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Volumn 6, Issue 12, 1999, Pages 891-899

Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium

Author keywords

Lipid monolayer; Membrane anchor; Surface plasmon resonance (SPR); Vancomycin resistant enterococci (VRE)

Indexed keywords


EID: 0033485286     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)80008-3     Document Type: Article
Times cited : (90)

References (42)
  • 1
    • 0014446989 scopus 로고
    • Specificity of combination between mucopeptide precursors and vancomycin or ristocetin
    • Perkins, H.R. (1969). Specificity of combination between mucopeptide precursors and vancomycin or ristocetin. Biochem. J. 111, 195-205.
    • (1969) Biochem. J. , vol.111 , pp. 195-205
    • Perkins, H.R.1
  • 2
    • 0021919998 scopus 로고
    • Structural features that affect the binding of teicoplanin, ristocetin A, and their derivatives to the bacterial cell wall model N-acetyl-D-alanyl-D-alanine
    • Barna, J.C.J., Williams, D.H. & Williamson, M.L (1985). Structural features that affect the binding of teicoplanin, ristocetin A, and their derivatives to the bacterial cell wall model N-acetyl-D-alanyl-D-alanine. J. Chem. Soc. Chem. Commun., 254-256.
    • (1985) J. Chem. Soc. Chem. Commun. , pp. 254-256
    • Barna, J.C.J.1    Williams, D.H.2    Williamson, M.L.3
  • 3
    • 0027401261 scopus 로고
    • The role of the sugar and chlorine substituents in the dimerization of vancomycin antibiotics
    • Gerhard, U., Mackay, J.P., Maplestone, R.A. & Williams, D.H. (1993). The role of the sugar and chlorine substituents in the dimerization of vancomycin antibiotics. J. Am. Chem. Soc. 115, 232-237.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 232-237
    • Gerhard, U.1    Mackay, J.P.2    Maplestone, R.A.3    Williams, D.H.4
  • 4
    • 0027936628 scopus 로고
    • Glycopeptide antibiotic activity and the possible role of dimerization: A model for biological signalling
    • Mackay, J.P., Gerhard, U., Beauregard, D.A., Westwell, M.S., Searle, M.S. & Williams, D.H. (1994). Glycopeptide antibiotic activity and the possible role of dimerization: A model for biological signalling. J. Am. Chem. Soc. 116, 4581-4590.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4581-4590
    • Mackay, J.P.1    Gerhard, U.2    Beauregard, D.A.3    Westwell, M.S.4    Searle, M.S.5    Williams, D.H.6
  • 5
    • 0028942365 scopus 로고
    • Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics
    • Beauregard, D.A., Williams, D.H., Gwynn, M.N. & Knowles, D.J.C. (1995). Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics. Antimicrob. Agents Chemother. 39, 781-785.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 781-785
    • Beauregard, D.A.1    Williams, D.H.2    Gwynn, M.N.3    Knowles, D.J.C.4
  • 6
    • 0030897582 scopus 로고    scopus 로고
    • Simultaneous recognition of a carboxylate-containing ligand and an intramolecular surrogate ligand in the crystal structure of an asymmetric vancomycin dimer
    • Loll, P.J., Bevivino, A.E., Korty, B.D. & Axelsen, P.H. (1997). Simultaneous recognition of a carboxylate-containing ligand and an intramolecular surrogate ligand in the crystal structure of an asymmetric vancomycin dimer. J. Am. Chem. Soc. 119, 1516-1522.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1516-1522
    • Loll, P.J.1    Bevivino, A.E.2    Korty, B.D.3    Axelsen, P.H.4
  • 8
    • 0000868352 scopus 로고
    • The resistance of enterococci to glycopeptides
    • Courvalin, P. (1990). The resistance of enterococci to glycopeptides. Antimicrob. Agents Chemother. 38, 1675-1677.
    • (1990) Antimicrob. Agents Chemother. , vol.38 , pp. 1675-1677
    • Courvalin, P.1
  • 10
    • 0030036053 scopus 로고    scopus 로고
    • Binding of vancomycin group antibiotics to a cell wall analogue from vancomycin-resistant bacteria
    • Dancer, R.J., Try, A.C., Sharman, G.J. & Williams, D.H. (1996). Binding of vancomycin group antibiotics to a cell wall analogue from vancomycin-resistant bacteria. J. Chem. Soc. Chem. Commun. 1445-1446.
    • (1996) J. Chem. Soc. Chem. Commun. , pp. 1445-1446
    • Dancer, R.J.1    Try, A.C.2    Sharman, G.J.3    Williams, D.H.4
  • 11
    • 0030479181 scopus 로고    scopus 로고
    • Novel vancomycin dimers with activity against vancomycin-resistant enterococci
    • Sundram, U.N., Griffin, J.H. & Nicas, T.I. (1996). Novel vancomycin dimers with activity against vancomycin-resistant enterococci. J. Am. Chem. Soc. 118, 13107-13108.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 13107-13108
    • Sundram, U.N.1    Griffin, J.H.2    Nicas, T.I.3
  • 12
    • 0033150261 scopus 로고    scopus 로고
    • Binding of a dimeric derivative of vancomycin to L-Lys-D-Ala-D-lactate in solution and at a surface
    • Rao, J., Yan, L., Lahiri, J., Whitesides, G.M., Weis, R.M. & Warren, H.S. (1999). Binding of a dimeric derivative of vancomycin to L-Lys-D-Ala-D-lactate in solution and at a surface. Chem. Biol. 6, 353-359.
    • (1999) Chem. Biol. , vol.6 , pp. 353-359
    • Rao, J.1    Yan, L.2    Lahiri, J.3    Whitesides, G.M.4    Weis, R.M.5    Warren, H.S.6
  • 14
    • 0033599497 scopus 로고    scopus 로고
    • Using surface plasmon resonance to study the binding of vancomycin and its dimer to self-assembled monolayers presenting D-Ala-D-Ala
    • Rao, J., Yan, L., Xu, B. & Whitesides, G.M. (1999). Using surface plasmon resonance to study the binding of vancomycin and its dimer to self-assembled monolayers presenting D-Ala-D-Ala. J. Am. Chem. Soc. 121, 2629-2630.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2629-2630
    • Rao, J.1    Yan, L.2    Xu, B.3    Whitesides, G.M.4
  • 15
    • 0029872767 scopus 로고    scopus 로고
    • Cooperativity in ligand binding expressed at a model cell membrane by the vancomycin group antibiotics
    • Westwell, M.S., Bardsley, B., Try, A.C., Dancer, R.J. & Williams, D.H. (1996). Cooperativity in ligand binding expressed at a model cell membrane by the vancomycin group antibiotics. J. Chem. Soc. Chem. Commun., 589-590.
    • (1996) J. Chem. Soc. Chem. Commun. , pp. 589-590
    • Westwell, M.S.1    Bardsley, B.2    Try, A.C.3    Dancer, R.J.4    Williams, D.H.5
  • 16
    • 0027595323 scopus 로고
    • Protein-binding to supported lipid membranes: Investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance
    • Terrettaz, S., Stora, T., Duschl, C. & Vogel, H. (1993). Protein-binding to supported lipid membranes: Investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance. Langmuir 9, 1361-1369.
    • (1993) Langmuir , vol.9 , pp. 1361-1369
    • Terrettaz, S.1    Stora, T.2    Duschl, C.3    Vogel, H.4
  • 18
    • 0026153423 scopus 로고
    • Quantitative-determination of surface concentration of protein with surface-plasmon resonance using radio-labelled proteins
    • Stenberg, E., Persson, B., Roos, H. & Urbaniczky, C. (1991). Quantitative-determination of surface concentration of protein with surface-plasmon resonance using radio-labelled proteins. J. Colloid Interface Sci. 143, 513-526.
    • (1991) J. Colloid Interface Sci. , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 19
    • 0344241156 scopus 로고    scopus 로고
    • Supported hybrid bilayer membranes as rugged cell membrane mimics
    • Plant, A.L. (1999). Supported hybrid bilayer membranes as rugged cell membrane mimics. Langmuir 15, 5128-5135.
    • (1999) Langmuir , vol.15 , pp. 5128-5135
    • Plant, A.L.1
  • 21
  • 22
    • 0030929527 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of glycopeptide antibiotic activity at a model membrane surface
    • Cooper, M.A., Williams, D.H. & Cho, Y.R. (1997). Surface plasmon resonance analysis of glycopeptide antibiotic activity at a model membrane surface. J. Chem. Soc. Chem. Commun., 1625-1626.
    • (1997) J. Chem. Soc. Chem. Commun. , pp. 1625-1626
    • Cooper, M.A.1    Williams, D.H.2    Cho, Y.R.3
  • 23
    • 0033538325 scopus 로고    scopus 로고
    • High affinity surface binding of a strongly dimerising vancomycin-group antibiotic to a model of resistant bacteria
    • O'Brien, D.P., Entress, R.M.H, Cooper, M.A., O'Brien, S.W., Hopkinson, A. & Williams, D.H. (1999). High affinity surface binding of a strongly dimerising vancomycin-group antibiotic to a model of resistant bacteria. J. Am. Chem. Soc. 121, 5259-5265.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5259-5265
    • O'Brien, D.P.1    Entress, R.M.H.2    Cooper, M.A.3    O'Brien, S.W.4    Hopkinson, A.5    Williams, D.H.6
  • 24
    • 0032144280 scopus 로고    scopus 로고
    • Interpreting kinetic rate constants from optical biosensor data recorded on a decaying surface
    • Joss, L., Morton, T.A., Doyle, M.L. & Myska, D.G. (1998). Interpreting kinetic rate constants from optical biosensor data recorded on a decaying surface. Anal. Chem. 261, 203-210.
    • (1998) Anal. Chem. , vol.261 , pp. 203-210
    • Joss, L.1    Morton, T.A.2    Doyle, M.L.3    Myska, D.G.4
  • 25
    • 0342813129 scopus 로고    scopus 로고
    • Experimental design for the kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
    • Karlsson, R. & Falt, A. (1997). Experimental design for the kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200, 121-133.
    • (1997) J. Immunol. Methods , vol.200 , pp. 121-133
    • Karlsson, R.1    Falt, A.2
  • 26
    • 0030443164 scopus 로고    scopus 로고
    • The glycopeptide story - How to kill deadly super bugs
    • Williams, D.H. (1996). The glycopeptide story - How to kill deadly super bugs. Nat. Prod. Rep. 13, 469-477.
    • (1996) Nat. Prod. Rep. , vol.13 , pp. 469-477
    • Williams, D.H.1
  • 27
    • 0031595843 scopus 로고    scopus 로고
    • 19F NMR in the measurement of binding affinities of chloroeremomycin to model bacterial cell-wall surfaces which mimic VanA and VanB resistance
    • 19F NMR in the measurement of binding affinities of chloroeremomycin to model bacterial cell-wall surfaces which mimic VanA and VanB resistance. Chem. Biol. 5, 329-337.
    • (1998) Chem. Biol. , vol.5 , pp. 329-337
    • Entress, R.M.H.1    Dancer, R.J.2    O'Brien, D.P.3    Try, A.C.4    Cooper, M.A.5    Williams, D.H.6
  • 28
    • 0022346887 scopus 로고
    • The role of the chlorine substituents in the antibiotic vancomycin: Preparation and characterization of mono- and didechlorovancomycin
    • Harris, C.M., Kannan, R., Kopecka, H. & Harris, T.M. (1985). The role of the chlorine substituents in the antibiotic vancomycin: Preparation and characterization of mono- and didechlorovancomycin. J. Am. Chem. Soc. 107, 6652-6658.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6652-6658
    • Harris, C.M.1    Kannan, R.2    Kopecka, H.3    Harris, T.M.4
  • 29
    • 8944258105 scopus 로고    scopus 로고
    • Reductive alkylation of glycopeptide antibiotics: Synthesis and antibacterial activity
    • Cooper, R.D.G.S., et al., & Thompson, R.C. (1996). Reductive alkylation of glycopeptide antibiotics: Synthesis and antibacterial activity. J. Antibiot. 49, 575-581.
    • (1996) J. Antibiot. , vol.49 , pp. 575-581
    • Cooper, R.D.G.S.1    Thompson, R.C.2
  • 30
    • 0031576683 scopus 로고    scopus 로고
    • The roles of dimerisation and membrane anchoring in activity of glycopeptide antibiotics against vancomycin-resistant bacteria
    • Sharman, G.J., et al., & Williams, D.H. (1997). The roles of dimerisation and membrane anchoring in activity of glycopeptide antibiotics against vancomycin-resistant bacteria. J. Am. Chem. Soc. 119, 12041-12047.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12041-12047
    • Sharman, G.J.1    Williams, D.H.2
  • 31
    • 0030866228 scopus 로고    scopus 로고
    • Role of hydrophobic side chains as determinants of antibiotic activity of semi-synthetic glycopeptide antibiotics
    • Allen, N.E., LeTourneau, D.L. & Hobbs, J.N. (1997). Role of hydrophobic side chains as determinants of antibiotic activity of semi-synthetic glycopeptide antibiotics. J. Antibiot. 50, 677-684.
    • (1997) J. Antibiot. , vol.50 , pp. 677-684
    • Allen, N.E.1    LeTourneau, D.L.2    Hobbs, J.N.3
  • 33
    • 0033574743 scopus 로고    scopus 로고
    • Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala D-Ala
    • Ge, M., et al., & Kahne, D. (1999). Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala D-Ala. Science 284, 507-511.
    • (1999) Science , vol.284 , pp. 507-511
    • Ge, M.1    Kahne, D.2
  • 34
    • 0024355483 scopus 로고
    • Structure, biochemistry and mechanism of action of glycopeptide antibiotics
    • Reynolds, P.E. (1989). Structure, biochemistry and mechanism of action of glycopeptide antibiotics. Eur. J. Clin. Microbiol. Infect. Dis. 8, 943-950.
    • (1989) Eur. J. Clin. Microbiol. Infect. Dis. , vol.8 , pp. 943-950
    • Reynolds, P.E.1
  • 35
    • 0029797308 scopus 로고    scopus 로고
    • Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semisynthetic glycopeptide antibiotic
    • Allen, N.E., Hobbs, J.N. & Nicas, T.I. (1996). Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semisynthetic glycopeptide antibiotic. Antimicrob. Agents Chemother. 40, 2356-2362.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2356-2362
    • Allen, N.E.1    Hobbs, J.N.2    Nicas, T.I.3
  • 37
    • 0025093558 scopus 로고
    • Inhibition of peptidoglycan biosynthesis by ramoplanin
    • Somner, E.A. & Reynolds, P.E. (1990). Inhibition of peptidoglycan biosynthesis by ramoplanin. Antimicrob. Agents Chemother. 34, 413-419.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 413-419
    • Somner, E.A.1    Reynolds, P.E.2
  • 38
    • 0030717475 scopus 로고    scopus 로고
    • Semi-quantitation of cooperativity in binding of vancomycin- group antibiotics to vancomycin-susceptible and -resistant organisms
    • Beauregard, D.A., Maguire, A.J., Williams, D.H. & Reynolds, P.E. (1997). Semi-quantitation of cooperativity in binding of vancomycin- group antibiotics to vancomycin-susceptible and -resistant organisms. Antimicrob. Agents Chemother. 41, 2418-2423.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2418-2423
    • Beauregard, D.A.1    Maguire, A.J.2    Williams, D.H.3    Reynolds, P.E.4
  • 40
    • 3042988525 scopus 로고
    • Conformational analysis 130.MM2. A hydrocarbon force field utilizing V1 and V2 torsional terms
    • Allinger, M.L. (1977). Conformational analysis 130.MM2. A hydrocarbon force field utilizing V1 and V2 torsional terms. J. Am. Chem. Soc. 99, 8127.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 8127
    • Allinger, M.L.1
  • 41
    • 33748960249 scopus 로고    scopus 로고
    • Enthaplic contribution to the chelate effect: A correlation between ligand binding constant and a specific hydrogen bond strength in complexes of glycopeptide antibiotics with cell wall analogues
    • Searle, M.S., et al., & Williams, D.H. (1996). Enthaplic contribution to the chelate effect: A correlation between ligand binding constant and a specific hydrogen bond strength in complexes of glycopeptide antibiotics with cell wall analogues. J. Chem. Soc. Perkin Trans. 1, 2781-2786.
    • (1996) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2781-2786
    • Searle, M.S.1    Williams, D.H.2


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