메뉴 건너뛰기




Volumn 307, Issue 1, 2003, Pages 133-138

Biopanning of endotoxin-specific phage displayed peptides

Author keywords

Biopanning; Endotoxin; Lipid A; Lipopolysaccharide; Surface plasmon resonance

Indexed keywords

ENDOTOXIN; LIPID A; LIPID BINDING PROTEIN; PEPTIDE; PEPTIDE LIBRARY;

EID: 0037634532     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01136-7     Document Type: Article
Times cited : (16)

References (35)
  • 2
  • 3
    • 0033955233 scopus 로고    scopus 로고
    • Genes, receptors, signals and responses to lipopolysaccharide endotoxin
    • Wong P.M., Chung S.W., Sultzer B.M. Genes, receptors, signals and responses to lipopolysaccharide endotoxin. Scand. J. Immunol. 51:2000;123-127.
    • (2000) Scand. J. Immunol. , vol.51 , pp. 123-127
    • Wong, P.M.1    Chung, S.W.2    Sultzer, B.M.3
  • 4
    • 0027478331 scopus 로고
    • Bactericidal/permeability increasing protein and host defense against Gram-negative bacteria and endotoxin
    • Elsbach P., Weiss J. Bactericidal/permeability increasing protein and host defense against Gram-negative bacteria and endotoxin. Curr. Opin. Immunol. 5:1993;103-107.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 103-107
    • Elsbach, P.1    Weiss, J.2
  • 5
    • 0028941067 scopus 로고
    • E5531, a pure endotoxin antagonist of high potency
    • Christ W.J., Asano O., Robidoux A.L.C.et al. E5531, a pure endotoxin antagonist of high potency. Science. 268:1995;80-83.
    • (1995) Science , vol.268 , pp. 80-83
    • Christ, W.J.1    Asano, O.2    Robidoux, A.L.C.3
  • 6
    • 0028343059 scopus 로고
    • Prevention of lipopolysaccharide-induced lethal toxicity by tyrosine kinase inhibitors
    • Novogrodsky A., Vanichkin A., Patya M., Gazit A., Osherov N., Levitzki A. Prevention of lipopolysaccharide-induced lethal toxicity by tyrosine kinase inhibitors. Science. 264:1994;1319-1322.
    • (1994) Science , vol.264 , pp. 1319-1322
    • Novogrodsky, A.1    Vanichkin, A.2    Patya, M.3    Gazit, A.4    Osherov, N.5    Levitzki, A.6
  • 7
    • 0017119987 scopus 로고
    • Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides
    • Morrison D.C., Jacobs D.M. Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides. Immunochemistry. 13:1976;813-818.
    • (1976) Immunochemistry , vol.13 , pp. 813-818
    • Morrison, D.C.1    Jacobs, D.M.2
  • 8
    • 0033054742 scopus 로고    scopus 로고
    • Clinical trials for severe sepsis. Past failures, and future hopes
    • vii
    • Cross A.S., Opal S. Clinical trials for severe sepsis. Past failures, and future hopes. Infect. Dis. Clin. North Am. 13(2):1999;285-297. vii.
    • (1999) Infect. Dis. Clin. North Am. , vol.13 , Issue.2 , pp. 285-297
    • Cross, A.S.1    Opal, S.2
  • 9
    • 0014077554 scopus 로고
    • Studies on the interaction between endotoxin and polymyxin B
    • Rifkind D. Studies on the interaction between endotoxin and polymyxin B. J. Bacteriol. 93:1967;1463-1464.
    • (1967) J. Bacteriol. , vol.93 , pp. 1463-1464
    • Rifkind, D.1
  • 10
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA. 84:1987;5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 11
    • 0033136960 scopus 로고    scopus 로고
    • Strategies for the control of LPS-mediated pathophysiological disorders
    • Chaby R. Strategies for the control of LPS-mediated pathophysiological disorders. Drug Discov. Today. 4:1999;209-222.
    • (1999) Drug Discov. Today , vol.4 , pp. 209-222
    • Chaby, R.1
  • 12
    • 0035929559 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of the interactions of 23-residue peptides with endotoxin
    • Thomas C.J., Surolia N., Surolia A. Kinetic and thermodynamic analysis of the interactions of 23-residue peptides with endotoxin. J. Biol. Chem. 276(38):2001;35701-35706.
    • (2001) J. Biol. Chem. , vol.276 , Issue.38 , pp. 35701-35706
    • Thomas, C.J.1    Surolia, N.2    Surolia, A.3
  • 13
    • 0019866623 scopus 로고
    • Involvement of the outer membrane in gentamicin and streptomycin uptake and killing in Pseudomonas aeruginosa
    • Hancock R.E., Raffle V.J., Nicas T.I. Involvement of the outer membrane in gentamicin and streptomycin uptake and killing in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 19:1981;777-785.
    • (1981) Antimicrob. Agents Chemother. , vol.19 , pp. 777-785
    • Hancock, R.E.1    Raffle, V.J.2    Nicas, T.I.3
  • 14
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren Z., Shai Y. Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers. 47:1998;451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 15
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu D., Rivas L. Animal antimicrobial peptides: an overview. Biopolymers. 47:1998;415-433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 16
    • 0030957876 scopus 로고    scopus 로고
    • Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes
    • Wieprecht T., Dathe M., Beyerman M., Krause E., Maloy W.L., MacDonald D.L., Bienert M. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry. 36:1997;6124-6132.
    • (1997) Biochemistry , vol.36 , pp. 6124-6132
    • Wieprecht, T.1    Dathe, M.2    Beyerman, M.3    Krause, E.4    Maloy, W.L.5    MacDonald, D.L.6    Bienert, M.7
  • 17
    • 0033569894 scopus 로고    scopus 로고
    • Surface plasmon resonance studies resolve the enigmatic endotoxin neutralizing activity of polymyxin B
    • Thomas C.J., Surolia N., Surolia A. Surface plasmon resonance studies resolve the enigmatic endotoxin neutralizing activity of polymyxin B. J. Biol. Chem. 274:1999;29624-29627.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29624-29627
    • Thomas, C.J.1    Surolia, N.2    Surolia, A.3
  • 18
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock R.E.W. Peptide antibiotics. Lancet. 349:1997;418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.W.1
  • 19
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy W.L., Kari U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers. 37:1995;105-122.
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 20
    • 0025285857 scopus 로고
    • Biochemistry of endotoxins
    • Raetz C.R.H. Biochemistry of endotoxins. Ann. Rev. Biochem. 59:1990;129-170.
    • (1990) Ann. Rev. Biochem. , vol.59 , pp. 129-170
    • Raetz, C.R.H.1
  • 21
    • 0024210147 scopus 로고
    • Antibody selectable filamentous fd phage vectors: Affinity purification of target genes
    • Parmley S.F., Smith G.P. Antibody selectable filamentous fd phage vectors: affinity purification of target genes. Genes. 73:1988;305-318.
    • (1988) Genes , vol.73 , pp. 305-318
    • Parmley, S.F.1    Smith, G.P.2
  • 22
    • 0031765237 scopus 로고    scopus 로고
    • Topological mimicry and epitope duplication in the guanylyl cyclase C receptor protein
    • Nandi A., Suguna K., Surolia A., Visweswariah S.S. Topological mimicry and epitope duplication in the guanylyl cyclase C receptor protein. Protein Sci. 7:1998;2175-2183.
    • (1998) Protein Sci. , vol.7 , pp. 2175-2183
    • Nandi, A.1    Suguna, K.2    Surolia, A.3    Visweswariah, S.S.4
  • 23
    • 0030976150 scopus 로고    scopus 로고
    • Bacteriophage display and discovery of peptides leads for drug development
    • Lowman H.B. Bacteriophage display and discovery of peptides leads for drug development. Ann. Rev. Biophys. Biomol. Struct. 26:1997;401-424.
    • (1997) Ann. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 401-424
    • Lowman, H.B.1
  • 24
    • 0033017472 scopus 로고    scopus 로고
    • Kinetics of the interaction of endotoxin with polymyxin B and its analogs: A surface plasmon resonance analysis
    • Thomas C.J., Surolia A. Kinetics of the interaction of endotoxin with polymyxin B and its analogs: a surface plasmon resonance analysis. FEBS Lett. 445(2-3):1997;420-424.
    • (1997) FEBS Lett. , vol.445 , Issue.2-3 , pp. 420-424
    • Thomas, C.J.1    Surolia, A.2
  • 26
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 27
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg D., Weiss R.M., Terwilliger The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA. 81:1984;140-144.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger3
  • 28
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg D., Schwarz E., Komaromy M., Wall R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:1984;125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 29
    • 0033784939 scopus 로고    scopus 로고
    • Quantitative analyses of binding affinity and specificity for glycolipid receptors by surface plasmon resonance
    • Mackenzie C.R., Hirama T. Quantitative analyses of binding affinity and specificity for glycolipid receptors by surface plasmon resonance. Methods Enzymol. 312:2000;205-216.
    • (2000) Methods Enzymol. , vol.312 , pp. 205-216
    • Mackenzie, C.R.1    Hirama, T.2
  • 30
    • 0028308297 scopus 로고
    • Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors
    • Peters E.A., Schatz P.J., Johnson S.S., Dower W.J. Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors. J. Bacteriol. 176:1994;4296-4305.
    • (1994) J. Bacteriol. , vol.176 , pp. 4296-4305
    • Peters, E.A.1    Schatz, P.J.2    Johnson, S.S.3    Dower, W.J.4
  • 31
    • 0031022395 scopus 로고    scopus 로고
    • Bilayer interactions of indolicidins, a small anti-microbial peptide rich in tryptophan, proline and basic amino acids
    • Ladokhin A.S., Selsted M.E., White S.H. Bilayer interactions of indolicidins, a small anti-microbial peptide rich in tryptophan, proline and basic amino acids. Biophys. J. 72:1997;794-805.
    • (1997) Biophys. J. , vol.72 , pp. 794-805
    • Ladokhin, A.S.1    Selsted, M.E.2    White, S.H.3
  • 32
    • 0033551685 scopus 로고    scopus 로고
    • Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin
    • Nagpal S., Gupta V., Kaur K.J., Salunke D.M. Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin. J. Biol. Chem. 274:1999;23296-23304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23296-23304
    • Nagpal, S.1    Gupta, V.2    Kaur, K.J.3    Salunke, D.M.4
  • 33
    • 0037377318 scopus 로고    scopus 로고
    • Sequence and structural diversity in endotoxin-binding dodecapeptides
    • Zhu Y., Ho B., Ding J.L. Sequence and structural diversity in endotoxin-binding dodecapeptides. Biochim. Biophys. Acta. 1611:2003;234-242.
    • (2003) Biochim. Biophys. Acta , vol.1611 , pp. 234-242
    • Zhu, Y.1    Ho, B.2    Ding, J.L.3
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specificity, gap penalties and weight matrix choice
    • Thomson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position specificity, gap penalties and weight matrix choice. Nucleic Acid Res. 22:1994;4673-4680.
    • (1994) Nucleic Acid Res. , vol.22 , pp. 4673-4680
    • Thomson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.