Aryl derivatives of 3H-1,2-benzoxathiepine 2,2-dioxide as carbonic anhydrase inhibitors

References

• (a) Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nature Rev Drug Discov 2008;7:168–81.(b) 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.(c) Supuran CT. Structure and function of carbonic anhydrases. Biochem J 2016;473:2023–32.
   PubMed Web of Science ®Google Scholar
• (a) Xu Y, Feng L, Jeffrey PD, et al. Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms. Nature 2008;452:56–61.(b) Del Prete S, Vullo D, Fisher GM, et al. Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum – the η-carbonic anhydrases. Bioorg Med Chem Lett 2014;24:4389–96.(c) Jensen EL, Clement R, Kosta A, et al. A new widespread subclass of carbonic anhydrase in marine phytoplankton. ISME J 2019;13:2094–106.
   PubMed Web of Science ®Google Scholar
• (a) Capasso C, Supuran CT. Anti-infective carbonic anhydrase inhibitors: a patent and literature review. Expert Opin Ther Pat 2013;23:693–704.(b) Capasso C, Supuran CT. An overview of the alpha-, beta- and gamma-carbonic anhydrases from bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria? J Enzyme Inhib Med Chem 2015;30:325–32.(c) Capasso C, Supuran CT. Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin Ther Targets 2015;19:1689–704.(d) Supuran CT, Capasso C. Biomedical applications of prokaryotic carbonic anhydrases. Expert Opin Ther Pat 2018;28:745–54.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. How many carbonic anhydrase inhibition mechanisms exist? J Enzyme Inhib Med Chem 2016;31:345–60.(b) Nocentini A, Supuran CT. Advances in the structural annotation of human carbonic anhydrases and impact on future drug discovery. Expert Opin Drug Discov 2019;14:1175–97.(c) Supuran CT. Advances in structure-based drug discovery of carbonic anhydrase inhibitors. Expert Opin Drug Discov 2017;12:61–88.(d) De Simone G, Supuran CT. (In)organic anions as carbonic anhydrase inhibitors. J Inorg Biochem 2012;111:117–29.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrase inhibitors as emerging agents for the treatment and imaging of hypoxic tumors. Expert Opin Investig Drugs 2018;27:963–70.(b) Supuran CT. Carbonic anhydrase inhibitors and their potential in a range of therapeutic areas. Expert Opin Ther Pat 2018;28:709–12.(c) Supuran CT. Applications of carbonic anhydrases inhibitors in renal and central nervous system diseases. Expert Opin Ther Pat 2018; 28:713–21.(d) Neri D, Supuran CT. Interfering with pH regulation in tumours as a therapeutic strategy. Nat Rev Drug Discov 2011;10:767–77.(e) Supuran CT, Alterio V, Di Fiore A, et al. Inhibition of carbonic anhydrase IX targets primary tumors, metastases, and cancer stem cells: three for the price of one. Med Res Rev 2018;38:1799–836.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrases and metabolism. Metabolites 2018;8:25.(b) Supuran CT. Carbonic anhydrase inhibition and the management of hypoxic tumors. Metabolites 2017;7:E48.(c) Da'dara AA, Angeli A, Ferraroni M, et al. Crystal structure and chemical inhibition of essential schistosome host-interactive virulence factor carbonic anhydrase SmCA. Commun Biol 2019;2:333.
   PubMed Web of Science ®Google Scholar
• Tars K, Vullo D, Kazaks A, et al. Sulfocoumarins (1,2-benzoxathiine 2,2-dioxides): a class of potent and isoform-selective inhibitors of tumor-associated carbonic anhydrases. J Med Chem 2013;56:293–300.
   PubMed Web of Science ®Google Scholar
• (a) Tanc M, Carta F, Bozdag M, et al. 7-Substituted-sulfocoumarins are isoform-selective, potent carbonic anhydrase II inhibitors. Bioorg Med Chem 2013;21:4502–10.(b) Nocentini A, Ceruso M, Carta F, Supuran CT. 7-Aryl-triazolyl-substituted sulfocoumarins are potent, selective inhibitors of the tumor-associated carbonic anhydrase IX and XII. J Enzyme Inhib Med Chem 2016;31:1226–33.(c) Grandane A, Tanc M, Mannelli LDC, et al. Substituted sulfocoumarins are selective carbonic anhdydrase IX and XII inhibitors with significant cytotoxicity against colorectal cancer cells. J. Med. Chem 2015;58:3975–83.
   PubMed Web of Science ®Google Scholar
• (a) Maresca A, Temperini C, Vu H, et al. Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc 2009;131:3057–62.(b) Maresca A, Temperini C, Pochet L, et al. Deciphering the mechanism of carbonic anhydrase inhibition with coumarins and thiocoumarins. J Med Chem 2010;53:335–44.(c) Temperini C, Innocenti A, Scozzafava A, et al. The coumarin-binding site in carbonic anhydrase accommodates structurally diverse inhibitors: the antiepileptic lacosamide as an example. J Med Chem 2010;53:850–4.(d) Touisni N, Maresca A, McDonald PC, et al. Glycosylcoumarin carbonic anhydrase IX and XII inhibitors strongly attenuate the growth of primary breast tumors. J Med Chem 2011;54:8271–7.
   PubMed Web of Science ®Google Scholar
• Pustenko A, Stepanovs D, Žalubovskis R, et al. 3H-1,2-benzoxathiepine 2,2-dioxides: a new class of isoform-selective carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem 2017;32:767–75.
   PubMed Web of Science ®Google Scholar
• Yin H, Zhang B, Yu H, et al. Two-photon fluorescent probes for biological Mg2+ detection based on 7-substituted coumarin. J Org Chem 2015;80:4306–12.
   PubMed Web of Science ®Google Scholar
• Gillis EP, Burke MD. A simple and modular strategy for small molecule synthesis: iterative Suzuki–Miyaura coupling of B-protected haloboronic acid building blocks. J Am Chem Soc 2007;129:6716–7.
   PubMed Web of Science ®Google Scholar
• Seoane A, Casanova N, Quinones N, et al. Straightforward assembly of benzoxepines by means of a rhodium(III)-catalyzed C-H functionalization of o-vinylphenols. J Am Chem Soc 2014;136:834–7.
   PubMed Web of Science ®Google Scholar
• Hoveyda HR, Marsault E, Gagnon R, et al. Optimization of the potency and pharmacokinetic properties of a macrocyclic ghrelin receptor agonist (Part I): development of ulimorelin (TZP-101) from hit to clinic. J Med Chem 2011;54:8305–20.
   PubMed Web of Science ®Google Scholar
• Khalifah RG. The carbon dioxide hydration activity of carbonic anhydrase. J Biol Chem 1971;246:2561–73.
   PubMed Web of Science ®Google Scholar
• (a) Nocentini A, Bua S, Del Prete S, et al. Malassezia globosa: activity and modeling studies. ChemMedChem 2018;13:816–23.(b) D'Ascenzio M, Guglielmi P, Carradori S, et al. Open saccharin-based secondary sulfonamides as potent and selective inhibitors of cancer-related carbonic anhydrase IX and XII isoforms. J Enzyme Inhib Med Chem 2017;32:51–9.(c) Nocentini A, Ceruso M, Bua S, et al. Discovery of β-adrenergic receptors blocker-carbonic anhydrase inhibitor hybrids for multitargeted antiglaucoma therapy. J Med Chem 2018;61:5380–94.(d) Köhler K, Hillebrecht A, Schulze Wischeler J, et al. Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste. Angew Chem Int Ed Engl 2007;46:7697–9.
   PubMed Web of Science ®Google Scholar
• (a) Vermelho AB, da Silva Cardoso V, Ricci Junior E, et al. Nanoemulsions of sulfonamide carbonic anhydrase inhibitors strongly inhibit the growth of Trypanosoma cruzi. J Enzyme Inhib Med Chem 2018;33:139–46.(b) Nocentini A, Carta F, Tanc M, et al. Deciphering the mechanism of human carbonic anhydrases inhibition with sulfocoumarins: computational and experimental studies. Chemistry 2018;24:7840–4.(c) Awadallah FM, Bua S, Mahmoud WR, et al. Inhibition studies on a panel of human carbonic anhydrases with N1-substituted secondary sulfonamides incorporating thiazolinone or imidazolone-indole tails. J Enzyme Inhib Med Chem 2018;33:629–38.
   PubMed Web of Science ®Google Scholar
• (a) Bua S, Bozdag M, Del Prete S, et al. Mono- and di-thiocarbamate inhibition studies of the δ-carbonic anhydrase TweCAδ from the marine diatom Thalassiosira weissflogii. J Enzyme Inhib Med Chem 2018;33:707–13.(b) Ferraroni M, Gaspari R, Scozzafava A, et al. Dioxygen, an unexpected carbonic anhydrase ligand. J Enzyme Inhib Med Chem 2018;33:999–1005.(c) El-Gazzar MG, Nafie NH, Nocentini A, et al. Carbonic anhydrase inhibition with a series of novel benzenesulfonamide-triazole conjugates. J Enzyme Inhib Med Chem 2018;33:1565–74.(d) Akocak S, Lolak N, Bua S, Supuran CT. Discovery of novel 1,3-diaryltriazene sulfonamides as carbonic anhydrase I, II, VII, and IX inhibitors. J Enzyme Inhib Med Chem 2018;33:1575–80.
   PubMed Web of Science ®Google Scholar
• (a) Nocentini A, Bonardi A, Gratteri P, et al. Steroids interfere with human carbonic anhydrase activity by using alternative binding mechanisms. J Enzyme Inhib Med Chem 2018;33:1453–9.(b) Nocentini A, Trallori E, Singh S, et al. 4-Hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms IX and XII showing hypoxia-enhanced antiproliferative profiles. J Med Chem 2018;61:10860–74.(c) Chohan ZH, Munawar A, Supuran CT. Transition metal ion complexes of Schiff bases. Synthesis, characterization and antibacterial properties. Met Based Drugs 2001;8:137–43.(d) 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
• (a) Supuran CT, Clare BW. Carbonic anhydrase inhibitors. Part 57. Quantum chemical QSAR of a group of 1,3,4-thiadiazole and 1,3,4-thiadiazoline disulfonamides with carbonic anhydrase inhibitory properties. Eur J Med Chem 1999;34:41–50.(b) Supuran CT, Ilies MA, Scozzafava A. Carbonic anhydrase inhibitors. Part 29. Interaction of isozymes I, II and IV with benzolamide-like derivatives. Eur J Med Chem 1998;33:739–52.(c) Sentürk M, Gülçin I, Daştan A, et al. Carbonic anhydrase inhibitors. Inhibition of human erythrocyte isozymes I and II with a series of antioxidant phenols. Bioorg Med Chem 2009;17:3207–11.
   Web of Science ®Google Scholar