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Volumn 8, Issue 12, 2013, Pages 2794-2801

Biochemical and biophysical analysis of a chiral PqsD inhibitor revealing tight-binding behavior and enantiomers with contrary thermodynamic signatures

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; HYDROXYL GROUP; PQSD INHIBITOR; UNCLASSIFIED DRUG;

EID: 84890852916     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400530d     Document Type: Article
Times cited : (24)

References (30)
  • 1
    • 10944272743 scopus 로고    scopus 로고
    • Antibacterial resistance worldwide: Causes, challenges and responses
    • Levy, S. B. and Marshall, B. (2004) Antibacterial resistance worldwide: Causes, challenges and responses Nat. Med. 10, S122-S129
    • (2004) Nat. Med. , vol.10
    • Levy, S.B.1    Marshall, B.2
  • 2
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan, J. R. and Deretic, V. (1996) Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia Microbiol. Rev. 60, 539-574
    • (1996) Microbiol. Rev. , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 3
    • 0024467106 scopus 로고
    • Outer membrane barrier as a mechanism of antimicrobial resistance
    • Nikaido, H. (1989) Outer membrane barrier as a mechanism of antimicrobial resistance Antimicrob. Agents Chemother. 33, 1831-1836
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1831-1836
    • Nikaido, H.1
  • 4
    • 0035087832 scopus 로고    scopus 로고
    • Multidrug efflux pumps and antimicrobial resistance in Pseudomonas aeruginosa and related organisms
    • Poole, K. (2001) Multidrug efflux pumps and antimicrobial resistance in Pseudomonas aeruginosa and related organisms J. Mol. Microbiol. Biotechnol. 3, 255-264
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 255-264
    • Poole, K.1
  • 5
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • Swinney, D. C. (2004) Biochemical mechanisms of drug action: What does it take for success? Nat. Rev. Drug Discovery 3, 801-808
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 801-808
    • Swinney, D.C.1
  • 6
    • 33746257392 scopus 로고    scopus 로고
    • Functional genetic analysis reveals a 2-alkyl-4-quinolone signaling system in the human pathogen Burkholderia pseudomallei and related bacteria
    • Diggle, S. P., Lumjiaktase, P., Dipilato, F., Kunakorn, M., Barrett, D. A., Chhabra, S. R., Camara, M., and Williams, P. (2006) Functional genetic analysis reveals a 2-alkyl-4-quinolone signaling system in the human pathogen Burkholderia pseudomallei and related bacteria Chem. Biol. 13, 701-710
    • (2006) Chem. Biol. , vol.13 , pp. 701-710
    • Diggle, S.P.1    Lumjiaktase, P.2    Dipilato, F.3    Kunakorn, M.4    Barrett, D.A.5    Chhabra, S.R.6    Camara, M.7    Williams, P.8
  • 7
    • 72049127267 scopus 로고    scopus 로고
    • Pyoverdine and PQS mediated subpopulation interactions involved in Pseudomonas aeurginsoa biofilm formation
    • Yang, L., Nilsson, M., Gjermansen, M., Givskov, M., and Tolker-Nielsen, T. (2009) Pyoverdine and PQS mediated subpopulation interactions involved in Pseudomonas aeurginsoa biofilm formation Mol. Microbiol. 74, 1380-1392
    • (2009) Mol. Microbiol. , vol.74 , pp. 1380-1392
    • Yang, L.1    Nilsson, M.2    Gjermansen, M.3    Givskov, M.4    Tolker-Nielsen, T.5
  • 8
    • 49849090152 scopus 로고    scopus 로고
    • Quorum sensing by 2-alkyl-4-quinolones in Pseudomonas aeruginsoa and other bacterial species
    • Summarized
    • Summarized in: Dubern, J.-F. and Diggle, S. P. (2008) Quorum sensing by 2-alkyl-4-quinolones in Pseudomonas aeruginsoa and other bacterial species Mol. BioSyst 4, 882-888
    • (2008) Mol. BioSyst , vol.4 , pp. 882-888
    • Dubern, J.-F.1    Diggle, S.P.2
  • 10
    • 79953716518 scopus 로고    scopus 로고
    • Biosynthesis of 2-alkyl-4(1 H)-quinolones in Pseudomonas aeruginosa: Potential for therapeutic interference with pathogenicity
    • Pistorius, D., Ullrich, A., Lucas, S., Hartmann, R. W., Kazmaier, U., and Müller, R. (2011) Biosynthesis of 2-alkyl-4(1 H)-quinolones in Pseudomonas aeruginosa: Potential for therapeutic interference with pathogenicity ChemBioChem 12, 850-853
    • (2011) ChemBioChem , vol.12 , pp. 850-853
    • Pistorius, D.1    Ullrich, A.2    Lucas, S.3    Hartmann, R.W.4    Kazmaier, U.5    Müller, R.6
  • 12
    • 84881408976 scopus 로고    scopus 로고
    • Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking
    • press
    • Weidel, E., de Jong, J. C., Brengel, C., Storz, M. P., Braunshausen, A., Negri, M., Plaza, A., Steinbach, A., Müller, R., and Hartmann, R. W. Structure optimization of 2-benzamidobenzoic acids as PqsD inhibitors for Pseudomonas aeruginosa infections and elucidation of binding mode by SPR, STD NMR, and molecular docking. J. Med. Chem. 2013, in press
    • (2013) J. Med. Chem.
    • Weidel, E.1    De Jong, J.C.2    Brengel, C.3    Storz, M.P.4    Braunshausen, A.5    Negri, M.6    Plaza, A.7    Steinbach, A.8    Müller, R.9    Hartmann, R.W.10
  • 13
    • 33845280171 scopus 로고
    • Significance of slow-binding enzyme inhibition and its relationship to reaction-intermediate analogues
    • Schloss, J. V. (1988) Significance of slow-binding enzyme inhibition and its relationship to reaction-intermediate analogues Acc. Chem. Res. 21, 348-353
    • (1988) Acc. Chem. Res. , vol.21 , pp. 348-353
    • Schloss, J.V.1
  • 14
    • 70149087320 scopus 로고    scopus 로고
    • Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate
    • Bera, A. K., Atanasova, V., Robinson, H., Eisenstein, E., Coleman, J. P., Pesci, E. C., and Parsons, J. F. (2009) Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate Biochemistry 48, 8644-8655
    • (2009) Biochemistry , vol.48 , pp. 8644-8655
    • Bera, A.K.1    Atanasova, V.2    Robinson, H.3    Eisenstein, E.4    Coleman, J.P.5    Pesci, E.C.6    Parsons, J.F.7
  • 15
    • 33645926045 scopus 로고    scopus 로고
    • Enantioselective rhodium-catalyzed addition of arylboronic acids to aldehydes using chiral spiro monophosphite ligands
    • Duan, H.-F., Xie, J.-H., Shi, W.-J., Zhang, Q., and Zhou, Q.-L. (2006) Enantioselective rhodium-catalyzed addition of arylboronic acids to aldehydes using chiral spiro monophosphite ligands Org. Lett. 8, 1479-1481
    • (2006) Org. Lett. , vol.8 , pp. 1479-1481
    • Duan, H.-F.1    Xie, J.-H.2    Shi, W.-J.3    Zhang, Q.4    Zhou, Q.-L.5
  • 17
    • 33746885488 scopus 로고    scopus 로고
    • Probing hot spots at protein-ligand binding sites: A fragment-based approach using biophysical methods
    • Ciulli, A., Williams, G., Smith, A. G., Blundell, T. L., and Abell, C. (2006) Probing hot spots at protein-ligand binding sites: A fragment-based approach using biophysical methods J. Med. Chem. 49, 4992-5000
    • (2006) J. Med. Chem. , vol.49 , pp. 4992-5000
    • Ciulli, A.1    Williams, G.2    Smith, A.G.3    Blundell, T.L.4    Abell, C.5
  • 18
    • 0000872589 scopus 로고    scopus 로고
    • Hydrogen-bond acceptor properties of nitro-O atoms: A combined crystallographic database and ab initio molecular orbital study
    • Allen, F. H., Baalham, C. A., Lommerse, J. P. M., Raithby, P. R., and Sparr, E. (1997) Hydrogen-bond acceptor properties of nitro-O atoms: A combined crystallographic database and ab initio molecular orbital study Acta Crystallogr. B53, 1017-1024
    • (1997) Acta Crystallogr. , vol.53 , pp. 1017-1024
    • Allen, F.H.1    Baalham, C.A.2    Lommerse, J.P.M.3    Raithby, P.R.4    Sparr, E.5
  • 19
    • 0000651746 scopus 로고    scopus 로고
    • Hydrogen-bond acceptor and donor properties of divalent sulfur (Y-S-Z and R-S-H)
    • Allen, F. H., Bird, C. M., Rowland, R. X., and Raithby, P. R. (1997) Hydrogen-bond acceptor and donor properties of divalent sulfur (Y-S-Z and R-S-H) Acta Crystallogr. B53, 696-701
    • (1997) Acta Crystallogr. , vol.53 , pp. 696-701
    • Allen, F.H.1    Bird, C.M.2    Rowland, R.X.3    Raithby, P.R.4
  • 20
    • 9644307952 scopus 로고    scopus 로고
    • Hydrogen bonding in complex of serine with histidine: Computational and spectroscopic study of model compounds
    • Vianello, L., Kovačević, B., Ambrožič, G., Mavri, J., and Maksić, Z. B. (2004) Hydrogen bonding in complex of serine with histidine: Computational and spectroscopic study of model compounds Chem. Phys. Lett. 400, 117-121
    • (2004) Chem. Phys. Lett. , vol.400 , pp. 117-121
    • Vianello, L.1    Kovačević, B.2    Ambrožič, G.3    Mavri, J.4    Maksić, Z.B.5
  • 21
    • 20544433165 scopus 로고
    • Van der Waals volumes and radii
    • Bondi, A. (1964) Van der Waals volumes and radii J. Phys. Chem. 68, 441-451
    • (1964) J. Phys. Chem. , vol.68 , pp. 441-451
    • Bondi, A.1
  • 22
    • 84871027166 scopus 로고    scopus 로고
    • Similar but different: Thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase
    • Berg, L., Niemiec, M. S., Qian, W., Andersson, C. D., Wittung-Stafshede, P., Ekström, F., and Linusson, A. (2012) Similar but different: Thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase Angew. Chem., Int. Ed. 51, 12716-12720
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 12716-12720
    • Berg, L.1    Niemiec, M.S.2    Qian, W.3    Andersson, C.D.4    Wittung-Stafshede, P.5    Ekström, F.6    Linusson, A.7
  • 23
    • 0017884417 scopus 로고
    • The hydrophobic effect and the organization of living matter
    • Tanford, C. (1978) The hydrophobic effect and the organization of living matter Science 200, 1012-1018
    • (1978) Science , vol.200 , pp. 1012-1018
    • Tanford, C.1
  • 24
    • 84863812540 scopus 로고    scopus 로고
    • Ligand binding stepwise disrupts water network in thrombin: Enthalpic and entropic changes reveal classical hydrophobic effect
    • Biela, A., Sielaff, F., Terwesten, F., Heine, A., Steinmetzer, T., and Klebe, F. (2012) Ligand binding stepwise disrupts water network in thrombin: Enthalpic and entropic changes reveal classical hydrophobic effect J. Med. Chem. 55, 6094-6110
    • (2012) J. Med. Chem. , vol.55 , pp. 6094-6110
    • Biela, A.1    Sielaff, F.2    Terwesten, F.3    Heine, A.4    Steinmetzer, T.5    Klebe, F.6
  • 25
    • 77953631827 scopus 로고    scopus 로고
    • A medicinal chemist's guide to molecular interactions
    • Bissantz, C., Kuhn, B., and Stahl, M. (2010) A medicinal chemist's guide to molecular interactions J. Med. Chem. 53, 5061-5084
    • (2010) J. Med. Chem. , vol.53 , pp. 5061-5084
    • Bissantz, C.1    Kuhn, B.2    Stahl, M.3
  • 26
    • 84877768087 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Role and ramifications in biomolecular ligand recognition and design
    • Chodera, J. D. and Mobley, D. L. (2013) Entropy-enthalpy compensation: Role and ramifications in biomolecular ligand recognition and design Annu. Rev. Biophys. 42, 121-142
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 121-142
    • Chodera, J.D.1    Mobley, D.L.2
  • 27
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA - A self-parameterizing force field
    • Krieger, E., Koraimann, G., and Virend, G. (2002) Increasing the precision of comparative models with YASARA NOVA-A self-parameterizing force field Proteins 47, 393-402
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Virend, G.3
  • 28
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan, Y., Wu, C., Chowdhury, S., Lee, M. C., Xiong, G., Zhang, W., Yang, R., Cieplak, P., Luo, R., and Lee, R. (2003) A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations J. Comput. Chem. 24, 1999-2012
    • (2003) J. Comput. Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, R.10
  • 29
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Hallliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function J. Comput. Chem. 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Hallliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 30
    • 84855757480 scopus 로고    scopus 로고
    • 2012.10; (), H3A 2R7, Chemical Computing Group Inc. Montreal, QC, Canada
    • Molecular Operating Environment (MOE), 2012.10; (2012), H3A 2R7, Chemical Computing Group Inc., Montreal, QC, Canada.
    • (2012) Molecular Operating Environment (MOE)


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