry , vol.41 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 18
    • 0023018907 scopus 로고
    • Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime
    • Huang, H. W. 1986. Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime. Biophys. J. 50:1061-1070.
    • (1986) Biophys. J , vol.50 , pp. 1061-1070
    • Huang, H.W.1
  • 19
    • 0028965734 scopus 로고
    • Acyl chain length dependence in the stability of melittin-phosphatidylcholine complexes. A light scattering and 31P-NMR study
    • Faucon, J. F., J. M. Bonmatin, J. Dufourcq, and E. J. Dufourc. 1995. Acyl chain length dependence in the stability of melittin-phosphatidylcholine complexes. A light scattering and 31P-NMR study. Biochim. Biophys. Acta. 1234:235-243.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 235-243
    • Faucon, J.F.1    Bonmatin, J.M.2    Dufourcq, J.3    Dufourc, E.J.4
  • 20
    • 0029947537 scopus 로고    scopus 로고
    • Influence of lipid chain unsaturation on melittin-induced micellization
    • Monette, M., and M. Lafleur. 1996. Influence of lipid chain unsaturation on melittin-induced micellization. Biophys. J. 70:2195-2202.
    • (1996) Biophys. J , vol.70 , pp. 2195-2202
    • Monette, M.1    Lafleur, M.2
  • 21
    • 0034117591 scopus 로고    scopus 로고
    • Effect of phospholipid composition on an amphipathic peptide-mediated pore formation in bilayers vesicles
    • Nicol, F., S. Nir, and F. C. Szoka. 2000. Effect of phospholipid composition on an amphipathic peptide-mediated pore formation in bilayers vesicles. Biophys. J. 78:818-829.
    • (2000) Biophys. J , vol.78 , pp. 818-829
    • Nicol, F.1    Nir, S.2    Szoka, F.C.3
  • 22
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F. Y., M. T. 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.Y.1    Lee, M.T.2    Huang, H.W.3
  • 23
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen, F. Y., M. T. Lee, and H. W. Huang. 2003. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 84:3751-3758.
    • (2003) Biophys. J , vol.84 , pp. 3751-3758
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 24
    • 4644333025 scopus 로고    scopus 로고
    • Influence of lipid chain unsaturation on membrane-bound melittin: A fluorescence approach
    • Raghuraman, H., and A. Chattopadhyay. 2004. Influence of lipid chain unsaturation on membrane-bound melittin: a fluorescence approach. Biochim. Biophys. Acta. 1665:29-39.
    • (2004) Biochim. Biophys. Acta , vol.1665 , pp. 29-39
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 25
    • 15244349709 scopus 로고    scopus 로고
    • Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores
    • Allende, D., S. A. Simon, and T. J. McIntosh. 2005. Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores. Biophys. J. 88:1828-1837.
    • (2005) Biophys. J , vol.88 , pp. 1828-1837
    • Allende, D.1    Simon, S.A.2    McIntosh, T.J.3
  • 26
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • McIntosh, T. J., and S. A. Simon. 2006. Roles of bilayer material properties in function and distribution of membrane proteins. Annu. Rev. Biophys. Biomol. Struct. 35:177-198.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 27
    • 0030586121 scopus 로고    scopus 로고
    • Hydration properties of lamellar and non-lamellar phases of phosphatidylcholine and phosphatidylethanolamine
    • McIntosh, T. J. 1996. Hydration properties of lamellar and non-lamellar phases of phosphatidylcholine and phosphatidylethanolamine. Chem. Phys. Lipids. 81:117-131.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 117-131
    • McIntosh, T.J.1
  • 28
    • 33845281853 scopus 로고
    • Physical properties of surfactant bilayer membranes: Thermal transitions, elasticity, rigidity, cohesion and colloidal interactions
    • Evans, E., and D. Needham. 1987. Physical properties of surfactant bilayer membranes: thermal transitions, elasticity, rigidity, cohesion and colloidal interactions. J. Phys. Chem. 91:4219-4228.
    • (1987) J. Phys. Chem , vol.91 , pp. 4219-4228
    • Evans, E.1    Needham, D.2
  • 29
    • 11944258697 scopus 로고
    • Entropy-driven tension and bending elasticity in condensed-fluid membranes
    • Evans, E., and W. Rawicz. 1990. Entropy-driven tension and bending elasticity in condensed-fluid membranes. Phys. Rev. Lett. 64:2094-2097.
    • (1990) Phys. Rev. Lett , vol.64 , pp. 2094-2097
    • Evans, E.1    Rawicz, W.2
  • 30
    • 45849089169 scopus 로고    scopus 로고
    • Elasticity, strength, and water permeability of bilayers that contain raft microdomain-forming lipids
    • Rawicz, W., B. A. Smith, T. J. McIntosh, S. A. Simon, and E. Evans. 2008. Elasticity, strength, and water permeability of bilayers that contain raft microdomain-forming lipids. Biophys. J. 94:4725-4736.
    • (2008) Biophys. J , vol.94 , pp. 4725-4736
    • Rawicz, W.1    Smith, B.A.2    McIntosh, T.J.3    Simon, S.A.4    Evans, E.5
  • 31
    • 0024214704 scopus 로고
    • Purification and assay of staphylococcal d-lysin
    • Birkbeck, T. H., and J. H. Freer. 1988. Purification and assay of staphylococcal d-lysin. Methods Enzymol. 165:16-22.
    • (1988) Methods Enzymol , vol.165 , pp. 16-22
    • Birkbeck, T.H.1    Freer, J.H.2
  • 32
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorous assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 34
    • 0004974366 scopus 로고
    • The interpretation of single channel recordings
    • 2nd Ed. D. Ogden, editor. The Company of Biologists Ltd, Cambridge, UK
    • Colquhoun, D., and A. G. Hawkes. 1987. The interpretation of single channel recordings. In Microelectrode Techniques. The Plymouth Workshop Handbook, 2nd Ed. D. Ogden, editor. The Company of Biologists Ltd., Cambridge, UK.
    • (1987) Microelectrode Techniques. The Plymouth Workshop Handbook
    • Colquhoun, D.1    Hawkes, A.G.2
  • 35
    • 0018526601 scopus 로고
    • Mechanics and thermodynamics of biomembranes: Part 1
    • Evans, E., and R. Skalak. 1979. Mechanics and thermodynamics of biomembranes: part 1. CRC Crit. Rev. Bioeng. 3:181-330.
    • (1979) CRC Crit. Rev. Bioeng , vol.3 , pp. 181-330
    • Evans, E.1    Skalak, R.2
  • 36
    • 33750931433 scopus 로고    scopus 로고
    • Elastic curvature constants of lipid monolayers and bilayers
    • Marsh, D. 2006. Elastic curvature constants of lipid monolayers and bilayers. Chem. Phys. Lipids. 144:146-159.
    • (2006) Chem. Phys. Lipids , vol.144 , pp. 146-159
    • Marsh, D.1
  • 37
    • 0033918516 scopus 로고    scopus 로고
    • Water permeability and mechanical strength of polyunsaturated lipid bilayers
    • Olbrich, K., W. Rawicz, D. Needham, and E. Evans. 2000. Water permeability and mechanical strength of polyunsaturated lipid bilayers. Biophys. J. 79:321-327.
    • (2000) Biophys. J , vol.79 , pp. 321-327
    • Olbrich, K.1    Rawicz, W.2    Needham, D.3    Evans, E.4
  • 38
    • 0016377872 scopus 로고
    • Bending resistance and chemically induced moments in membrane bilayers
    • Evans, E. 1974. Bending resistance and chemically induced moments in membrane bilayers. Biophys. J. 14:923-931.
    • (1974) Biophys. J , vol.14 , pp. 923-931
    • Evans, E.1
  • 39
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz, W., K. C. Olbrich, T. McIntosh, D. Needham, and E. Evans. 2000. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys. J. 79:328-339.
    • (2000) Biophys. J , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 40
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers: Theory and possible experiments
    • Helfrich, W. 1973. Elastic properties of lipid bilayers: theory and possible experiments. Z. Naturforsch. 28c:693-703.
    • (1973) Z. Naturforsch , vol.28 c , pp. 693-703
    • Helfrich, W.1
  • 41
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner, S. M. 1985. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. USA. 82:3665-3669.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 42
    • 0001983871 scopus 로고
    • Polymorphism of lipid-water systems
    • R. Lipowski and E. Sackmann, editors. Elsevier Science, Amsterdam, The Netherlands
    • Seddon, J. M., and R. H. Templer. 1995. Polymorphism of lipid-water systems. In Structure and Dynamics of Membranes, Vol. 1. R. Lipowski and E. Sackmann, editors. Elsevier Science, Amsterdam, The Netherlands.
    • (1995) Structure and Dynamics of Membranes , vol.1
    • Seddon, J.M.1    Templer, R.H.2
  • 43
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes. 1996
    • Marsh, D. 1996. Lateral pressure in membranes. 1996. Biochim. Biophys. Acta. 1286:183-223.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 44
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • Cantor, R. S. 1999. Lipid composition and the lateral pressure profile in bilayers. Biophys. J. 76:2625-2639.
    • (1999) Biophys. J , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 45
    • 0032857624 scopus 로고    scopus 로고
    • The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria
    • Cantor, R. S. 1999. The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria. Chem. Phys. Lipids. 101:45-56.
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 45-56
    • Cantor, R.S.1
  • 46
    • 0020788538 scopus 로고
    • Synthesis and polymorphic phase behavior of polyunsaturated phosphatidylcholines and phosphatidylethanolamines
    • Dekker, C. J., W. S. Geurts van Kessel, J. P. Klomp, J. Pieters, and B. De Kruijff. 1983. Synthesis and polymorphic phase behavior of polyunsaturated phosphatidylcholines and phosphatidylethanolamines. Chem. Phys. Lipids. 33:93-106.
    • (1983) Chem. Phys. Lipids , vol.33 , pp. 93-106
    • Dekker, C.J.1    Geurts van Kessel, W.S.2    Klomp, J.P.3    Pieters, J.4    De Kruijff, B.5
  • 47
    • 0025105212 scopus 로고
    • Membrane curvature, lipid segregation, and structural transitions for phospholipids under dual-solvent stress
    • Rand, R. P., N. L. Fuller, S. M. Gruner, and V. A. Parsegian. 1990. Membrane curvature, lipid segregation, and structural transitions for phospholipids under dual-solvent stress. Biochemistry. 29:76-87.
    • (1990) Biochemistry , vol.29 , pp. 76-87
    • Rand, R.P.1    Fuller, N.L.2    Gruner, S.M.3    Parsegian, V.A.4
  • 48
    • 0035997044 scopus 로고    scopus 로고
    • The effects of acyl chain length and saturation of diacylglycerols and phosphatidylcholines on membrane monolayer curvature
    • Szule, J. A., N. L. Fuller, and R. P. Rand. 2002. The effects of acyl chain length and saturation of diacylglycerols and phosphatidylcholines on membrane monolayer curvature. Biophys. J. 83:977-984.
    • (2002) Biophys. J , vol.83 , pp. 977-984
    • Szule, J.A.1    Fuller, N.L.2    Rand, R.P.3
  • 49
    • 0030049701 scopus 로고    scopus 로고
    • Pore formation induced by the peptide melittin in different lipid vesicle membranes
    • Rex, S. 1996. Pore formation induced by the peptide melittin in different lipid vesicle membranes. Biophys. Chem. 58:75-85.
    • (1996) Biophys. Chem , vol.58 , pp. 75-85
    • Rex, S.1
  • 50
    • 22544433150 scopus 로고    scopus 로고
    • Effect of chain length and asymmetry on material properties of bilayer membranes
    • Illya, G., R. Lipowsky, and J. C. Shillcock. 2005. Effect of chain length and asymmetry on material properties of bilayer membranes. J. Chem. Phys. 122:244901.
    • (2005) J. Chem. Phys , vol.122 , pp. 244901
    • Illya, G.1    Lipowsky, R.2    Shillcock, J.C.3
  • 51
    • 34948881202 scopus 로고    scopus 로고
    • Lipid tail chain asymmetry and the strength of membrane-induced interactions between membrane proteins
    • Dan, N. 2007. Lipid tail chain asymmetry and the strength of membrane-induced interactions between membrane proteins. Biochim. Biophys. Acta. 1768:2393-2399.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2393-2399
    • Dan, N.1
  • 52
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kučerka, N., S. Tristram-Nagle, and J. F. Nagle. 2005. Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 208:193-202.
    • (2005) J. Membr. Biol , vol.208 , pp. 193-202
    • Kučerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 53
    • 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
  • 56
    • 0035936573 scopus 로고    scopus 로고
    • 31P NMR spectroscopic study of the effect of transmembrane α-helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes
    • 31P NMR spectroscopic study of the effect of transmembrane α-helical peptides on the lamellar-reversed hexagonal phase transition of phosphatidylethanolamine model membranes. Biochemistry. 40:760-768.
    • (2001) Biochemistry , vol.40 , pp. 760-768
    • Liu, F.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 57
    • 0345074088 scopus 로고    scopus 로고
    • Interactions of the antimicrobial β-peptide β-17 with phospholipid vesicles differ from membrane interactions of magainins
    • Epand, R. F., N. Umezawa, E. A. Porter, S. H. Gellman, and R. M. Epand. 2003. Interactions of the antimicrobial β-peptide β-17 with phospholipid vesicles differ from membrane interactions of magainins. Eur. J. Biochem. 270:1240-1248.
    • (2003) Eur. J. Biochem , vol.270 , pp. 1240-1248
    • Epand, R.F.1    Umezawa, N.2    Porter, E.A.3    Gellman, S.H.4    Epand, R.M.5
  • 58
    • 28444488982 scopus 로고    scopus 로고
    • Many-body effect of antimicrobial peptides: On the correlation between lipid's spontaneous curvature and pore formation
    • Lee, M. T., W. C. Hung, F. Y. Chen, and H. W. Huang. 2005. Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formation. Biophys. J. 89:4006-4016.
    • (2005) Biophys. J , vol.89 , pp. 4006-4016
    • Lee, M.T.1    Hung, W.C.2    Chen, F.Y.3    Huang, H.W.4
  • 59
    • 33745747109 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin
    • Ramamoorthy, A., S. Thennarasu, D. K. Lee, A. Tan, and L. Maloy. 2006. Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophys. J. 91:206-216.
    • (2006) Biophys. J , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.K.3    Tan, A.4    Maloy, L.5
  • 61
    • 0026704101 scopus 로고
    • Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thickness in model membranes
    • Nezil, F. A., and M. Bloom. 1992. Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thickness in model membranes. Biophys. J. 61:1176-1183.
    • (1992) Biophys. J , vol.61 , pp. 1176-1183
    • Nezil, F.A.1    Bloom, M.2
  • 62
    • 0030949722 scopus 로고    scopus 로고
    • The influence of cholesterol on phospholipid membrane curvature and bending elasticity
    • Chen, Z., and R. P. Rand. 1997. The influence of cholesterol on phospholipid membrane curvature and bending elasticity. Biophys. J. 73:267-276.
    • (1997) Biophys. J , vol.73 , pp. 267-276
    • Chen, Z.1    Rand, R.P.2
  • 63
    • 33748465151 scopus 로고    scopus 로고
    • Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC
    • Pokorny, A., L. E. Yandek, A. I. Elegbede, A. Hinderliter, and P. F. Almeida. 2006. Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC. Biophys. J. 91:2184-2197.
    • (2006) Biophys. J , vol.91 , pp. 2184-2197
    • Pokorny, A.1    Yandek, L.E.2    Elegbede, A.I.3    Hinderliter, A.4    Almeida, P.F.5
  • 64
    • 2642533608 scopus 로고    scopus 로고
    • Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction
    • Hinderliter, A., R. L. Biltonen, and P. F. Almeida. 2004. Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction. Biochemistry. 43:7102-7110.
    • (2004) Biochemistry , vol.43 , pp. 7102-7110
    • Hinderliter, A.1    Biltonen, R.L.2    Almeida, P.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.