Inhibition studies of Brucella suis β-carbonic anhydrases with a series of 4-substituted pyridine-3-sulphonamides

References

• (a) Supuran CT, Capasso C. An overview of the bacterial carbonic anhydrases. Metabolites 2017;7:E56.(b) Capasso C, Supuran CT. An overview of the carbonic anhydrases from two pathogens of the oral cavity: Streptococcus mutans and Porphyromonas gingivalis. Curr Top Med Chem 2016;16:2359–68.(c) Köhler S, Ouahrani-Bettache S, Winum JY. Brucella suis carbonic anhydrases and their inhibitors: towards alternative antibiotics? J Enzyme Inhib Med Chem 2017;32:683–7.(d) Supuran CT. Bacterial carbonic anhydrases as drug targets: toward novel antibiotics? Front Pharmacol 2011;2:34.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT, Capasso C. Carbonic anhydrase from Porphyromonas Gingivalis as a drug target. Pathogens 2017;6:E30. (b) Capasso C, Supuran CT. Inhibition of bacterial carbonic anhydrases as a novel approach to escape drug resistance. Curr Top Med Chem 2017;17:1237–48. (c) Supuran CT, Capasso C. New light on bacterial carbonic anhydrases phylogeny based on the analysis of signal peptide sequences. Enzyme Inhib Med Chem 2016;31:1254–60. (d) Supuran CT. Legionella pneumophila carbonic anhydrases: underexplored antibacterial drug targets. Pathogens 2016;5:E44.
   PubMed Web of Science ®Google Scholar
• (a) De Vita D, Angeli A, Pandolfi F, et al. Inhibition of the α-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties. J Enzyme Inhib Med Chem 2017;32:798–804. (b) Del Prete S, Vullo D, Osman SM, et al. Sulfonamide inhibition profiles of the β-carbonic anhydrase from the pathogenic bacterium Francisella tularensis responsible of the febrile illness tularemia. Bioorg Med Chem 2017;25:3555–61. (c) Vullo D, Del Prete S, Di Fonzo P, et al. Comparison of the sulfonamide inhibition profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei. Molecules 2017;22:E421.
   PubMed Web of Science ®Google Scholar
• (a) Vullo D, Kumar RSS, Scozzafava A, et al. Sulphonamide inhibition studies of the β-carbonic anhydrase from the bacterial pathogen Clostridium perfringens. Enzyme Inhib Med Chem 2018;33:31–6. (b) Angeli A, Abbas G, Del Prete S, et al. Acyl selenoureido benzensulfonamides show potent inhibitory activity against carbonic anhydrases from the pathogenic bacterium Vibrio cholerae. Bioorg Chem 2017;75:170–2. (c) Aspatwar A, Hammarén M, Koskinen S, et al. β-CA-specific inhibitor dithiocarbamate Fc14-584B: a novel antimycobacterial agent with potential to treat drug-resistant tuberculosis. J Enzyme Inhib Med Chem 2017;32:832–40.
   PubMed Web of Science ®Google Scholar
• (a) Mohamed MA, Abdel-Aziz AA, Sakr HM, et al. Synthesis and human/bacterial carbonic anhydrase inhibition with a series of sulfonamides incorporating phthalimido moieties. Bioorg Med Chem 2017;25:2524–9. (b) Modak JK, Liu YC, Supuran CT, Roujeinikova A. Structure–activity relationship for sulphonamide inhibition of Helicobacter pylori α-carbonic anhydrase. J Med Chem 2016;59:11098–109. (c) Cau Y, Mori M, Supuran CT, Botta M. Mycobacterial carbonic anhydrase inhibition with phenolic acids and esters: kinetic and computational investigations. Org Biomol Chem 2016;14:8322–30.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Advances in structure-based drug discovery of carbonic anhydrase inhibitors. Expert Opin Drug Discov 2017;12:61–88. (b) Supuran Structure and function of carbonic anhydrases. Biochem J 2016;473:2023–32. (c) Supuran CT. How many carbonic anhydrase inhibition mechanisms exist? J Enzyme Inhib Med Chem 2016;31:345–60.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Bortezomib inhibits bacterial and fungal β-carbonic anhydrases. Bioorg Med Chem 2016;24:4406–9. (b) Lomelino CL, Supuran CT, McKenna R. Non-classical inhibition of carbonic anhydrase. Int J Mol Sci 2016;17:E1150. (c) Annunziato G, Angeli A, D'Alba F, et al. Discovery of new potential anti-infective compounds based on carbonic anhydrase inhibitors by rational target-focused repurposing approaches. ChemMedChem 2016;11:1904–14.
   PubMed Web of Science ®Google Scholar
• (a) Ferraroni M, Del Prete S, Vullo D, et al. Crystal structure and kinetic studies of a tetrameric type II β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae. Acta Crystallogr D Biol Crystallogr 2015;71:2449–56.(b) Orhan F, Şentürk M, Supuran CT. Interaction of anions with a newly characterized alpha carbonic anhydrase from Halomonas sp. J Enzyme Inhib Med Chem 2016;31:1119–23. (c) Eminoğlu A, Vullo D, Aşık A, et al. Cloning, expression and biochemical characterization of a β-carbonic anhydrase from the soil bacterium Enterobacter sp. B13. J Enzyme Inhib Med Chem 2016;31:1111–8.
   PubMedGoogle Scholar
• (a) Joseph P, Turtaut F, Ouahrani-Bettache S, et al. Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Brucella suis. J Med Chem 2010;53:2277–85. (b) Joseph P, Ouahrani-Bettache S, Montero JL, et al. A new β-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth. Bioorg Med Chem 2011;19:1172–8.
   PubMed Web of Science ®Google Scholar
• (a) Winum JY, Köhler S, Supuran CT. Brucella carbonic anhydrases: new targets for designing anti-infective agents. Curr Pharm Des 2010;16:3310–6. (b) Vullo D, Nishimori I, Scozzafava A, et al. Inhibition studies of a beta-carbonic anhydrase from Brucella suis with a series of water soluble glycosyl sulfanilamides. Bioorg Med Chem Lett 2010;20:2178–82. (c) Supuran CT. Inhibition of bacterial carbonic anhydrases and zinc proteases: from orphan targets to innovative new antibiotic drugs. Curr Med Chem 2012;19:831–44.
   PubMed Web of Science ®Google Scholar
• (a) Riafrecha LE, Vullo D, Supuran CT, Colinas PA. C-glycosides incorporating the 6-methoxy-2-naphthyl moiety are selective inhibitors of fungal and bacterial carbonic anhydrases. J Enzyme Inhib Med Chem 2015;30:857–61. (b) Riafrecha LE, Vullo D, Ouahrani-Bettache S, et al. Inhibition of β-carbonic anhydrases from Brucella suis with C-cinnamoyl glycosides incorporating the phenol moiety. J Enzyme Inhib Med Chem 2015;30:1017–20. (c) Ombouma J, Vullo D, Köhler S, et al. N-glycosyl-N-hydroxysulfamides as potent inhibitors of Brucella suis carbonic anhydrases. J Enzyme Inhib Med Chem 2015;30:1010–2. (d) Ceruso M, Carta F, Osman SM, et al. Inhibition studies of bacterial, fungal and protozoan β-class carbonic anhydrases with Schiff bases incorporating sulfonamide moieties. Bioorg Med Chem 2015;23:4181–7.
   PubMed Web of Science ®Google Scholar
• Sławiński J, Szafrański K, Vullo D, Supuran CT. Carbonic anhydrase inhibitors. Synthesis of heterocyclic 4-substituted pyridine-3-sulfonamide derivatives and their inhibition of the human cytosolic isozymes I and II and transmembrane tumor-associated isozymes IX and XII. Eur J Med Chem 2013;69:701–10.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 2008;7:168–81. (b) Supuran CT. Structure-based drug discovery of carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem 2012;27:759–72. (c) Alterio V, Di Fiore A, D'Ambrosio K, et al. Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem Rev 2012;112:4421–68.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrases: from biomedical applications of the inhibitors and activators to biotechnological use for CO2 capture. J Enzyme Inhib Med Chem 2013;28:229–30. (b) Capasso Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin Ther Targets 2015;19:1689–704. (c) Neri D, Supuran CT. Interfering with pH regulation in tumours as a therapeutic strategy. Nat. Rev. Drug Discov 2011;10:767–77. (d) Monti SM, Supuran CT, Simone GD. Anticancer carbonic anhydrase inhibitors: a patent review (2008–2013). Expert Opin Ther Patents 2013;23:737–49.
   PubMed Web of Science ®Google Scholar
• (a) Masini E, Carta F, Scozzafava A, Supuran CT. Antiglaucoma carbonic anhydrase inhibitors: a patent review. Expert Opin Ther Patents 2013;23:705–16. (b) Supuran CT. Acetazolamide for the treatment of idiopathic intracranial hypertension. Expert Rev Neurother 2015;15:851–6. (c) Scozzafava A. Antiobesity carbonic anhydrase inhibitors: a literature and patent review. Expert Opin Ther Patents 2013;23:725–35.
   PubMed Web of Science ®Google Scholar
• (a) Carta F, Supuran CT. Diuretics with carbonic anhydrase inhibitory action: a patent and literature review (2005–2013). Expert Opin Ther Pat 2013;23:681–91. (b) Supuran CT. Carbonic anhydrase inhibitors. Bioorg Med Chem Lett 2010;20:3467–74. (c) Supuran CT. Drug interaction considerations in the therapeutic use of carbonic anhydrase inhibitors. Expert Opin Drug Metab Toxicol 2016;12:423–31. (d) Karioti A, Carta F, Supuran CT. An Update on Natural Products with Carbonic Anhydrase Inhibitory Activity. Curr Pharm Des 2016;22:1570–91. (e) Winum JY, Supuran CT. Recent advances in the discovery of zinc-binding motifs for the development of carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem 2015;30:321–4.
   PubMed Web of Science ®Google Scholar
• (a) Carta F, Di Cesare Mannelli L, Pinard M, et al. A class of sulfonamide carbonic anhydrase inhibitors with neuropathic pain modulating effects. Bioorg Med Chem 2015;23:1828–40. (b) Supuran CT. Carbonic anhydrase inhibition and the management of neuropathic pain. Expert Rev Neurother 2016;16:961–8.
   PubMed Web of Science ®Google Scholar
• Di Cesare Mannelli L, Micheli L, Carta F, et al. Carbonic anhydrase inhibition for the management of cerebral ischemia: in vivo evaluation of sulfonamide and coumarin inhibitors. J Enzyme Inhib Med Chem 2016;31:894–9.
   PubMed Web of Science ®Google Scholar
• (a) Margheri F, Ceruso M, Carta F, et al. Overexpression of the transmembrane carbonic anhydrase isoforms IX and XII in the inflamed synovium. J Enzyme Inhib Med Chem 2016;31(sup4):60–3. (b) Bua S, Di Cesare Mannelli L, Vullo D, et al. Design and synthesis of novel nonsteroidal anti-inflammatory drugs and carbonic anhydrase inhibitors hybrids (NSAIDs-CAIs) for the treatment of rheumatoid arthritis. J Med Chem 2017;60:1159–70.
   Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• (a) Scozzafava A, Briganti F, Mincione G, et al. Carbonic anhydrase inhibitors: synthesis of water-soluble, aminoacyl/dipeptidyl sulfonamides possessing long-lasting intraocular pressure-lowering properties via the topical route. J Med Chem 1999;42:3690–700. (b) Puccetti L, Fasolis G, Vullo D, et al. Carbonic anhydrase inhibitors. Inhibition of cytosolic/tumor-associated carbonic anhydrase isozymes I, II, IX, and XII with Schiff's bases incorporating chromone and aromatic sulfonamide moieties, and their zinc complexes. Bioorg Med Chem Lett 2005;15:3096–101.
   PubMed Web of Science ®Google Scholar
• (a) Garaj V, Puccetti L, Fasolis G, et al. Carbonic anhydrase inhibitors: novel sulfonamides incorporating 1, 3, 5-triazine moieties as inhibitors of the cytosolic and tumour-associated carbonic anhydrase isozymes I, II and IX. Bioorg Med Chem Lett 2005;1:3102–8. (b) Scozzafava A, Menabuoni L, Mincione F, Supuran CT. Carbonic anhydrase inhibitors. A general approach for the preparation of water-soluble sulfonamides incorporating polyamino − polycarboxylate tails and of their metal complexes possessing long-lasting, topical intraocular pressure-lowering properties. J Med Chem 2002;45:1466–76.
   Web of Science ®Google Scholar
• (a) Supuran CT, Nicolae A, Popescu A. Carbonic anhydrase inhibitors. Part 35. Synthesis of Schiff bases derived from sulfanilamide and aromatic aldehydes: the first inhibitors with equally high affinity towards cytosolic and membrane-bound isozymes. Eur J Med Chem 1996;31:431–8. (b) Şentürk M, Gülçin I, Beydemir Ş, et al. In vitro inhibition of human carbonic anhydrase I and II isozymes with natural phenolic compounds. Chem Biol Drug Des 2011;77:494–9. (c) Carta F, Aggarwal M, Maresca A, et al. Dithiocarbamates: a new class of carbonic anhydrase inhibitors. Crystallographic and kinetic investigations. Chem Commun (Camb) 2012;48:1868–70.
   Web of Science ®Google Scholar
• (a) Supuran CT, Barboiu M, Luca C, et al. Carbonic anhydrase activators. Part 14. Syntheses of mono and bis pyridinium salt derivatives of 2-amino-5-(2-aminoethyl)- and 2-amino-5-(3-aminopropyl)-1,3,4-thiadiazole and their interaction with isozyme II. Eur J Med Chem 1996;31:597–606. (b) Carta F, Aggarwal M, Maresca A, et al. Dithiocarbamates strongly inhibit carbonic anhydrases and show antiglaucoma action in vivo. J Med Chem 2012;55:1721–30. (c) Maresca A, Carta F, Vullo D, Supuran CT. Dithiocarbamates strongly inhibit the β-class carbonic anhydrases from Mycobacterium tuberculosis. J Enzyme Inhib Med Chem 2013;28:407–11.
   Web of Science ®Google Scholar
• (a) Fabrizi F, Mincione F, Somma T, et al. A new approach to antiglaucoma drugs: carbonic anhydrase inhibitors with or without NO donating moieties. Mechanism of action and preliminary pharmacology. J Enzyme Inhib Med Chem 2012;27:138–47. (b) Zimmerman SA, Ferry JG, Supuran CT. Inhibition of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases. Curr Top Med Chem 2007;7:901–8. (c) Oztürk Sarikaya SB, Topal F, Sentürk M, et al. In vitro inhibition of α-carbonic anhydrase isozymes by some phenolic compounds. Bioorg Med Chem Lett 2011;21:4259–62.
   PubMed Web of Science ®Google Scholar