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Research Article

Sulfonamides incorporating fluorine and 1,3,5-triazine moieties are effective inhibitors of three β-class carbonic anhydrases from Mycobacterium tuberculosis

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Pages 686-689 | Received 10 Aug 2013, Accepted 04 Sep 2013, Published online: 24 Oct 2013

References

  • Suarez Covarrubias A, Larsson AM, Hogbom M, et al. Structure and function of carbonic anhydrases from Mycobacterium tuberculosis. J Biol Chem 2005;280:18782–9
  • Covarrubias AS, Bergfors T, Jones TA, Hogbom M. Structural mechanics of the pH-dependent activity of beta-carbonic anhydrase from Mycobacterium tuberculosis. J Biol Chem 2006;281:4993–9
  • Minakuchi T, Nishimori I, Vullo D, et al. Molecular cloning, characterization, and inhibition studies of the Rv1284 beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides and a sulfamate. J Med Chem 2009;52:2226–32
  • Nishimori I, Minakuchi T, Vullo D, et al. Carbonic anhydrase inhibitors. Cloning, characterization, and inhibition studies of a new beta-carbonic anhydrase from Mycobacterium tuberculosis. J Med Chem 2009;52:3116–20
  • Guzel O, Maresca A, Scozzafava A, et al. Discovery of low nanomolar and subnanomolar inhibitors of the mycobacterial beta-carbonic anhydrases Rv1284 and Rv3273. J Med Chem 2009;52:4063–7
  • Carta F, Maresca A, Covarrubias AS, et al. Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c. Bioorg Med Chem Lett 2009;19:6649–54
  • Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 2008;7:168–81
  • Neri D, Supuran CT. Interfering with pH regulation in tumours as a therapeutic strategy. Nat Rev Drug Discov 2011;10:767–77
  • Pastorekova S, Parkkila S, Pastorek J, Supuran CT. Carbonic anhydrases: current state of the art, therapeutic applications and future prospects. J Enzyme Inhib Med Chem 2004;19:199–229
  • Supuran CT. Carbonic anhydrase inhibitors and activators for novel therapeutic applications. Future Med Chem 2011;3:1165–80
  • Supuran CT. Bacterial carbonic anhydrases as drug targets: toward novel antibiotics? Front Pharmacol 2011;2:34
  • Dye C. Doomsday postponed? Preventing and reversing epidemics of drug-resistant tuberculosis. Nat Rev Microbiol 2009;7:81–7
  • Furtado GH, Nicolau DP. Overview perspective of bacterial resistance. Expert Opin Ther Pat 2010;20:1273–6
  • Ginsberg AM. Emerging drugs for active tuberculosis. Semin Respir Crit Care Med 2008;29:552–9
  • Showalter HD, Denny WA. A roadmap for drug discovery and its translation to small molecule agents in clinical development for tuberculosis treatment. Tuberculosis (Edinb) 2008;88:S3–17
  • Tomioka H, Tatano Y, Yasumoto K, Shimizu T. Recent advances in antituberculous drug development and novel drug targets. Expert Rev Respir Med 2008;2:455–71
  • Supuran CT, Scozzafava A, Casini A. Carbonic anhydrase inhibitors. Med Res Rev 2003;23:146–89
  • Winum JY, Kohler S, Supuran CT. Brucella carbonic anhydrases: new targets for designing anti-infective agents. Curr Pharm Des 2010;16:3310–16
  • Vullo D, Nishimori I, Minakuchi T, et al. Inhibition studies with anions and small molecules of two novel beta-carbonic anhydrases from the bacterial pathogen Salmonella enterica serovar Typhimurium. Bioorg Med Chem Lett 2011;21:3591–5
  • Nishimori I, Onishi S, Takeuchi H, Supuran CT. The alpha and beta classes carbonic anhydrases from Helicobacter pylori as novel drug targets. Curr Pharm Des 2008;14:622–30
  • Supuran CT. Carbonic anhydrase inhibition with natural products: novel chemotypes and inhibition mechanisms. Mol Divers 2011;15:305–16
  • Supuran CT. Carbonic anhydrase inhibitors. Bioorg Med Chem Lett 2010;20:3467–74
  • Pacchiano F, Carta F, Vullo D, et al. Inhibition of beta-carbonic anhydrases with ureido-substituted benzenesulfonamides. Bioorg Med Chem Lett 2011;21:102–5
  • Carta F, Garaj V, Maresca A, et al. Sulfonamides incorporating 1,3,5-triazine moieties selectively and potently inhibit carbonic anhydrase transmembrane isoforms IX, XII and XIV over cytosolic isoforms I and II: solution and X-ray crystallographic studies. Bioorg Med Chem 2011;19:3105--19
  • Ceruso M, Vullo D, Scozzafava A, Supuran CT. Inhibition of human carbonic anhydrase isoforms I-XIV with sulfonamides incorporating fluorine and 1,3,5-triazine moieties. Bioorg Med Chem 2013 [Epub ahead of print]. http://dx.doi.org/10.1016/j.bmc.2013.09.031
  • Nishimori I, Minakuchi T, Maresca A, et al. The beta-carbonic anhydrases from Mycobacterium tuberculosis as drug targets. Curr Pharm Des 2010;16:3300–9
  • Ilies MA, Vullo D, Pastorek J, et al. Carbonic anhydrase inhibitors. Inhibition of tumor-associated isozyme IX by halogenosulfanilamide and halogenophenylaminobenzolamide derivatives. J Med Chem 2003;46:2187–96
  • Khalifah RG. The carbon dioxide hydration activity of carbonic anhydrase: I. stop-flow kinetic studies on the native human isoenzymes B and C. J Biol Chem 1971;246:2561–73
  • Kolayli S, Karahalil F, Sahin H, et al. Characterization and inhibition studies of an alpha-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti. J Enzyme Inhib Med Chem 2011;26:895–900
  • Schlicker C, Hall RA, Vullo D, et al. Structure and inhibition of the CO2-sensing carbonic anhydrase Can2 from the pathogenic fungus Cryptococcus neoformans. J Mol Biol 2009;385:1207–20

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