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Volumn 47, Issue 24, 2008, Pages 6468-6478

Parameters involved in antimicrobial and endotoxin detoxification activities of antimicrobial peptides

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; BACTERIA; BACTERIOLOGY; COMPUTER NETWORKS; DETOXIFICATION; ORGANIC ACIDS; PEPTIDES; POLYSACCHARIDES; PROTEINS; STRUCTURE (COMPOSITION);

EID: 45749084085     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800450f     Document Type: Article
Times cited : (72)

References (53)
  • 1
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido, H. (1994) Prevention of drug access to bacterial targets: Permeability barriers and active efflux. Science 264, 382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 2
    • 0034718563 scopus 로고    scopus 로고
    • The lipopolysaccharide barrier: Correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics
    • Snyder, D. S., and McIntosh, T. J. (2000) The lipopolysaccharide barrier: Correlation of antibiotic susceptibility with antibiotic permeability and fluorescent probe binding kinetics. Biochemistry 39, 11777-11787.
    • (2000) Biochemistry , vol.39 , pp. 11777-11787
    • Snyder, D.S.1    McIntosh, T.J.2
  • 3
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985) Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49, 1-32.
    • (1985) Microbiol. Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 4
    • 0021185399 scopus 로고
    • Alterations in outer membrane permeability
    • Hancock, R. E. (1984) Alterations in outer membrane permeability. Annu. Rev. Microbiol. 38, 237-264.
    • (1984) Annu. Rev. Microbiol , vol.38 , pp. 237-264
    • Hancock, R.E.1
  • 5
    • 0036877034 scopus 로고    scopus 로고
    • The role of bacteriolysis in the pathophysiology of inflammation, infection and post-infectious sequelae
    • Ginsburg, I. (2002) The role of bacteriolysis in the pathophysiology of inflammation, infection and post-infectious sequelae. APMIS 110, 753-770.
    • (2002) APMIS 110 , pp. 753-770
    • Ginsburg, I.1
  • 6
    • 0032997542 scopus 로고    scopus 로고
    • Recognition of gram-negative bacteria and endotoxin by the innate immune system
    • Ulevitch, R. J., and Tobias, P. S. (1999) Recognition of gram-negative bacteria and endotoxin by the innate immune system. Curr. Opin. Immunol. 11, 19-22.
    • (1999) Curr. Opin. Immunol , vol.11 , pp. 19-22
    • Ulevitch, R.J.1    Tobias, P.S.2
  • 7
    • 0022462376 scopus 로고
    • Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum
    • Tobias, P. S., Soldau, K., and Ulevitch, R. J. (1986) Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J. Exp. Med. 164, 777-793.
    • (1986) J. Exp. Med , vol.164 , pp. 777-793
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 9
    • 0033583034 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide activates nuclear factor-κB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes
    • Zhang, F. X., Kirschning, C. J., Mancinelli, R., Xu, X. P., Jin, Y., Faure, E., Mantovani, A., Rothe, M., Muzio, M., and Arditi, M. (1999) Bacterial lipopolysaccharide activates nuclear factor-κB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes. J. Biol. Chem. 274, 7611-7614.
    • (1999) J. Biol. Chem , vol.274 , pp. 7611-7614
    • Zhang, F.X.1    Kirschning, C.J.2    Mancinelli, R.3    Xu, X.P.4    Jin, Y.5    Faure, E.6    Mantovani, A.7    Rothe, M.8    Muzio, M.9    Arditi, M.10
  • 10
    • 0037180768 scopus 로고    scopus 로고
    • The immunopathogenesis of sepsis
    • Cohen, J. (2002) The immunopathogenesis of sepsis. Nature 420, 885-891.
    • (2002) Nature , vol.420 , pp. 885-891
    • Cohen, J.1
  • 11
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92.
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 12
    • 3142770748 scopus 로고    scopus 로고
    • Endotoxin neutralizing peptides
    • Jerala, R., and Porro, M. (2004) Endotoxin neutralizing peptides. Curr. Top. Med. Chem. 4, 1173-1184.
    • (2004) Curr. Top. Med. Chem , vol.4 , pp. 1173-1184
    • Jerala, R.1    Porro, M.2
  • 13
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E., and Scott, M. G. (2000) The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. U.S.A. 97, 8856-8861.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 14
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (Lipopolysaccharide) Neutralization by Innate Immunity Host-Defense Peptides: Peptide Properties and Plausible Modes of Action
    • Rosenfeld, Y., Papo, N., and Shai, Y. (2006) Endotoxin (Lipopolysaccharide) Neutralization by Innate Immunity Host-Defense Peptides: Peptide Properties and Plausible Modes of Action. J. Biol. Chem. 281, 1636-1643.
    • (2006) J. Biol. Chem , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 15
    • 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
  • 16
    • 0034665513 scopus 로고    scopus 로고
    • An α-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression
    • Scott, M. G., Rosenberger, C. M., Gold, M. R., Finlay, B. B., and Hancock, R. E. (2000) An α-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression. J. Immunol. 165, 3358-3365.
    • (2000) J. Immunol , vol.165 , pp. 3358-3365
    • Scott, M.G.1    Rosenberger, C.M.2    Gold, M.R.3    Finlay, B.B.4    Hancock, R.E.5
  • 17
    • 2142753042 scopus 로고    scopus 로고
    • Biophysical characterization of endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-lysin
    • Andra, J., Koch, M. H., Bartels, R., and Brandenburg, K. (2004) Biophysical characterization of endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-lysin. Antimicrob. Agents Chemother. 48, 1593-1599.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 1593-1599
    • Andra, J.1    Koch, M.H.2    Bartels, R.3    Brandenburg, K.4
  • 18
    • 2342514277 scopus 로고    scopus 로고
    • Effects of antimicrobial peptides derived from the beetle Allomyrina dichotoma defensin on mouse peritoneal macrophages stimulated with lipopolysaccharide
    • Motobu, M., Amer, S., Yamada, M., Nakamura, K., Saido-Sakanaka, H., Asaoka, A., Yamakawa, M., and Hirota, Y. (2004) Effects of antimicrobial peptides derived from the beetle Allomyrina dichotoma defensin on mouse peritoneal macrophages stimulated with lipopolysaccharide. J. Vet. Med. Sci. 66, 319-322.
    • (2004) J. Vet. Med. Sci , vol.66 , pp. 319-322
    • Motobu, M.1    Amer, S.2    Yamada, M.3    Nakamura, K.4    Saido-Sakanaka, H.5    Asaoka, A.6    Yamakawa, M.7    Hirota, Y.8
  • 19
    • 0028949278 scopus 로고
    • Human CAP18: A novel antimicrobial lipopolysaccharide- binding protein
    • Larrick, J. W., Hirata, M., Balint, R. F., Lee, J., Zhong, J., and Wright, S. C. (1995) Human CAP18: A novel antimicrobial lipopolysaccharide- binding protein. Infect. Immun. 63, 1291-1297.
    • (1995) Infect. Immun , vol.63 , pp. 1291-1297
    • Larrick, J.W.1    Hirata, M.2    Balint, R.F.3    Lee, J.4    Zhong, J.5    Wright, S.C.6
  • 21
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown, K. L., and Hancock, R. E. (2005) Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 18, 24-30.
    • (2005) Curr. Opin. Immunol , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 22
    • 0032942642 scopus 로고    scopus 로고
    • The amphipathic helix concept: Length effects on ideally amphipathic LiKj(i=2j) peptides to acquire optimal hemolytic activity
    • Castano, S., Cornut, I., Buttner, K., Dasseux, J. L., and Dufourcq, J. (1999) The amphipathic helix concept: Length effects on ideally amphipathic LiKj(i=2j) peptides to acquire optimal hemolytic activity. Biochim. Biophys. Acta 1416, 161-175.
    • (1999) Biochim. Biophys. Acta , vol.1416 , pp. 161-175
    • Castano, S.1    Cornut, I.2    Buttner, K.3    Dasseux, J.L.4    Dufourcq, J.5
  • 23
    • 0038192455 scopus 로고    scopus 로고
    • The antibiotic activity of cationic linear amphipathic peptides: Lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes
    • Beven, L., Castano, S., Dufourcq, J., Wieslander, A., and Wroblewski, H. (2003) The antibiotic activity of cationic linear amphipathic peptides: Lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes. Eur. J. Biochem. 270, 2207-2217.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2207-2217
    • Beven, L.1    Castano, S.2    Dufourcq, J.3    Wieslander, A.4    Wroblewski, H.5
  • 24
    • 0026787169 scopus 로고
    • Interaction of D-amino acid incorporated analogues of pardaxin with membranes
    • Pouny, Y., and Shai, Y. (1992) Interaction of D-amino acid incorporated analogues of pardaxin with membranes. Biochemistry 31, 9482-9490.
    • (1992) Biochemistry , vol.31 , pp. 9482-9490
    • Pouny, Y.1    Shai, Y.2
  • 25
    • 0026354984 scopus 로고
    • Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers
    • Rapaport, D., and Shai, Y. (1991) Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers. J. Biol. Chem. 266, 23769-23775.
    • (1991) J. Biol. Chem , vol.266 , pp. 23769-23775
    • Rapaport, D.1    Shai, Y.2
  • 26
    • 0034726410 scopus 로고    scopus 로고
    • Analysis of lipopolysaccharide (LPS)-binding characteristics of serum components using gel filtration of FITC-labeled LPS
    • de Haas, C. J., van Leeuwen, H. J., Verhoef, J., van Kessel, K. P., and van Strijp, J. A. (2000) Analysis of lipopolysaccharide (LPS)-binding characteristics of serum components using gel filtration of FITC-labeled LPS. J. Immunol. Methods 242, 79-89.
    • (2000) J. Immunol. Methods , vol.242 , pp. 79-89
    • de Haas, C.J.1    van Leeuwen, H.J.2    Verhoef, J.3    van Kessel, K.P.4    van Strijp, J.A.5
  • 27
    • 0034705132 scopus 로고    scopus 로고
    • Cyclization of a cytolytic amphipathic α-helical peptide and its diastereomer: Effect on structure, interaction with model membranes, and biological function
    • Oren, Z., and Shai, Y. (2000) Cyclization of a cytolytic amphipathic α-helical peptide and its diastereomer: Effect on structure, interaction with model membranes, and biological function. Biochemistry 39, 6103-6114.
    • (2000) Biochemistry , vol.39 , pp. 6103-6114
    • Oren, Z.1    Shai, Y.2
  • 28
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm, L. K., and Tatulian, S. A. (1997) Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30, 365-429.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 29
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 30
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • Wu, C. S., Ikeda, K., and Yang, J. T. (1981) Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20, 566-670.
    • (1981) Biochemistry , vol.20 , pp. 566-670
    • Wu, C.S.1    Ikeda, K.2    Yang, J.T.3
  • 31
    • 0035210771 scopus 로고    scopus 로고
    • Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate
    • Meng, F. G., Zeng, X., Hong, Y. K., and Zhou, H. M. (2001) Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate. Biochimie 83, 953-956.
    • (2001) Biochimie , vol.83 , pp. 953-956
    • Meng, F.G.1    Zeng, X.2    Hong, Y.K.3    Zhou, H.M.4
  • 32
    • 0032754358 scopus 로고    scopus 로고
    • Relationship between plasma levels of lipopolysaccharide (LPS) and LPS-binding protein in patients with severe sepsis and septic shock
    • Opal, S. M., Scannon, P. J., Vincent, J. L., White, M., Carroll, S. F., Palardy, J. E., Parejo, N. A., Pribble, J. P., and Lemke, J. H. (1999) Relationship between plasma levels of lipopolysaccharide (LPS) and LPS-binding protein in patients with severe sepsis and septic shock. J. Infect. Dis. 180, 1584-1589.
    • (1999) J. Infect. Dis , vol.180 , pp. 1584-1589
    • Opal, S.M.1    Scannon, P.J.2    Vincent, J.L.3    White, M.4    Carroll, S.F.5    Palardy, J.E.6    Parejo, N.A.7    Pribble, J.P.8    Lemke, J.H.9
  • 33
    • 0025647096 scopus 로고
    • Membrane insertion and lateral diffusion of fluorescence-labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers
    • Frey, S., and Tamm, L. K. (1990) Membrane insertion and lateral diffusion of fluorescence-labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers. Biochem. J. 272, 713-719.
    • (1990) Biochem. J , vol.272 , pp. 713-719
    • Frey, S.1    Tamm, L.K.2
  • 34
    • 0033839604 scopus 로고    scopus 로고
    • Mechanisms of action of rabbit CAP18 on monolayers and liposomes made from endotoxins or phospholipids
    • Gutsmann, T., Fix, M., Larrick, J. W., and Wiese, A. (2000) Mechanisms of action of rabbit CAP18 on monolayers and liposomes made from endotoxins or phospholipids. J. Membr. Biol. 176, 223-236.
    • (2000) J. Membr. Biol , vol.176 , pp. 223-236
    • Gutsmann, T.1    Fix, M.2    Larrick, J.W.3    Wiese, A.4
  • 35
    • 15444370838 scopus 로고    scopus 로고
    • A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides
    • Papo, N., and Shai, Y. (2005) A molecular mechanism for lipopolysaccharide protection of Gram-negative bacteria from antimicrobial peptides. J. Biol. Chem. 280, 10378-10387.
    • (2005) J. Biol. Chem , vol.280 , pp. 10378-10387
    • Papo, N.1    Shai, Y.2
  • 36
    • 0037133202 scopus 로고    scopus 로고
    • Conjugation of a magainin analogue with lipophilic acids controls hydrophobicity, solution assembly, and cell selectivity
    • Avrahami, D., and Shai, Y. (2002) Conjugation of a magainin analogue with lipophilic acids controls hydrophobicity, solution assembly, and cell selectivity. Biochemistry 41, 2254-2263.
    • (2002) Biochemistry , vol.41 , pp. 2254-2263
    • Avrahami, D.1    Shai, Y.2
  • 37
    • 1842478127 scopus 로고    scopus 로고
    • A new group of antifungal and antibacterial lipopeptides derived from non-membrane active peptides conjugated to palmitic acid
    • Avrahami, D., and Shai, Y. (2004) A new group of antifungal and antibacterial lipopeptides derived from non-membrane active peptides conjugated to palmitic acid. J. Biol. Chem. 279, 12277-12285.
    • (2004) J. Biol. Chem , vol.279 , pp. 12277-12285
    • Avrahami, D.1    Shai, Y.2
  • 38
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 39
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • Frey, S., and Tamm, L. K. (1991) Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys. J. 60, 922-930.
    • (1991) Biophys. J , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 40
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes:Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z., Lerman, J. C., Gudmundsson, G. H., Agerberth, B., and Shai, Y. (1999) Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes:Relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341, 501-513.
    • (1999) Biochem. J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 41
    • 0033576264 scopus 로고    scopus 로고
    • 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids
    • Sharon, M., Oren, Z., Shai, Y., and Anglister, J. (1999) 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids. Biochemistry 38, 15305-15316.
    • (1999) Biochemistry , vol.38 , pp. 15305-15316
    • Sharon, M.1    Oren, Z.2    Shai, Y.3    Anglister, J.4
  • 42
    • 0037072808 scopus 로고    scopus 로고
    • The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers
    • Papo, N., Oren, Z., Pag, U., Sahl, H. G., and Shai, Y. (2002) The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers. J. Biol. Chem. 277, 33913-33921.
    • (2002) J. Biol. Chem , vol.277 , pp. 33913-33921
    • Papo, N.1    Oren, Z.2    Pag, U.3    Sahl, H.G.4    Shai, Y.5
  • 43
    • 25444458008 scopus 로고    scopus 로고
    • Anti-endotoxin properties of cationic host defence peptides and proteins
    • Bowdish, D. M., and Hancock, R. E. (2005) Anti-endotoxin properties of cationic host defence peptides and proteins. J. Endotoxin Res. 11, 230-236.
    • (2005) J. Endotoxin Res , vol.11 , pp. 230-236
    • Bowdish, D.M.1    Hancock, R.E.2
  • 45
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren, Z., and Shai, Y. (1998) Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers 47, 451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 46
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-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
  • 47
    • 9444225012 scopus 로고    scopus 로고
    • Mode of action of the antimicrobial peptide indolicidin
    • Falla, T. J., Karunaratne, D. N., and Hancock, R. E. (1996) Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271, 19298-19303.
    • (1996) J. Biol. Chem , vol.271 , pp. 19298-19303
    • Falla, T.J.1    Karunaratne, D.N.2    Hancock, R.E.3
  • 48
    • 0025977855 scopus 로고
    • Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers
    • Matsuzaki, K., Harada, M., Funakoshi, S., Fujii, N., and Miyajima, K. (1991) Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. Biochim. Biophys. Acta 1063, 162-170.
    • (1991) Biochim. Biophys. Acta , vol.1063 , pp. 162-170
    • Matsuzaki, K.1    Harada, M.2    Funakoshi, S.3    Fujii, N.4    Miyajima, K.5
  • 50
    • 0027436038 scopus 로고
    • Role of the physical state of Salmonella lipopolysaccharide in expression of biological and endotoxic properties
    • Shnyra, A., Hultenby, K., and Lindberg, A. A. (1993) Role of the physical state of Salmonella lipopolysaccharide in expression of biological and endotoxic properties. Infect. Immun. 61, 5351-5360.
    • (1993) Infect. Immun , vol.61 , pp. 5351-5360
    • Shnyra, A.1    Hultenby, K.2    Lindberg, A.A.3
  • 51
    • 4444340627 scopus 로고    scopus 로고
    • Cyclic antimicrobial peptides based on Limulus anti-lipopolysaccharide factor for neutralization of lipopolysaccharide
    • Andra, J., Lamata, M., Martinez de Tejada, G., Bartels, R., Koch, M. H., and Brandenburg, K. (2004) Cyclic antimicrobial peptides based on Limulus anti-lipopolysaccharide factor for neutralization of lipopolysaccharide. Biochem. Pharmacol. 68, 1297-1307.
    • (2004) Biochem. Pharmacol , vol.68 , pp. 1297-1307
    • Andra, J.1    Lamata, M.2    Martinez de Tejada, G.3    Bartels, R.4    Koch, M.H.5    Brandenburg, K.6
  • 52
    • 34147162786 scopus 로고    scopus 로고
    • Thermodynamic analysis of the lipopolysaccharide-dependent resistance of gram-negative bacteria against polymyxin B
    • Howe, J., Andra, J., Conde, R., Iriarte, M., Garidel, P., Koch, M. H., Gutsmann, T., Moriyon, I., and Brandenburg, K. (2007) Thermodynamic analysis of the lipopolysaccharide-dependent resistance of gram-negative bacteria against polymyxin B. Biophys. J. 92, 2796-2805.
    • (2007) Biophys. J , vol.92 , pp. 2796-2805
    • Howe, J.1    Andra, J.2    Conde, R.3    Iriarte, M.4    Garidel, P.5    Koch, M.H.6    Gutsmann, T.7    Moriyon, I.8    Brandenburg, K.9
  • 53
    • 34548178989 scopus 로고    scopus 로고
    • Mechanism of interaction of optimized Limulus-derived cyclic peptides with endotoxins: Thermodynamic, biophysical and microbiological analysis
    • Andra, J., Howe, J., Garidel, P., Rossle, M., Richter, W., Leiva-Leon, J., Moriyon, I., Bartels, R., Gutsmann, T., and Brandenburg, K. (2007) Mechanism of interaction of optimized Limulus-derived cyclic peptides with endotoxins: Thermodynamic, biophysical and microbiological analysis. Biochem. J. 406, 297-307.
    • (2007) Biochem. J , vol.406 , pp. 297-307
    • Andra, J.1    Howe, J.2    Garidel, P.3    Rossle, M.4    Richter, W.5    Leiva-Leon, J.6    Moriyon, I.7    Bartels, R.8    Gutsmann, T.9    Brandenburg, K.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.