Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray crystallographic studies

Bioorganic and Medicinal Chemistry Letters

Volumn 18, Issue 15, 2008, Pages 4282-4286

  Temperini, Claudia ^a   Innocenti, Alessio ^a   Scozzafava, Andrea ^a   Supuran, Claudiu T ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Anticancer agent; Carbonic anhydrase; Coumate; Isozyme; Sulfamate; X ray crystallography

Indexed keywords

667 COUMATE; ACETAZOLAMIDE; ANTINEOPLASTIC AGENT; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE INHIBITOR; EMD 486019; ISOENZYME; TOPIRAMATE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; DRUG ACTIVITY; DRUG BINDING; DRUG MECHANISM; ENZYME ACTIVITY; ENZYME INHIBITION; HUMAN; KINETICS; MOLECULAR INTERACTION; MOUSE; NONHUMAN; X RAY CRYSTALLOGRAPHY;

ANIMALS; CARBONIC ANHYDRASE INHIBITORS; CARBONIC ANHYDRASES; COUMARINS; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; HUMANS; ISOENZYMES; MICE; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; SULFONAMIDES; SULFONIC ACIDS;

MAMMALIA;

EID: 47749140697     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.06.105     Document Type: Article

References (44)

1. Supuran C.T. Nature Rev. Drug Discov. 7 (2008) 168
2. Pastorekova S., Parkkila S., Pastorek J., and Supuran C.T. J. Enzyme Inhib. Med. Chem. 19 (2004) 199-229
3. Supuran C.T., Scozzafava A., and Casini A. Development of sulfonamide carbonic anhydrase inhibitors. In: Supuran C.T., Scozzafava A., and Conway J. (Eds). Carbonic Anhydrase-Its Inhibitors and Activators (2004), CRC Press, Boca Raton 67-147
4. Thiry A., Dogné J.-M., Masereel B., and Supuran C.T. Trends Pharmacol. Sci. 27 (2006) 566
5. Supuran C.T., Scozzafava A., and Casini A. Med. Res. Rev. 23 (2003) 146
6. Scozzafava A., Mastrolorenzo A., and Supuran C.T. Expert Opin. Ther. Pat. 14 (2004) 667
7. Winum J.Y., Montero J.L., Scozzafava A., and Supuran C.T. Mini-Rev. Med. Chem. 6 (2006) 921
8. Winum J.Y., Scozzafava A., Montero J.L., and Supuran C.T. Med. Res. Rev. 25 (2005) 186
9. Winum J.-Y., Scozzafava A., Montero J.-L., and Supuran C.T. Expert Opin. Ther. Pat. 16 (2006) 27
10. Köhler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., and Klebe G. Angew. Chem. Int. Ed. Engl. 46 (2007) 7697
11. Winum J.-Y., Scozzafava A., Montero J.-L., and Supuran C.T. Med. Res. Rev. 26 (2006) 767
12. Winum J.-Y., Rami M., Scozzafava A., Montero J.-L., and Supuran C.T. Med. Res. Rev. 28 (2008) 445
13. Alterio V., Vitale R.M., Monti S.M., Pedone C., Scozzafava A., Cecchi A., De Simone G., and Supuran C.T. J. Am. Chem. Soc. 128 (2006) 8329
14. Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A., and Klebe G. J. Med. Chem. 47 (2004) 550
15. Menchise V., De Simone G., Alterio V., Di Fiore A., Pedone C., Scozzafava A., and Supuran C.T. J. Med. Chem. 48 (2005) 5721
16. De Simone G., Di Fiore A., Menchise V., Pedone C., Antel J., Casini A., Scozzafava A., Wurl M., and Supuran C.T. Bioorg. Med. Chem. Lett. 15 (2005) 2315
17. Casini A., Antel J., Abbate F., Scozzafava A., David S., Waldeck H., Schafer S., and Supuran C.T. Bioorg. Med. Chem. Lett. 13 (2003) 841
18. Abbate F., Casini A., Owa T., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 14 (2004) 217
19. Abbate F., Supuran C.T., Scozzafava A., Orioli P., Stubbs M., and Klebe G. J. Med. Chem. 45 (2002) 3583
20. Winum J.Y., Temperini C., El Cheikh K., Innocenti A., Vullo D., Ciattini S., Montero J.L., Scozzafava A., and Supuran C.T. J. Med. Chem. 49 (2006) 7024
21. Boriack P.A., Christianson D.W., Kingery-Wood J., and Whitesides G.M. J. Med. Chem. 38 (1995) 2286
22. Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A., Dean T., Laipis P., Silverman D.N., and Christianson D.W. Protein Sci. 7 (1998) 556
23. Kim C.Y., Chang J.S., Doyon J.B., Baird T.T., Fierke C.A., Jain A., and Christianson D.W. J. Am. Chem. Soc. 122 (2000) 12125
24. Whittington D.A., Waheed A., Ulmasov B., Shah G.N., Grubb J.H., Sly W.S., and Christianson D.W. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 9545
25. Vidgren J., Svensson A., and Liljas A. Int. J. Biol. Macromol. 15 (1993) 97
26. Abbate F., Winum J.Y., Potter B.V., Casini A., Montero J.L., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 14 (2004) 231
27. Lloyd M.D., Pederick R.L., Natesh R., Woo L.W., Purohit A., Reed M.J., Acharya K.R., and Potter B.V. Biochem. J. 385 (2005) 715
28. Lloyd M.D., Thiyagarajan N., Ho Y.T., Woo L.W., Sutcliffe O.B., Purohit A., Reed M.J., Acharya K.R., and Potter B.V. Biochemistry 44 (2005) 6858
29. Leese M.P., Leblond B., Smith A., Newman S.P., Di Fiore A., De Simone G., Supuran C.T., Purohit A., Reed M.J., and Potter B.V.L. J. Med. Chem. 49 (2006) 7683
30. Gruneberg S., Stubbs M.T., and Klebe G. J. Med. Chem. 45 (2002) 3588
31. Casini A., Winum J.Y., Montero J.L., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 13 (2003) 837
32. Winum J.Y., Innocenti A., Nasr J., Montero J.L., Scozzafava A., Vullo D., and Supuran C.T. Bioorg. Med. Chem. Lett. 15 (2005) 2353
33. Winum J.Y., Cecchi A., Montero J.L., Innocenti A., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 15 (2005) 3302
34. Švastová E., Hulíková A., Rafajová M., Zatovicová M., Gibadulinová A., Casini A., Cecchi A., Scozzafava A., Supuran C.T., Pastorek J., and Pastoreková S. FEBS Lett. 577 (2004) 439
35. Nishimori I., Minakuchi T., Onishi S., Vullo D., Cecchi A., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. 15 (2007) 7229
36. 12-14.
37. 4 in 50 mM Tris-HCl pH 7.7-7.8 and 1 mM sodium 4-(hydroxymercury)benzoate) with added 50 mM EMD 486019 and equilibrated over a reservoir of 1 ml of precipitant buffer. Crystals were transferred into a cryoprotectant solution (20% ethylene glycol), mounted in nylon loop and exposed to a cold (100° K) nitrogen stream. Diffraction data were collected on a CCD Detector KM4 CCD/Sapphire using CuKα radiation (1.5418 Å). Data were processed with MOSFLM and the CCP4 suite.[19,20] The structure was analyzed by difference Fourier technique, using the PDB file 1BV3[21] as starting model for the refinement. Electron density maps (2Fo-Fc) and (Fo-Fc) were calculated with the REFMAC5 program[22] and displayed using the graphic program O.[23] The final model of the complex had an R-factor of 20.0%, R-free 25.0%, for 18403 reflections in the resolution range 10.0-1.90 Å with a rms deviation from standard geometry of 0.009 Å in bond lengths and 1.2° in bond angles.
38. Temperini C., Cecchi A., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 18 (2008) 2567
39. Di Fiore A., Pedone C., Antel J., Waldeck H., Witte A., Wurl M., Scozzafava A., Supuran C.T., and De Simone G. Bioorg. Med. Chem. Lett. 18 (2008) 2669
40. Leslie, A. G. W. MOSFLM users guide, MRC-LMB, 1994, Cambridge, UK.
41. Collaborative Computational Project, Number 4. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. Sect. D. 1994, 50, 760-763.
42. Eriksson A.E., Jones T.A., and Liljas A. Proteins Struct. Funct. 4 (1988) 274
43. Brunger A.T., Adams P.D., Clore G.M., Delano W.L., Gros P., Grosse-Kunsteleve R.W., Fiang J., Kuszewsky J., Niles M., Pannu N.S., Read R.J., Rice L.M., Simmonson T., and Warren G.L. Acta Crystallogr. Sect. D. 54 (1998) 905
44. Jones T.A., Zhou J.Y., Cowan S.W., and Kjeldgaard M. Acta Crystallogr. Sect. A 47 (1991) 110