메뉴 건너뛰기




Volumn 11, Issue 10, 2016, Pages 2693-2705

IDD388 Polyhalogenated Derivatives as Probes for an Improved Structure-Based Selectivity of AKR1B10 Inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; POLYHALO DERIVATIVE; AKR1B10 PROTEIN, HUMAN; HALOGEN; MOLECULAR PROBE;

EID: 84992188326     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00382     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 54549110136 scopus 로고    scopus 로고
    • The aldo-keto reductase superfamily and its role in drug metabolism and detoxification
    • Barski, O. A., Tipparaju, S. M., and Bhatnagar, A. (2008) The aldo-keto reductase superfamily and its role in drug metabolism and detoxification Drug Metab. Rev. 40, 553-624 10.1080/03602530802431439
    • (2008) Drug Metab. Rev. , vol.40 , pp. 553-624
    • Barski, O.A.1    Tipparaju, S.M.2    Bhatnagar, A.3
  • 3
    • 79957564846 scopus 로고    scopus 로고
    • Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde
    • Ruiz, F. X., Moro, A., Gallego, O., Ardèvol, A., Rovira, C., Petrash, J. M., Parés, X., and Farrés, J. (2011) Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde Chem.-Biol. Interact. 191, 199-205 10.1016/j.cbi.2011.02.007
    • (2011) Chem.-Biol. Interact. , vol.191 , pp. 199-205
    • Ruiz, F.X.1    Moro, A.2    Gallego, O.3    Ardèvol, A.4    Rovira, C.5    Petrash, J.M.6    Parés, X.7    Farrés, J.8
  • 5
    • 84887409478 scopus 로고    scopus 로고
    • Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111)
    • Zhang, L., Zhang, H., Zhao, Y., Li, Z., Chen, S., Zhai, J., Chen, Y., Xie, W., Wang, Z., Li, Q., Zheng, X., and Hu, X. (2013) Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111) FEBS Lett. 587, 3681-3686 10.1016/j.febslet.2013.09.031
    • (2013) FEBS Lett. , vol.587 , pp. 3681-3686
    • Zhang, L.1    Zhang, H.2    Zhao, Y.3    Li, Z.4    Chen, S.5    Zhai, J.6    Chen, Y.7    Xie, W.8    Wang, Z.9    Li, Q.10    Zheng, X.11    Hu, X.12
  • 6
    • 84898005162 scopus 로고    scopus 로고
    • Structural Basis for the Inhibition of AKR1B10 by Caffeic Acid Phenethyl Ester (CAPE)
    • Zhang, L., Zhang, H., Zheng, X., Zhao, Y., Chen, S., Chen, Y., Zhang, R., Li, Q., and Hu, X. (2014) Structural Basis for the Inhibition of AKR1B10 by Caffeic Acid Phenethyl Ester (CAPE) ChemMedChem 9, 706-709 10.1002/cmdc.201300455
    • (2014) ChemMedChem , vol.9 , pp. 706-709
    • Zhang, L.1    Zhang, H.2    Zheng, X.3    Zhao, Y.4    Chen, S.5    Chen, Y.6    Zhang, R.7    Li, Q.8    Hu, X.9
  • 9
    • 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 10.1021/jm100112j
    • (2010) J. Med. Chem. , vol.53 , pp. 5061-5084
    • Bissantz, C.1    Kuhn, B.2    Stahl, M.3
  • 10
  • 11
    • 80053555768 scopus 로고    scopus 로고
    • Strength and Character of Halogen Bonds in Protein-Ligand Complexes
    • Riley, K. E. and Hobza, P. (2011) Strength and Character of Halogen Bonds in Protein-Ligand Complexes Cryst. Growth Des. 11, 4272-4278 10.1021/cg200882f
    • (2011) Cryst. Growth Des. , vol.11 , pp. 4272-4278
    • Riley, K.E.1    Hobza, P.2
  • 12
    • 84874046410 scopus 로고    scopus 로고
    • Halogen bonding (X-bonding): A biological perspective
    • Scholfield, M. R., Zanden, C. M. V., Carter, M., and Ho, P. S. (2013) Halogen bonding (X-bonding): A biological perspective Protein Sci. 22, 139-152 10.1002/pro.2201
    • (2013) Protein Sci. , vol.22 , pp. 139-152
    • Scholfield, M.R.1    Zanden, C.M.V.2    Carter, M.3    Ho, P.S.4
  • 13
    • 84888630744 scopus 로고    scopus 로고
    • Halogen Interactions in Protein-Ligand Complexes: Implications of Halogen Bonding for Rational Drug Design
    • Sirimulla, S., Bailey, J. B., Vegesna, R., and Narayan, M. (2013) Halogen Interactions in Protein-Ligand Complexes: Implications of Halogen Bonding for Rational Drug Design J. Chem. Inf. Model. 53, 2781-2791 10.1021/ci400257k
    • (2013) J. Chem. Inf. Model. , vol.53 , pp. 2781-2791
    • Sirimulla, S.1    Bailey, J.B.2    Vegesna, R.3    Narayan, M.4
  • 16
    • 44349168793 scopus 로고    scopus 로고
    • Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features
    • Steuber, H., Heine, A., Podjarny, A., and Klebe, G. (2008) Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features J. Mol. Biol. 379, 991-1016 10.1016/j.jmb.2008.03.063
    • (2008) J. Mol. Biol. , vol.379 , pp. 991-1016
    • Steuber, H.1    Heine, A.2    Podjarny, A.3    Klebe, G.4
  • 18
    • 84875223602 scopus 로고    scopus 로고
    • X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP(+) and the potent aldose reductase inhibitor fidarestat: Implications for inhibitor binding and selectivity
    • Ruiz, F. X., Cousido-Siah, A., Mitschler, A., Farrés, J., Parés, X., and Podjarny, A. (2013) X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP(+) and the potent aldose reductase inhibitor fidarestat: Implications for inhibitor binding and selectivity Chem.-Biol. Interact. 202, 178-185 10.1016/j.cbi.2012.12.013
    • (2013) Chem.-Biol. Interact. , vol.202 , pp. 178-185
    • Ruiz, F.X.1    Cousido-Siah, A.2    Mitschler, A.3    Farrés, J.4    Parés, X.5    Podjarny, A.6
  • 20
    • 20544433165 scopus 로고
    • Van der Waals volumes + radii
    • Bondi, A. (1964) Van Der Waals volumes + radii J. Phys. Chem. 68, 441-451 10.1021/j100785a001
    • (1964) J. Phys. Chem. , vol.68 , pp. 441-451
    • Bondi, A.1
  • 21
    • 34247375160 scopus 로고    scopus 로고
    • Evidence for a novel binding site conformer of aldose reductase in ligand-bound state
    • Steuber, H., Zentgraf, M., La Motta, C., Sartini, S., Heine, A., and Klebe, G. (2007) Evidence for a novel binding site conformer of aldose reductase in ligand-bound state J. Mol. Biol. 369, 186-197 10.1016/j.jmb.2007.03.021
    • (2007) J. Mol. Biol. , vol.369 , pp. 186-197
    • Steuber, H.1    Zentgraf, M.2    La Motta, C.3    Sartini, S.4    Heine, A.5    Klebe, G.6
  • 23
    • 0031424157 scopus 로고    scopus 로고
    • The Alrestatin Double-Decker: Binding of Two Inhibitor Molecules to Human Aldose Reductase Reveals a New Specificity Determinant
    • Harrison, D. H. T., Bohren, K. M., Petsko, G. A., Ringe, D., and Gabbay, K. H. (1997) The Alrestatin Double-Decker: Binding of Two Inhibitor Molecules to Human Aldose Reductase Reveals a New Specificity Determinant Biochemistry 36, 16134-16140 10.1021/bi9717136
    • (1997) Biochemistry , vol.36 , pp. 16134-16140
    • Harrison, D.H.T.1    Bohren, K.M.2    Petsko, G.A.3    Ringe, D.4    Gabbay, K.H.5
  • 24
    • 33748758728 scopus 로고    scopus 로고
    • Expect the unexpected or caveat for drug designers: Multiple structure determinations using aldose reductase crystals treated under varying soaking and co-crystallisation conditions
    • Steuber, H., Zentgraf, M., Gerlach, C., Sotriffer, C. A., Heine, A., and Klebe, G. (2006) Expect the unexpected or caveat for drug designers: multiple structure determinations using aldose reductase crystals treated under varying soaking and co-crystallisation conditions J. Mol. Biol. 363, 174-187 10.1016/j.jmb.2006.08.011
    • (2006) J. Mol. Biol. , vol.363 , pp. 174-187
    • Steuber, H.1    Zentgraf, M.2    Gerlach, C.3    Sotriffer, C.A.4    Heine, A.5    Klebe, G.6
  • 25
    • 0031019986 scopus 로고    scopus 로고
    • Study of Non-Covalent Enzyme-Inhibitor Complexes of Aldose Reductase by Electrospray Mass Spectrometry
    • Potier, N., Barth, P., Tritsch, D., Biellmann, J.-F., and Van Dorsselaer, A. (1997) Study of Non-Covalent Enzyme-Inhibitor Complexes of Aldose Reductase by Electrospray Mass Spectrometry Eur. J. Biochem. 243, 274-282 10.1111/j.1432-1033.1997.0274a.x
    • (1997) Eur. J. Biochem. , vol.243 , pp. 274-282
    • Potier, N.1    Barth, P.2    Tritsch, D.3    Biellmann, J.-F.4    Van Dorsselaer, A.5
  • 26
    • 34447108978 scopus 로고    scopus 로고
    • Water, water everywhere - Except where it matters?
    • Homans, S. W. (2007) Water, water everywhere-except where it matters? Drug Discovery Today 12, 534-539 10.1016/j.drudis.2007.05.004
    • (2007) Drug Discovery Today , vol.12 , pp. 534-539
    • Homans, S.W.1
  • 27
    • 84857380650 scopus 로고    scopus 로고
    • Rational Approaches to Improving Selectivity in Drug Design
    • Huggins, D. J., Sherman, W., and Tidor, B. (2012) Rational Approaches to Improving Selectivity in Drug Design J. Med. Chem. 55, 1424-1444 10.1021/jm2010332
    • (2012) J. Med. Chem. , vol.55 , pp. 1424-1444
    • Huggins, D.J.1    Sherman, W.2    Tidor, B.3
  • 28
    • 84865132980 scopus 로고    scopus 로고
    • DoGSiteScorer: A web server for automatic binding site prediction, analysis and druggability assessment
    • Volkamer, A., Kuhn, D., Rippmann, F., and Rarey, M. (2012) DoGSiteScorer: a web server for automatic binding site prediction, analysis and druggability assessment Bioinformatics 28, 2074-2075 10.1093/bioinformatics/bts310
    • (2012) Bioinformatics , vol.28 , pp. 2074-2075
    • Volkamer, A.1    Kuhn, D.2    Rippmann, F.3    Rarey, M.4
  • 29
    • 45249123710 scopus 로고    scopus 로고
    • Exploring the Flap Pocket of the Antimalarial Target Plasmepsin II: The "55% Rule" Applied to Enzymes
    • Zürcher, M., Gottschalk, T., Meyer, S., Bur, D., and Diederich, F. (2008) Exploring the Flap Pocket of the Antimalarial Target Plasmepsin II: The "55% Rule" Applied to Enzymes ChemMedChem 3, 237-240 10.1002/cmdc.200700236
    • (2008) ChemMedChem , vol.3 , pp. 237-240
    • Zürcher, M.1    Gottschalk, T.2    Meyer, S.3    Bur, D.4    Diederich, F.5
  • 30
    • 40949163431 scopus 로고    scopus 로고
    • Role of the Active-Site Solvent in the Thermodynamics of Factor Xa Ligand Binding
    • Abel, R., Young, T., Farid, R., Berne, B. J., and Friesner, R. A. (2008) Role of the Active-Site Solvent in the Thermodynamics of Factor Xa Ligand Binding J. Am. Chem. Soc. 130, 2817-2831 10.1021/ja0771033
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2817-2831
    • Abel, R.1    Young, T.2    Farid, R.3    Berne, B.J.4    Friesner, R.A.5
  • 31
    • 84926158682 scopus 로고    scopus 로고
    • Applying thermodynamic profiling in lead finding and optimization
    • Klebe, G. (2015) Applying thermodynamic profiling in lead finding and optimization Nat. Rev. Drug Discovery 14, 95-110 10.1038/nrd4486
    • (2015) Nat. Rev. Drug Discovery , vol.14 , pp. 95-110
    • Klebe, G.1
  • 32
    • 84859169880 scopus 로고    scopus 로고
    • Drug development: Raise standards for preclinical cancer research
    • Begley, C. G. and Ellis, L. M. (2012) Drug development: Raise standards for preclinical cancer research Nature 483, 531-533 10.1038/483531a
    • (2012) Nature , vol.483 , pp. 531-533
    • Begley, C.G.1    Ellis, L.M.2
  • 33
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague, S. J. (2003) Implications of protein flexibility for drug discovery Nat. Rev. Drug Discovery 2, 527-541 10.1038/nrd1129
    • (2003) Nat. Rev. Drug Discovery , vol.2 , pp. 527-541
    • Teague, S.J.1
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 70349597601 scopus 로고    scopus 로고
    • Electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation
    • Moriarty, N. W., Grosse-Kunstleve, R. W., and Adams, P. D. (2009) electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation Acta Crystallogr., Sect. D: Biol. Crystallogr. 65, 1074-1080 10.1107/S0907444909029436
    • (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 45
    • 3042524904 scopus 로고
    • A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges - The Resp Model
    • Bayly, C. I., Cieplak, P., Cornell, W. D., and Kollman, P. A. (1993) A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges-the Resp Model J. Phys. Chem. 97, 10269-10280 10.1021/j100142a004
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 46
    • 84961980743 scopus 로고
    • COSMO: A new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • Klamt, A. and Schuurmann, G. (1993) COSMO: a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient J. Chem. Soc., Perkin Trans. 2 799-805 10.1039/P29930000799
    • (1993) J. Chem. Soc., Perkin Trans. 2 , pp. 799-805
    • Klamt, A.1    Schuurmann, G.2
  • 47
    • 84878077947 scopus 로고    scopus 로고
    • Assessing the Accuracy and Performance of Implicit Solvent Models for Drug Molecules: Conformational Ensemble Approaches
    • Kolář, M., Fanfrlík, J., Lepšík, M., Forti, F., Luque, F. J., and Hobza, P. (2013) Assessing the Accuracy and Performance of Implicit Solvent Models for Drug Molecules: Conformational Ensemble Approaches J. Phys. Chem. B 117, 5950-5962 10.1021/jp402117c
    • (2013) J. Phys. Chem. B , vol.117 , pp. 5950-5962
    • Kolář, M.1    Fanfrlík, J.2    Lepšík, M.3    Forti, F.4    Luque, F.J.5    Hobza, P.6
  • 48
    • 84976209197 scopus 로고    scopus 로고
    • Cuby: An integrative framework for computational chemistry
    • Řezáč, J. (2016) Cuby: An integrative framework for computational chemistry J. Comput. Chem. 37, 1230 10.1002/jcc.24312
    • (2016) J. Comput. Chem. , vol.37 , pp. 1230
    • Řezáč, J.1
  • 49
    • 84865676787 scopus 로고    scopus 로고
    • Combined QM/MM (ONIOM) and QSAR Approach to the Study of Complex Formation of Matrix Metalloproteinase-9 with a Series of Biphenylsulfonamides - LERE-QSAR Analysis (V)
    • Yoshida, T., Hitaoka, S., Mashima, A., Sugimoto, T., Matoba, H., and Chuman, H. (2012) Combined QM/MM (ONIOM) and QSAR Approach to the Study of Complex Formation of Matrix Metalloproteinase-9 with a Series of Biphenylsulfonamides-LERE-QSAR Analysis (V) J. Phys. Chem. B 116, 10283-10289 10.1021/jp305476x
    • (2012) J. Phys. Chem. B , vol.116 , pp. 10283-10289
    • Yoshida, T.1    Hitaoka, S.2    Mashima, A.3    Sugimoto, T.4    Matoba, H.5    Chuman, H.6
  • 50
    • 77951680464 scopus 로고    scopus 로고
    • A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu
    • Grimme, S., Antony, J., Ehrlich, S., and Krieg, H. (2010) A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu J. Chem. Phys. 132, 154104 10.1063/1.3382344
    • (2010) J. Chem. Phys. , vol.132 , pp. 154104
    • Grimme, S.1    Antony, J.2    Ehrlich, S.3    Krieg, H.4
  • 51
    • 33846595224 scopus 로고    scopus 로고
    • Density functional theory augmented with an empirical dispersion term. Interaction energies and geometries of 80 noncovalent complexes compared with ab initio quantum mechanics calculations
    • Jurečka, P., Černý, J., Hobza, P., and Salahub, D. R. (2007) Density functional theory augmented with an empirical dispersion term. Interaction energies and geometries of 80 noncovalent complexes compared with ab initio quantum mechanics calculations J. Comput. Chem. 28, 555-569 10.1002/jcc.20570
    • (2007) J. Comput. Chem. , vol.28 , pp. 555-569
    • Jurečka, P.1    Černý, J.2    Hobza, P.3    Salahub, D.R.4
  • 52
    • 4243539377 scopus 로고
    • Electronic structure calculations on workstation computers: The program system turbomole
    • Ahlrichs, R., Bär, M., Häser, M., Horn, H., and Kölmel, C. (1989) Electronic structure calculations on workstation computers: The program system turbomole Chem. Phys. Lett. 162, 165-169 10.1016/0009-2614(89)85118-8
    • (1989) Chem. Phys. Lett. , vol.162 , pp. 165-169
    • Ahlrichs, R.1    Bär, M.2    Häser, M.3    Horn, H.4    Kölmel, C.5
  • 53
    • 67849101722 scopus 로고    scopus 로고
    • Semiempirical Quantum Chemical PM6Method Augmented by Dispersion and H-Bonding Correction Terms Reliably Describes Various Types of Noncovalent Complexes
    • Řezáč, J., Fanfrlík, J., Salahub, D., and Hobza, P. (2009) Semiempirical Quantum Chemical PM6Method Augmented by Dispersion and H-Bonding Correction Terms Reliably Describes Various Types of Noncovalent Complexes J. Chem. Theory Comput. 5, 1749-1760 10.1021/ct9000922
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 1749-1760
    • Řezáč, J.1    Fanfrlík, J.2    Salahub, D.3    Hobza, P.4
  • 54
    • 84855668199 scopus 로고    scopus 로고
    • Advanced Corrections of Hydrogen Bonding and Dispersion for Semiempirical Quantum Mechanical Methods
    • Řezáč, J. and Hobza, P. (2012) Advanced Corrections of Hydrogen Bonding and Dispersion for Semiempirical Quantum Mechanical Methods J. Chem. Theory Comput. 8, 141-151 10.1021/ct200751e
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 141-151
    • Řezáč, J.1    Hobza, P.2
  • 55
    • 35448937584 scopus 로고    scopus 로고
    • Optimization of parameters for semiempirical methods V: Modification of NDDO approximations and application to 70 elements
    • Stewart, J. P. (2007) Optimization of parameters for semiempirical methods V: Modification of NDDO approximations and application to 70 elements J. Mol. Model. 13, 1173-1213 10.1007/s00894-007-0233-4
    • (2007) J. Mol. Model. , vol.13 , pp. 1173-1213
    • Stewart, J.P.1
  • 56
    • 2542462121 scopus 로고    scopus 로고
    • Optimization of parameters for semiempirical methods IV: Extension of MNDO, AM1, and PM3 to more main group elements
    • Stewart, J. P. (2004) Optimization of parameters for semiempirical methods IV: extension of MNDO, AM1, and PM3 to more main group elements J. Mol. Model. 10, 155-164 10.1007/s00894-004-0183-z
    • (2004) J. Mol. Model. , vol.10 , pp. 155-164
    • Stewart, J.P.1
  • 57
    • 77957291978 scopus 로고    scopus 로고
    • A Reliable Docking/Scoring Scheme Based on the Semiempirical Quantum Mechanical PM6-DH2Method Accurately Covering Dispersion and H-Bonding: HIV-1 Protease with 22 Ligands
    • Fanfrlík, J., Bronowska, A. K., Řezáč, J., Přenosil, O., Konvalinka, J., and Hobza, P. (2010) A Reliable Docking/Scoring Scheme Based on the Semiempirical Quantum Mechanical PM6-DH2Method Accurately Covering Dispersion and H-Bonding: HIV-1 Protease with 22 Ligands J. Phys. Chem. B 114, 12666-12678 10.1021/jp1032965
    • (2010) J. Phys. Chem. B , vol.114 , pp. 12666-12678
    • Fanfrlík, J.1    Bronowska, A.K.2    Řezáč, J.3    Přenosil, O.4    Konvalinka, J.5    Hobza, P.6
  • 58
    • 84883853834 scopus 로고    scopus 로고
    • The Semiempirical Quantum Mechanical Scoring Function for in Silico Drug Design
    • Lepšík, M., Řezáč, J., Kolář, M., Pecina, A., Hobza, P., and Fanfrlík, J. (2013) The Semiempirical Quantum Mechanical Scoring Function for In Silico Drug Design ChemPlusChem 78, 921-931 10.1002/cplu.201300199
    • (2013) ChemPlusChem , vol.78 , pp. 921-931
    • Lepšík, M.1    Řezáč, J.2    Kolář, M.3    Pecina, A.4    Hobza, P.5    Fanfrlík, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.