Structure-guided design of novel thiazolidine inhibitors of O -Acetyl serine sulfhydrylase from mycobacterium tuberculosis

Journal of Medicinal Chemistry

Volumn 56, Issue 16, 2013, Pages 6457-6466

  Poyraz, Ömer ^a   Jeankumar, Variam Ullas ^b   Saxena, Shalini ^b   Schnell, Robert ^a   Haraldsson, Martin ^a   Yogeeswari, Perumal ^b   Sriram, Dharmarajan ^b   Schneider, Gunter ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b BIRLA INSTITUTE OF TECHNOLOGY AND SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

3 [[5 (2 METHOXYBENZYLIDENE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (3,4 DIMETHOXYBENZYLIDENE) 3 ETHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (3,4 DIMETHOXYBENZYLIDENE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (3,4,5 TRIMETHOXYBENZYLIDENE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 FLUOROBENZYLIDENE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 HYDROXY 3 METHOXYBENZYLIDENE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 HYDROXYBENZYLIDENE) 3 ALLYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 HYDROXYBENZYLIDENE) 3 ETHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 HYDROXYBENZYLIDENE) 3 ISOPROPYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 HYDROXYBENZYLIDENE) 3 PROPYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 HYDROXYBENZYLIDINE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 (4 METHOXYBENZYLIDENE) 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 [4 (BENZYLOXY)BENZYLIDENE] 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; 3 [[5 [4 (DIMETHYLAMINO)BENZYLIDENE] 3 METHYL 4 OXOTHIAZOLIDIN 2 YLIDENE]AMINO]BENZOIC ACID; ANTIINFECTIVE AGENT; BACTERIAL ENZYME; CYSTEINE; HYDROGEN SULFIDE; O ACETYL SERINE SULFHYDRYLASE; PYRIDOXAL 5 PHOSPHATE; THIAZOLIDINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DRUG DESIGN; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG SCREENING; DRUG STRUCTURE; DRUG SYNTHESIS; DRUG TARGETING; ENZYME INHIBITION; IC 50; IN VITRO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHARMACOPHORE; STRUCTURE ACTIVITY RELATION;

CYSTEINE SYNTHASE; DRUG DESIGN; ENZYME INHIBITORS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MYCOBACTERIUM TUBERCULOSIS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 84883167771     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400710k     Document Type: Article

References (31)

1. Dye, C.; Williams, B. G. The Population Dynamics and Control of Tuberculosis Science 2010, 328, 856-861
2. Koul, A.; Arnoult, E.; Lounis, N.; Guillemont, J.; Andries, K. The challenge of new drug discovery for tuberculosis Nature 2011, 469, 483-490
3. Gengenbacher, M.; Kaufmann, S. H. E. Mycobacterium tuberculosis: success through dormancy FEMS Microbiol. Rev. 2012, 36, 514-532
4. Ehrt, S.; Schnappinger, D. Mycobacterial survival strategies in the phagosome: defence against host stresses Cell. Microbiol. 2009, 11, 1170-1178
5. Jothivasan, V. K.; Hamilton, C. J. Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular molecular weight thiol in actinomycetes Nat. Prod. Rep. 2008, 25, 1091-1117
6. Hampshire, T.; Soneji, S.; Bacon, J.; James, B. W.; Hinds, J.; Laing, K.; Stabler, R. A.; Marsh, P. D.; Butcher, P. D. Stationary phase gene expression of Mycobacterium tuberculosis following a progressive nutrient depletion: a model for persistent organisms Tuberculosis 2004, 84, 228-238
7. Betts, J. C.; Lukey, P. T.; Robb, L. C.; McAdam, R. A.; Duncan, K. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling Mol. Microbiol. 2002, 43, 717-731
8. Voskuil, M. I.; Visconti, K. C.; Schoolnik, G. K. Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy Tuberculosis 2004, 84, 218-227
9. Schnappinger, D.; Ehrt, S.; Voskuil, M. I.; Liu, Y.; Mangan, J. A.; Monahan, I. M.; Dolganov, G.; Efron, B.; Butcher, P. D.; Nathan, C.; Schoolnik, G. K. Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: Insights into the phagosomal environment J. Exp. Med. 2003, 198, 693-704
10. Bhave, D. P.; Muse, W. B., III; Carroll, K. S. Drug targets in mycobacterial sulfur metabolism Infect. Disord. Drug Targets 2007, 7, 140-158
11. Hatzios, S. K.; Bertozzi, C. R. The Regulation of Sulfur Metabolism in Mycobacterium tuberculosis PLoS Pathogens 2011, 7, e1002036 10.1371/journal. ppat.1002036
12. Schnell, R.; Oehlmann, W.; Singh, M.; Schneider, G. Structural insights into catalysis and inhibition of O -acetylserine sulfhydrylase from Mycobacterium tuberculosis-crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex J. Biol. Chem. 2007, 282, 23473-23481
13. Kumar, V. U. J.; Poyraz, O.; Saxena, S.; Schnell, R.; Yogeeswari, P.; Schneider, G.; Sriram, D. Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O -acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening Bioorg. Med. Chem. Lett. 2013, 23, 1182-1186
14. Friesner, R. A.; Murphy, R. B.; Repasky, M. P.; Frye, L. L.; Greenwood, J. R.; Halgren, T. A.; Sanschagrin, P. C.; Mainz, D. T. Extra Precision Glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes J. Med. Chem. 2006, 49, 6177-6196
15. Friesner, R. A.; Banks, J. L.; Murphy, R. B.; Halgren, T. A.; Klicic, J. J.; Mainz, D. T.; Repasky, M. P.; Knoll, E. H.; Shelley, M.; Perry, J. K.; Shaw, D. E.; Francis, P.; Shenkin, P. S. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy J. Med. Chem. 2004, 47, 1739-1749
16. Eldridge, M. D.; Murray, C. W.; Auton, T. R.; Paolini, G. V.; Mee, R. P. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes J. Comput.-Aided. Mol. Des. 1997, 11, 425-445
17. Dayam, R.; Aiello, F.; Deng, J.; Wu, Y.; Garofalo, A.; Chen, X.; Neamati, N. Discovery of Small Molecule Integrin αVβ3 Antagonists as Novel Anticancer Agents J. Med. Chem. 2006, 49, 4526-4534
18. Vicini, P.; Geronikaki, A.; Incerti, M.; Zani, F.; Dearden, J.; Hewittc, M. 2-Heteroarylimino-5-benzylidene-4-thiazolidinones analogues of 2-thiazolylimino-5-benzylidene-4-thiazolidinones with antimicrobial activity: synthesis and structure-activity relationship Bioorg. Med. Chem. 2008, 16, 3714-3724
19. Verma, A.; Saraf, K. S. 4-Thiazolidinone A biologically active scaffold Eur. J. Med. Chem. 2008, 43, 897-905
20. Jain, K. A.; Vaidya, A.; Ravichandran, V.; Kashaw, S. K.; Agrawal, K. R. Recent developments and biological activities of thiazolidinone derivatives: A review Bioorg. Med. Chem. 2012, 20, 3378-3395
21. Maccari, R.; Ottana, R.; Curinga, C.; Vigorita, M. G.; Rakowitz, D.; Steindlb, T.; Langer, T. Structure-activity relationships and molecular modelling of 5-arylidene-2,4-thiazolidinediones active as aldose reductase inhibitors Bioorg. Med. Chem. 2005, 13, 2809-2823
22. Kosma, P.; Selzer, E.; Mereiter, K. 4-({(Z)-5-[(Z)-3-Ethoxy-4- hydroxybenzylidene]-3-methyl-4-oxo-1,3-thiazolidin-2-ylidene}amino)benzoic acid dimethylformamide monosolvate Acta Crystallogr., Sect. E: Struct. Rep. Online 2012, E68, o3417-o3418
23. Huang, B.; Vetting, M. W.; Roderick, S. L. The active site of O -acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase J. Bacteriol. 2005, 187, 3201-3205
24. Francois, J. A.; Kumaran, S.; Jez, J. M. Structural basis for interaction of O -acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex Plant Cell 2006, 18, 3647-3655
25. Salsi, E.; Bayden, A. S.; Spyrakis, F.; Amadasi, A.; Campanini, B.; Bettati, S.; Dodatko, T.; Cozzini, P.; Kellogg, G. E.; Cook, P. F.; Roderick, S. L.; Mozzarelli, A. Design of O -acetylserine sulfhydrylase inhibitors by mimicking nature J. Med. Chem. 2010, 53, 345-356
26. Campanini, B.; Speroni, F.; Salsi, E.; Cook, P. F.; Roderick, S. L.; Huang, B.; Bettati, S.; Mozzarelli, A. Interaction of serine acetyltransferase with O -acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy Protein Sci. 2005, 14, 2115-2124
27. Spyrakis, F.; Felici, P.; Bayden, A. S.; Salsi, E.; Miggiano, R.; Kellogg, G. E.; Cozzini, P.; Cook, P. F.; Mozzarelli, A.; Campanini, B. Fine tuning of the active site modulates specificity in the interaction of O -acetylserine sulfhydrylase isozymes with serine acetyltransferase Biochim. Biophys. Acta 2013, 1834, 169-181
28. Nagpal, I.; Raj, I.; Subbarao, N.; Gourinath, S. Virtual screening, identification and in vitro testing of novel inhibitors of O -acetyl- l -serine sulfhydrylase of Entamoeba histolytica PLoS One 2012, 7, e30305 10.1371/journal.pone.0030305
29. Amori, L.; Katkevica, S.; Bruno, A.; Campanini, B.; Fekici, P.; Moxxareilli, A.; Costantino, G. Design and synthesis of trans-2-substituted- cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O -acetylserine sulfhydrylase Med. Chem. Commun. 2012, 3, 1111-1116
30. Gaitonde, M. K. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids Biochem. J. 1967, 104, 627-633
31. Wu, G.; Yuan, Y.; Hodge, C. N. Determining appropriate substrate conversion for enzymatic assays in high-throughput screening J. Biomol. Screening 2003, 8, 694-700