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Volumn 23, Issue 11, 2009, Pages 3692-3701

Selectivity of cateslytin for fungi: The role of acidic lipid-ergosterol membrane fluidity in antimicrobial action

Author keywords

Cholesterol; Domains; Infrared; NMR

Indexed keywords

AMPHOLYTE; CATESLYTIN; CHOLESTEROL; DIMYRISTOYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; ERGOSTEROL; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 70350530629     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-135574     Document Type: Article
Times cited : (20)

References (56)
  • 1
    • 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
  • 2
    • 0031740520 scopus 로고    scopus 로고
    • Magainins as paradigm for the mode of action of pore forming polypeptides
    • Matsuzaki, K. (1998) Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta Biomembranes 1376, 391-400
    • (1998) Biochim. Biophys. Acta Biomembranes , vol.1376 , pp. 391-400
    • Matsuzaki, K.1
  • 3
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, maganin-2, across lipid bilayers by forming a pore
    • Matsuzaki, K., Murase, O., Fujii, N., and Miyajima, K. (1995) Translocation of a channel-forming antimicrobial peptide, maganin-2, across lipid bilayers by forming a pore. Biochemistry 34, 6521-6526
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 4
    • 0028919743 scopus 로고
    • Action of melittin on the DPPC-cholesterol liquid-ordered phase: A solid-state H-2-NMR and P-31 NMR study
    • Pott, T., and Dufourc, E. J. (1995) Action of melittin on the DPPC-cholesterol liquid-ordered phase: a solid-state H-2-NMR and P-31 NMR study. Biophys. J. 68, 965-977
    • (1995) Biophys. J. , vol.68 , pp. 965-977
    • Pott, T.1    Dufourc, E.J.2
  • 5
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462, 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 6
    • 45749113323 scopus 로고    scopus 로고
    • Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. a new mode of action for antimicrobial peptides?
    • DOI 10.1021/bi800448h
    • Jean-François, F., Castano, S., Desbat, B., Odaert, B., Roux, M., Metz-Boutigue, M. H., and Dufourc, E. J. (2008) Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains: a new mode of action for antimicrobial peptides? Biochemistry 47, 6394-6402 (Pubitemid 351874231)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6394-6402
    • Jean-Francois, F.1    Castano, S.2    Desbat, B.3    Odaert, B.4    Roux, M.5    Metz-Boutigue, M.-H.6    Dufourc, E.J.7
  • 7
    • 56049097681 scopus 로고    scopus 로고
    • Surfactin-trigged small vesicle formation of negatively charged membranes: A novel membrane-lysis mechanism
    • Buchoux, S., Lai-Kee-Him, J., Garnier, M., Tsan, P., Besson, F., Brisson, A., and Dufourc, E. J. (2008) Surfactin-trigged small vesicle formation of negatively charged membranes: a novel membrane-lysis mechanism. Biophys. J. 95, 3840-3849
    • (2008) Biophys. J. , vol.95 , pp. 3840-3849
    • Buchoux, S.1    Lai-Kee-Him, J.2    Garnier, M.3    Tsan, P.4    Besson, F.5    Brisson, A.6    Dufourc, E.J.7
  • 8
    • 60549086215 scopus 로고    scopus 로고
    • Peptide induced demixing in PG/PE lipid mixtures: A mechanism for the specificity of antimicrobial peptides towards bacterial membranes?
    • Arouri, A., Dathe, M., and Blume, A. (2009) Peptide induced demixing in PG/PE lipid mixtures: a mechanism for the specificity of antimicrobial peptides towards bacterial membranes? Biochim. Biophys. Acta Biomembranes 1788, 650-659
    • (2009) Biochim. Biophys. Acta Biomembranes , vol.1788 , pp. 650-659
    • Arouri, A.1    Dathe, M.2    Blume, A.3
  • 9
    • 42749091734 scopus 로고    scopus 로고
    • Dual mechanism of bacterial lethality for a cationic sequence-random copolymer that mimics host-defense antimicrobial peptides
    • Epand, R. F., Mowery, B. P., Lee, S. E., Stahl, S. S., Lehrer, R. I., Gellman, S. H., and Epand, R. M. (2008) Dual mechanism of bacterial lethality for a cationic sequence-random copolymer that mimics host-defense antimicrobial peptides. J. Mol. Biol. 379, 38-50
    • (2008) J. Mol. Biol. , vol.379 , pp. 38-50
    • Epand, R.F.1    Mowery, B.P.2    Lee, S.E.3    Stahl, S.S.4    Lehrer, R.I.5    Gellman, S.H.6    Epand, R.M.7
  • 10
    • 33748929313 scopus 로고    scopus 로고
    • Role of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides
    • Epand, R. F., Schmitt, M. A., Gellman, S. H., and Epand, R. M. (2006) Role of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides. Biochim. Biophys. Acta Biomembranes 1758, 1343-1350
    • (2006) Biochim. Biophys. Acta Biomembranes , vol.1758 , pp. 1343-1350
    • Epand, R.F.1    Schmitt, M.A.2    Gellman, S.H.3    Epand, R.M.4
  • 11
    • 58149190056 scopus 로고    scopus 로고
    • Lipid domains in bacterial membranes and the action of antimicrobial agents
    • Epand, R. M., and Epand, R. F. (2009) Lipid domains in bacterial membranes and the action of antimicrobial agents. Biochim. Biophys. Acta Biomembranes 1788, 289-294
    • (2009) Biochim. Biophys. Acta Biomembranes , vol.1788 , pp. 289-294
    • Epand, R.M.1    Epand, R.F.2
  • 12
    • 54849407971 scopus 로고    scopus 로고
    • Bacterial membranes as predictors of antimicrobial potency
    • Epand, R. M., Rotem, S., Mor, A., Berno, B., and Epand, R. F. (2008) Bacterial membranes as predictors of antimicrobial potency. J. Am. Chem. Soc. 130, 14346-14352
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14346-14352
    • Epand, R.M.1    Rotem, S.2    Mor, A.3    Berno, B.4    Epand, R.F.5
  • 14
    • 58749101895 scopus 로고    scopus 로고
    • Pore formation induced by an antimicrobial peptide: Electrostatic effects
    • Jean-François, F., Elezgaray, J., Bergson, P., Vacher, P., and Dufourc, E. J. (2008) Pore formation induced by an antimicrobial peptide: electrostatic effects. Biophys. J. 95, 5748-5756
    • (2008) Biophys. J. , vol.95 , pp. 5748-5756
    • Jean-François, F.1    Elezgaray, J.2    Bergson, P.3    Vacher, P.4    Dufourc, E.J.5
  • 15
    • 34249811510 scopus 로고    scopus 로고
    • Plant sterols in "rafts": A better way to regulate membrane thermal shocks
    • Beck, J. G., Mathieu, D., Loudet, C., Buchoux, S., and Dufourc, E. J. (2007) Plant sterols in "rafts": a better way to regulate membrane thermal shocks. FASEB J. 21, 1714-1723
    • (2007) FASEB J. , vol.21 , pp. 1714-1723
    • Beck, J.G.1    Mathieu, D.2    Loudet, C.3    Buchoux, S.4    Dufourc, E.J.5
  • 16
    • 67349185295 scopus 로고    scopus 로고
    • Sterols and membrane dynamics
    • Dufourc, E. J. (2008) Sterols and membrane dynamics. J. Chem. Biol. 1, 63-77
    • (2008) J. Chem. Biol. , vol.1 , pp. 63-77
    • Dufourc, E.J.1
  • 17
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons, K., and Ehehalt, R. (2002) Cholesterol, lipid rafts, and disease. J. Clin. Invest. 110, 597-603
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 18
    • 0034529050 scopus 로고    scopus 로고
    • Cell biology: How cells handle cholesterol
    • Simons, K., and Ikonen, E. (2000) Cell biology: how cells handle cholesterol. Science 290, 1721-1726
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 19
    • 84889479066 scopus 로고    scopus 로고
    • Solid state NMR in biomembranes
    • Larijani, B., Woscholski, R., and Rosser, C. A., eds John Wiley & Sons, London
    • Dufourc, E. J. (2006) Solid state NMR in biomembranes. In Chemical Biology (Larijani, B., Woscholski, R., and Rosser, C. A., eds) pp. 113-131, John Wiley & Sons, London
    • (2006) Chemical Biology , pp. 113-131
    • Dufourc, E.J.1
  • 21
    • 0034176596 scopus 로고    scopus 로고
    • Phospholipid and sterol analysis of plasma membranes of azole-resistant Candida albicans strains
    • DOI 10.1016/S0378-1097(00)00071-9, PII S0378109700000719
    • Loffler, J., Einsele, H., Hebart, H., Schumacher, U., Hrastnik, C., and Daum, G. (2000) Phospholipid and sterol analysis of plasma membranes of azole-resistant Candida albicans strains. FEMS Microbiol. Lett. 185, 59-63 (Pubitemid 30145607)
    • (2000) FEMS Microbiology Letters , vol.185 , Issue.1 , pp. 59-63
    • Loffler, J.1    Einsele, H.2    Hebart, H.3    Schumacher, U.4    Hrastnik, C.5    Daum, G.6
  • 22
    • 33746786361 scopus 로고    scopus 로고
    • Fast and quantitative recovery of hydrophobic and amphipathic peptides after incorporation into phospholipid membranes
    • DOI 10.1021/ac060207w
    • Khemtémourian, L., Bathany, K., Schmitter, J. M., and Dufourc, E. J. (2006) Fast and quantitative recovery of hydrophobic and amphipathic peptides after incorporation into phospholipid membranes. Anal. Chem. 78, 5348-5353 (Pubitemid 44182352)
    • (2006) Analytical Chemistry , vol.78 , Issue.15 , pp. 5348-5353
    • Khemtemourian, L.1    Bathany, K.2    Schmitter, J.-M.3    Dufourc, E.J.4
  • 23
    • 35748982910 scopus 로고    scopus 로고
    • Variability in secondary structure of the antimicrobial peptide Cateslytin in powder, solution, DPC micelles and at the air-water interface
    • DOI 10.1007/s00249-007-0169-8
    • Jean-François, F., Khemtemourian, L., Odaert, B., Castano, S., Grelard, A., Manigand, C., Bathany, K., Metz-Boutigue, M. H., and Dufourc, E. J. (2007) Variability in secondary structure of the antimicrobial peptide cateslytin in powder, solution, DPC micelles and at the air-water interface. Eur. Biophys. J. Biophys. Lett. 36, 1019-1027 (Pubitemid 350045035)
    • (2007) European Biophysics Journal , vol.36 , Issue.8 , pp. 1019-1027
    • Jean-Francois, F.1    Khemtemourian, L.2    Odaert, B.3    Castano, S.4    Grelard, A.5    Manigand, C.6    Bathany, K.7    Metz-Boutigue, M.-H.8    Dufourc, E.J.9
  • 24
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • DOI 10.1016/S0304-4157(99)00004-0, PII S0304415799000040
    • Goormaghtigh, E., Raussens, V., and Ruysschaert, J. M. (1999) Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1422, 105-185 (Pubitemid 29313327)
    • (1999) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1422 , Issue.2 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.-M.3
  • 25
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis, J. H., Jeffrey, K. R., Bloom, M., Valic, M. I., and Higgs, T. P. (1976) Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42, 390-394
    • (1976) Chem. Phys. Lett. , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 26
    • 0346213760 scopus 로고
    • Direct determination of the oriented sample NMR spectrum from the powder spectrum for systems with a local axial symmetry
    • Bloom, M., Davis, J. H., and Mackay, A. L. (1981) Direct determination of the oriented sample NMR spectrum from the powder spectrum for systems with a local axial symmetry. Chem. Phys. Lett. 80, 198-202
    • (1981) Chem. Phys. Lett. , vol.80 , pp. 198-202
    • Bloom, M.1    Davis, J.H.2    Mackay, A.L.3
  • 28
    • 24044479637 scopus 로고    scopus 로고
    • Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi- And multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy
    • DOI 10.1016/j.bbamem.2005.07.008, PII S0005273605002208
    • Castano, S., and Desbat, B. (2005) Structure and orientation study of fusion peptide FP23 of gp41 from HIV-1 alone or inserted into various lipid membrane models (mono-, bi- and multibi-layers) by FT-IR spectroscopies and Brewster angle microscopy. Biochim. Biophys. Acta 1715, 81-95 (Pubitemid 41219696)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1715 , Issue.2 , pp. 81-95
    • Castano, S.1    Desbat, B.2
  • 29
    • 0025932954 scopus 로고
    • Interactions of cholesterol with the membrane lipid matrix: A solid state NMR approach
    • Leonard, A., and Dufourc, E. J. (1991) Interactions of cholesterol with the membrane lipid matrix: a solid state NMR approach. Biochimie (Paris) 73, 1295-1302
    • (1991) Biochimie (Paris) , vol.73 , pp. 1295-1302
    • Leonard, A.1    Dufourc, E.J.2
  • 30
    • 21144453569 scopus 로고    scopus 로고
    • The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: A deuterium NMR and calorimetric study
    • DOI 10.1529/biophysj.104.051375
    • Hsueh, Y. W., Gilbert, K., Trandum, C., Zuckermann, M., and Thewalt, J. (2005) The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: a deuterium NMR and calorimetric study. Biophys. J. 88, 1799-1808 (Pubitemid 40976193)
    • (2005) Biophysical Journal , vol.88 , Issue.3 , pp. 1799-1808
    • Hsueh, Y.-W.1    Gilbert, K.2    Trandum, C.3    Zuckermann, M.4    Thewalt, J.5
  • 31
    • 0020492879 scopus 로고
    • Low-frequency motion in membranes the effect of cholesterol and proteins
    • Cornell, B. A., Davenport, J. B., and Separovic, F. (1982) Low-frequency motion in membranes the effect of cholesterol and proteins. Biochim. Biophys. Acta 689, 337-345
    • (1982) Biochim. Biophys. Acta , vol.689 , pp. 337-345
    • Cornell, B.A.1    Davenport, J.B.2    Separovic, F.3
  • 32
    • 58849083755 scopus 로고    scopus 로고
    • Phase equilibria in DOPC/DPPC-d62/cholesterol mixtures
    • Davis, J. H., Clair, J. J., and Juahsz, J. (2009) Phase equilibria in DOPC/DPPC-d62/cholesterol mixtures. Biophys. J. 96, 521-539
    • (2009) Biophys. J. , vol.96 , pp. 521-539
    • Davis, J.H.1    Clair, J.J.2    Juahsz, J.3
  • 33
    • 58149185333 scopus 로고    scopus 로고
    • Lipid lateral diffusion and membrane heterogeneity
    • Lindblom, G., and Oradd, G. (2009) Lipid lateral diffusion and membrane heterogeneity. Biochim. Biophys. Acta Biomembranes 1788, 234-244
    • (2009) Biochim. Biophys. Acta Biomembranes , vol.1788 , pp. 234-244
    • Lindblom, G.1    Oradd, G.2
  • 36
    • 0028929692 scopus 로고
    • Restatement of order parameters in biomembranes: Calculation of C-C bond order parameters from C-D quadrupolar splittings
    • Douliez, J. P., Leonard, A., and Dufourc, E. J. (1995) Restatement of order parameters in biomembranes: calculation of C-C bond order parameters from C-D quadrupolar splittings. Biophys. J. 68, 1727-1739
    • (1995) Biophys. J. , vol.68 , pp. 1727-1739
    • Douliez, J.P.1    Leonard, A.2    Dufourc, E.J.3
  • 37
    • 33748600386 scopus 로고    scopus 로고
    • 2H-NMR and neutron diffraction
    • Douliez, J. P., Leonard, A., and Dufourc, E. J. (1996) Conformational order of DMPC sn-1 versus sn-2 chains and membrane thickness: an approach to molecular protrusion by solid-state 2H-NMR and neutron diffraction. J. Phys. Chem. 100, 18450-18457 (Pubitemid 126790156)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.47 , pp. 18450-18457
    • Douliez, J.-P.1    Leonard, A.2    Dufourc, E.J.3
  • 38
    • 0016760687 scopus 로고
    • Deuterium order parameters in relation to thermodynamics properties of a phospholipid bilayer: A statistical mechanical interpretation
    • Schindler, H., and Seelig, J. (1975) Deuterium order parameters in relation to thermodynamics properties of a phospholipid bilayer: a statistical mechanical interpretation. Biochemistry 14, 2283-2287
    • (1975) Biochemistry , vol.14 , pp. 2283-2287
    • Schindler, H.1    Seelig, J.2
  • 39
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: Theory and application to lipid membranes
    • Seelig, J. (1977) Deuterium magnetic resonance: theory and application to lipid membranes. Q. Rev. Biophys. 10, 353-418
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 353-418
    • Seelig, J.1
  • 40
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
    • DOI 10.1110/ps.041024904
    • Zandomeneghi, G., Krebs, M. R. H., Mccamon, M. G., and Fändrich, M. (2004) FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Prot. Sci. 13, 3314-3321 (Pubitemid 39557800)
    • (2004) Protein Science , vol.13 , Issue.12 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fandrich, M.4
  • 41
    • 4243468938 scopus 로고    scopus 로고
    • The cation-pi interaction
    • Ma, J. C., and Dougherty, D. A. (1997) The cation-pi interaction. Chem. Rev. 97, 1303-1324
    • (1997) Chem. Rev. , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 42
    • 30344445381 scopus 로고    scopus 로고
    • Ion channel formation by Alzheimer's disease amyloid beta-peptide (A beta 40) in unilamellar liposomes is determined by anionic phospholipids
    • DOI 10.1016/j.peptides.2005.07.004, PII S0196978105003463
    • Alarcon, J. M., Brito, J. A., Hermosilla, T., Atwater, I., Mears, D., and Rojas, E. (2006) Ion channel formation by Alzheimer's disease amyloid beta-peptide (A beta 40) in unilamellar liposomes is determined by anionic phospholipids. Peptides 27, 95-104 (Pubitemid 43061042)
    • (2006) Peptides , vol.27 , Issue.1 , pp. 95-104
    • Alarcon, J.M.1    Brito, J.A.2    Hermosilla, T.3    Atwater, I.4    Mears, D.5    Rojas, E.6
  • 43
    • 0034929069 scopus 로고    scopus 로고
    • Electrostatic peptide-lipid interactions of amyloid-beta peptide and pentalysine with membrane surfaces monitored by P-31 MAS NMR
    • Bonev, B., Watts, A., Bokvist, M., and Grobner, G. (2001) Electrostatic peptide-lipid interactions of amyloid-beta peptide and pentalysine with membrane surfaces monitored by P-31 MAS NMR. Phys. Chem. Chem. Phys. 3, 2904-2910
    • (2001) Phys. Chem. Chem. Phys. , vol.3 , pp. 2904-2910
    • Bonev, B.1    Watts, A.2    Bokvist, M.3    Grobner, G.4
  • 44
    • 35349002742 scopus 로고    scopus 로고
    • Negatively Charged Phospholipid Membranes Induce Amyloid Formation of Medin via an alpha-Helical Intermediate
    • DOI 10.1016/j.jmb.2007.08.064, PII S0022283607011461
    • Olofsson, A., Borowik, T., Grobner, G., and Sauer-Eriksson, A. E. (2007) Negatively charged phospholipid membranes induce amyloid formation of media via an alpha-helical intermediate. J. Mol. Biol. 374, 186-194 (Pubitemid 47600226)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.1 , pp. 186-194
    • Olofsson, A.1    Borowik, T.2    Grobner, G.3    Sauer-Eriksson, A.E.4
  • 45
    • 0342378042 scopus 로고    scopus 로고
    • Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes
    • DOI 10.1021/bi971843e
    • Terzi, E., Holzemann, G., and Seelig, J. (1997) Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes. Biochemistry 36, 14845-14852 (Pubitemid 27524407)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14845-14852
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 46
    • 58549084816 scopus 로고    scopus 로고
    • Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity
    • Wong, P. T., Schauerte, J. A., Wisser, K. C., Ding, H., Lee, E. L., Steel, D. G., and Gafni, A. (2009) Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity. J. Mol. Biol. 386, 81-96
    • (2009) J. Mol. Biol. , vol.386 , pp. 81-96
    • Wong, P.T.1    Schauerte, J.A.2    Wisser, K.C.3    Ding, H.4    Lee, E.L.5    Steel, D.G.6    Gafni, A.7
  • 47
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu, D., and Rivas, L. (1998) Animal antimicrobial peptides: an overview. Biopolymers 47, 415-433
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 48
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 49
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M., and Vogel, H. J. (1999) Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462, 11-28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 50
    • 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
  • 51
    • 37349002470 scopus 로고    scopus 로고
    • Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization
    • DOI 10.1529/biophysj.107.116681
    • Mason, A. J., Marquette, A., and Bechinger, B. (2007) Zwitterionic phospholipids and sterols modulate antimicrobial peptide-induced membrane destabilization. Biophys. J. 93, 4289-4299 (Pubitemid 350294476)
    • (2007) Biophysical Journal , vol.93 , Issue.12 , pp. 4289-4299
    • Mason, A.J.1    Marquette, A.2    Bechinger, B.3
  • 52
    • 33644886043 scopus 로고    scopus 로고
    • Membrane activity of biomimetic facially amphiphilic antibiotics
    • Arnt, L., Rennie, J. R., Linser, S., Willumeit, R., and Tew, G. N. (2006) Membrane activity of biomimetic facially amphiphilic antibiotics. J. Phys. Chem. B 110, 3527-3532
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3527-3532
    • Arnt, L.1    Rennie, J.R.2    Linser, S.3    Willumeit, R.4    Tew, G.N.5
  • 54
    • 20444369884 scopus 로고    scopus 로고
    • Induced resistance to the antimicrobial peptide lactoferricin B in Staphylococcus aureus
    • DOI 10.1016/j.febslet.2005.05.017, PII S0014579305006150
    • Samuelsen, O., Haukland, H. H., Jenssen, H., Kramer, M., Sandvik, K., Ulvatne, H., and Vorland, L. H. (2005) Induced resistance to the antimicrobial peptide lactoferricin B in Staphylococcus aureus. FEBS Lett. 579, 3421-3426 (Pubitemid 40800292)
    • (2005) FEBS Letters , vol.579 , Issue.16 , pp. 3421-3426
    • Samuelsen, O.1    Haukland, H.H.2    Jenssen, H.3    Kramer, M.4    Sandvik, K.5    Ulvatne, H.6    Vorland, L.H.7
  • 55
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • DOI 10.1016/S0966-842X(02)02333-8, PII S0966842X02023338
    • Peschel, A. (2002) How do bacteria resist human antimicrobial peptides? Trends Microbiol. 10, 179-186 (Pubitemid 34242955)
    • (2002) Trends in Microbiology , vol.10 , Issue.4 , pp. 179-186
    • Peschel, A.1
  • 56
    • 23044457737 scopus 로고    scopus 로고
    • Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus
    • DOI 10.1128/AAC.49.8.3114-3121.2005
    • Xiong, Y. Q., Mukhopadhyay, K., Yeaman, M. R., Adler-Moore, J., and Bayer, A. S. (2005) Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus. Antimicrobiol. Agents Chemother. 49, 3114-3121 (Pubitemid 41060548)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.8 , pp. 3114-3121
    • Xiong, Y.Q.1    Mukhopadhyay, K.2    Yeaman, M.R.3    Adler-Moore, J.4    Bayer, A.S.5


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