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The Scientific World Journal
Volume 2014, Article ID 703053, 6 pages
http://dx.doi.org/10.1155/2014/703053
Research Article

Salicylanilide Diethyl Phosphates as Potential Inhibitors of Some Mycobacterial Enzymes

1Department of Inorganic and Organic Chemistry, Faculty of Pharmacy, Charles University in Prague, Heyrovského 1203, 500 05 Hradec Králové, Czech Republic
2Department of Biochemical Sciences, Faculty of Pharmacy, Charles University in Prague, Heyrovského 1203, 500 05 Hradec Králové, Czech Republic
3Medicinal Chemistry Research Laboratory, Pharmacy Group, Birla Institute of Technology and Science, Hyderabad 500078, India

Received 24 July 2014; Accepted 26 September 2014; Published 4 November 2014

Academic Editor: Andrei Surguchov

Copyright © 2014 Martin Krátký et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. Saifullah, P. Arulselvan, M. E. El Zowalaty et al., “Development of a highly biocompatible antituberculosis nanodelivery formulation based on para-aminosalicylic acid—zinc layered hydroxide nanocomposites,” The Scientific World Journal, vol. 2014, Article ID 401460, 12 pages, 2014. View at Publisher · View at Google Scholar
  2. J. Vinšová, J. Kozic, M. Krátký et al., “Salicylanilide diethyl phosphates: synthesis, antimicrobial activity and cytotoxicity,” Bioorganic and Medicinal Chemistry, vol. 22, no. 2, pp. 728–737, 2014. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Krátký, J. Vinšová, E. Novotná et al., “Salicylanilide derivatives block Mycobacterium tuberculosis through inhibition of isocitrate lyase and methionine aminopeptidase,” Tuberculosis, vol. 92, no. 5, pp. 434–439, 2012. View at Publisher · View at Google Scholar · View at Scopus
  4. S. K. Hatzios and C. R. Bertozzi, “The regulation of sulfur metabolism in Mycobacterium tuberculosis,” PLoS Pathogens, vol. 7, no. 7, Article ID e1002036, 8 pages, 2011. View at Publisher · View at Google Scholar · View at Scopus
  5. M. Krátký, J. Vinšová, E. Novotná, J. Mandíková, F. Trejtnar, and J. Stolaříková, “Antibacterial activity of salicylanilide 4-(trifluoromethyl)benzoates,” Molecules, vol. 18, no. 4, pp. 3674–3688, 2013. View at Publisher · View at Google Scholar · View at Scopus
  6. A. B. Andersen, P. Andersen, and L. Ljungqvist, “Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis,” Infection and Immunity, vol. 60, no. 6, pp. 2317–2323, 1992. View at Google Scholar · View at Scopus
  7. Z. Y. Feng, N. E. Cáceres, G. Sarath, and R. G. Barletta, “Mycobacterium smegmatis L-alanine dehydrogenase (Ald) is required for proficient utilization of alanine as a sole nitrogen source and sustained anaerobic growth,” Journal of Bacteriology, vol. 184, no. 18, pp. 5001–5010, 2002. View at Publisher · View at Google Scholar · View at Scopus
  8. B. Ling, M. Sun, S. Bi, Z. Jing, and Y. Liu, “Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase,” Journal of Molecular Graphics and Modelling, vol. 35, pp. 1–10, 2012. View at Publisher · View at Google Scholar · View at Scopus
  9. J. C. Betts, P. T. Lukey, L. C. Robb, R. A. McAdam, and K. Duncan, “Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling,” Molecular Microbiology, vol. 43, no. 3, pp. 717–731, 2002. View at Publisher · View at Google Scholar · View at Scopus
  10. D. Dube, S. M. Tripathi, and R. Ramachandran, “Identification of in vitro inhibitors of Mycobacterium tuberculosis Lysine ε-aminotransferase by pharmacophore mapping and three-dimensional flexible searches,” Medicinal Chemistry Research, vol. 17, no. 2-7, pp. 182–188, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. M. I. Voskuil, K. C. Visconti, and G. K. Schoolnik, “Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy,” Tuberculosis, vol. 84, no. 3-4, pp. 218–227, 2004. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Ökvist, R. Dey, S. Sasso, E. Grahn, P. Kast, and U. Krengel, “1.6 Å crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed,” Journal of Molecular Biology, vol. 357, no. 5, pp. 1483–1499, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. E. L. White, K. Southworth, L. Ross et al., “A novel inhibitor of Mycobacterium tuberculosis pantothenate synthetase,” Journal of Biomolecular Screening, vol. 12, no. 1, pp. 100–105, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. Yang, P. Gao, Y. Liu et al., “A discovery of novel Mycobacterium tuberculosis pantothenate synthetase inhibitors based on the molecular mechanism of actinomycin D inhibition,” Bioorganic and Medicinal Chemistry Letters, vol. 21, no. 13, pp. 3943–3946, 2011. View at Publisher · View at Google Scholar · View at Scopus
  15. G. H. Dixon and H. L. Kornberg, “Assay methods for key enzymes of the glyoxylate cycle,” Biochemical Journal, vol. 72, p. P3, 1959. View at Google Scholar
  16. S. M. Tripathi and R. Ramachandran, “Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures “open” and “closed” enzyme conformations,” Proteins: Structure, Function and Genetics, vol. 72, no. 3, pp. 1089–1095, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. S. M. Tripathi and R. Ramachandran, “Overexpression, purification, crystallization and preliminary X-ray analysis of Rv2780 from Mycobacterium tuberculosis H37Rv,” Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 64, no. 5, pp. 367–370, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. S. M. Tripathi and R. Ramachandran, “Overexpression, purification and crystallization of lysine ε-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv,” Acta Crystallographica F: Structural Biology and Crystallization Communications, vol. 62, no. 6, pp. 572–575, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Adepu, K. S. Kumar, and S. Sandra, “C-N bond formation under Cu-catalysis: synthesis and in vitro evaluation of N-aryl substituted thieno[2,3-d]pyrimidin-4(3H)-ones against chorismate mutase,” Bioorganic and Medicinal Chemistry, vol. 20, no. 17, pp. 5127–5138, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. G. Samala, P. B. Devi, R. Nallangi, P. Yogeeswari, and D. Sriram, “Development of 3-phenyl-4,5,6,7-tetrahydro-1H-pyrazolo[4,3-c]pyridine derivatives as novel Mycobacterium tuberculosis pantothenate synthetase inhibitors,” European Journal of Medicinal Chemistry, vol. 69, pp. 356–364, 2013. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Wang and D. Eisenberg, “Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate,” Protein Science, vol. 12, no. 5, pp. 1097–1108, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. E. F. Pettersen, T. D. Goddard, C. C. Huang et al., “UCSF Chimera—a visualization system for exploratory research and analysis,” Journal of Computational Chemistry, vol. 25, no. 13, pp. 1605–1612, 2004. View at Publisher · View at Google Scholar · View at Scopus
  23. O. Trott and A. J. Olson, “Software news and update AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading,” Journal of Computational Chemistry, vol. 31, no. 2, pp. 455–461, 2010. View at Publisher · View at Google Scholar · View at Scopus
  24. The PyMol Molecular Graphics System, “Version 1.1r1, Schrödinger, LLC,” http://www.pymol.org.