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Research Paper

Diversely N-substituted benzenesulfonamides dissimilarly bind to human carbonic anhydrases: crystallographic investigations of N-nitrosulfonamides

ORCID Icon, , , ORCID Icon & ORCID Icon
Article: 2178430 | Received 13 Jan 2023, Accepted 06 Feb 2023, Published online: 16 Feb 2023

References

  • Supuran CT, Capasso C. An overview of the bacterial carbonic anhydrases. Metabolites. 2017;7(4):56.
  • Supuran CT. Structure and function of carbonic anhydrases. Biochem J. 2016;473(14):2023–2032.
  • Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov. 2008;7(2):168–181.
  • Capasso C, Supuran CT. Inhibition of bacterial carbonic anhydrases as a novel approach to escape drug resistance. Curr Top Med Chem. 2017;17(11):1237–1248.
  • Neri D, Supuran CT. Interfering with pH regulation in tumours as a therapeutic strategy. Nat Rev Drug Discov. 2011;10(10):767–777.
  • Alterio V, Di Fiore A, D'Ambrosio K, Supuran CT, De Simone G. Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem Rev. 2012;112(8):4421–4468.
  • Supuran CT, Scozzafava A. Carbonic anhydrases as targets for medicinal chemistry. Bioorg Med Chem. 2007;15(13):4336–4350.
  • Supuran CT. Carbonic anhydrase inhibitors and their potential in a range of therapeutic areas. Expert Opin Ther Pat. 2018;28(10):709–712.
  • Supuran CT. Multitargeting approaches involving carbonic anhydrase inhibitors: hybrid drugs against a variety of disorders. J Enzyme Inhib Med Chem. 2021;36(1):1702–1714.
  • Mishra CB, Tiwari M, Supuran CT. Progress in the development of human carbonic anhydrase inhibitors and their pharmacological applications: where are we today? Med Res Rev. 2020;40(6):2485–2565.
  • Supuran CT. Carbonic anhydrase inhibitors and activators for novel therapeutic applications. Future Med Chem. 2011;3(9):1165–1180.
  • Bozdag M, Ferraroni M, Nuti E, Vullo D, Rossello A, Carta F, Scozzafava A, Supuran CT. Combining the tail and the ring approaches for obtaining potent and isoform-selective carbonic anhydrase inhibitors: solution and X-ray crystallographic studies. Bioorg Med Chem. 2014;22(1):334–340.
  • Kumar A, Siwach K, Supuran CT, Sharma PK. A decade of tail-approach based design of selective as well as potent tumor associated carbonic anhydrase inhibitors. Bioorg Chem. 2022;126:105920.
  • Al-Warhi T, Sabt A, Elkaeed EB, Eldehna WM. Recent advancements of coumarin-based anticancer agents: an up-to-date review. Bioorg Chem. 2020;103:104163.
  • Maresca A, Temperini C, Vu H, Pham NB, Poulsen SA, Scozzafava A, Quinn RJ, Supuran CT. Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc. 2009;131(8):3057–3062.
  • Briganti F, Pierattelli R, Scozzafava A, Supuran CT. Carbonic anhydrase inhibitors. Part 37. Novel classes of carbonic anhydrase inhibitors and their interaction with the native and cobalt-substituted enzyme: kinetic and spectroscopic investigations. Eur J Med Chem. 1996;31(12):1001–1010.
  • Di Fiore A, Maresca A, Alterio V, Supuran CT, De Simone G. Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II. Chem Commun. 2011;47(42):11636–11638.
  • Nocentini A, Vullo D, Bartolucci G, Supuran CT. N-nitrosulfonamides: a new chemotype for carbonic anhydrase inhibition. Bioorg Med Chem. 2016;24(16):3612–3617.
  • Bonardi A, Vermelho AB, da Silva Cardoso V, de Souza Pereira MC, da Silva Lara L, Selleri S, Gratteri P, Supuran CT, Nocentini A. N-nitrosulfonamides as carbonic anhydrase inhibitors: a promising chemotype for targeting Chagas disease and leishmaniasis. ACS Med Chem Lett. 2019;10(4):413–418.
  • Supuran CT. Carbon- versus sulphur-based zinc binding groups for carbonic anhydrase inhibitors? J Enzyme Inhib Med Chem. 2018;33(1):485–495.
  • Scott AD, Phillips C, Alex A, Flocco M, Bent A, Randall A, O'Brien R, Damian L, Jones LH. Thermodynamic optimisation in drug discovery: a case study using carbonic anhydrase inhibitors. ChemMedChem. 2009;4(12):1985–1989.
  • Sjöblom B, Polentarutti M, Djinovic-Carugo K. Structural study of X-ray induced activation of carbonic anhydrase. Proc Natl Acad Sci U S A. 2009;106(26):10609–10613.
  • Baronas D, Dudutienė V, Paketurytė V, Kairys V, Smirnov A, Juozapaitienė V, Vaškevičius A, Manakova E, Gražulis S, Zubrienė A, et al. Structure and mechanism of secondary sulfonamide binding to carbonic anhydrases. Eur Biophys J. 2021;50(7):993–1011.
  • 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(8):2561–2573.
  • Lesli AGW, Powell HR. Processing diffraction data with mosflm. In: Read RJ, Sussman JL, editors. Evolving methods for macromolecular crystallography. Vol. 245. Dordrecht: NATO Science Series, Springer; 2007. p. 41–51.
  • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr. 1997;53(Pt 3):240–255.
  • Emsley P, Lohkamp B, Scott W, Cowtan K. Features and development of Coot. Acta Crystallogr D Biol Crystallogr. 2010;66(Pt 4):486–501.
  • Lovell SC, Davis IW, Arendall IIW, de Bakker PIW, Word JM, Prisant MG, Richardson JS, Richardson DC. Structure validation by Cα geometry: ϕ, ψ and Cβ deviation. Proteins. 2003;50(3):437–450.
  • Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. UCSF Chimera—a visualization system for exploratory research and analysis. J Comput Chem. 2004;25(13):1605–1612.