Carbonic anhydrase inhibitors: Inhibition of the β-class enzymes from the fungal pathogens Candida albicans and Cryptococcus neoformans with simple anions

Bioorganic and Medicinal Chemistry Letters

Volumn 18, Issue 18, 2008, Pages 5066-5070

  Innocenti, Alessio ^a   Mühlschlegel, Fritz A ^b   Hall, Rebecca A ^b   Steegborn, Clemens ^c   Scozzafava, Andrea ^a   Supuran, Claudiu T ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b UNIVERSITY OF KENT   (United Kingdom)

^c RUHR UNIVERSITY BOCHUM   (Germany)

Author keywords

Carbonic anhydrases; Anions; Can2; Candida albicans; Cryptococcus neoformans; Fungal pathogens; Nce103

Indexed keywords

BENZENEBORONIC ACID; BICARBONATE; BISULFITE; CAN2 ENZYME; CARBON DIOXIDE; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE INHIBITOR; CARBONIC ACID; CYANIDE; FUNGAL ENZYME; HALOGENIDE DERIVATIVE; HYDROGEN SULFIDE; NCE103 ENZYME; NITRATE; NITRITE; PERCHLORATE; PSEUDOHALOGENIDE DERIVATIVE; SULFAMIC ACID; SULFATE; SULFUR ACID AMIDE; UNCLASSIFIED DRUG;

ARTICLE; CANDIDA ALBICANS; CATALYSIS; CONTROLLED STUDY; CRYPTOCOCCUS NEOFORMANS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; NONHUMAN;

ANIONS; CANDIDA ALBICANS; CARBONATES; CARBONIC ANHYDRASE INHIBITORS; CARBONIC ANHYDRASES; CRYPTOCOCCUS NEOFORMANS; HALOGENS; HUMANS; ISOENZYMES; MOLECULAR STRUCTURE; NITRATES; SULFATES; SULFIDES;

CANDIDA ALBICANS; FILOBASIDIELLA NEOFORMANS; FUNGI;

EID: 51549100007     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.07.122     Document Type: Article

References (47)

1. Supuran C.T. Nat. Rev. Drug. Discov. 7 (2008) 168
2. Tripp B.C., Smith K.S., and Ferry J.G. J. Biol. Chem. 276 (2001) 48615
3. In: Supuran C.T., Scozzafava A., and Conway J. (Eds). Carbonic Anhydrase-Its Inhibitors and Activators (2004), CRC Press, Boca Raton (FL), USA 1-376 and references cited therein.
4. Supuran C.T., Scozzafava A., and Casini A. Med. Res. Rev 23 (2003) 146
5. Supuran C.T. Carbonic anhydrases catalytic mechanism distribution and physiological roles. In: Supuran C.T., Scozzafava A., and Conway J. (Eds). Carbonic Anhydrase-Its Inhibitors and Activators (2004), CRC Press, Boca Raton (FL), USA 1-24
6. Innocenti A., Scozzafava A., Parkkila S., Puccetti L., De Simone G., and Supuran C.T. Bioorg. Med. Chem. Lett. 18 (2008) 2267
7. Supuran C.T., and Scozzafava A. Expert Opin. Ther. Pat. 12 (2002) 217-242
8. Scozzafava A., Mastrolorenzo A., and Supuran C.T. Expert Opin. Ther. Pat. 14 (2004) 667-702
9. Smith K.S., and Ferry J.G. FEMS Microbiol. Rev. 24 (2000) 335
10. Smith K.S., Jakubzick C., Whittam T.S., and Ferry J.G. Proc. Natl. Acad Sci. U.S.A. 96 (1999) 15185
11. So A.K., Espie G.S., Williams E.B., Shively J.M., Heinhorst S., and Cannon G.C. J. Bacteriol. 186 (2004) 623
12. Mitsuhashi S., Mizushima T., Yamashita E., Yamamoto M., Kumasaka T., Moriyama H., Ueki T., Miyachi S., and Tsukihara T. J. Biol. Chem. 275 (2000) 5521
13. Kimber M.S., and Pai E.F. EMBO J. 19 (2000) 1407
14. Cronk J.D., Endrizzi J.A., Cronk M.R., O'Neill J.W., and Zhang K.Y. Protein Sci. 10 (2001) 911
15. Xu Y., Feng L., Jeffrey P.D., Shi Y., and Morel F.M. Nature 452 (2008) 56
16. Cox E.H., McLendon G.L., Morel F.M., Lane T.W., Prince R.C., Pickering I.J., and George G.N. Biochemistry 39 (2000) 12128
17. Lane T.W., and Morel F.M. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 4627
18. Klengel T., Liang W.J., Chaloupka J., Ruoff C., Schropel K., Naglik J.R., Eckert S.E., Mogensen E.G., Haynes K., Tuite M.F., Levin L.R., Buck J., and Mühlschlegel F.A. Curr. Biol. 15 (2005) 2021
19. Bahn, Y.S.; Cox, G.M. Perfect J.R., and Heitman J. Curr. Biol 15 (2005) 2013
20. Mogensen E.G., Janbon G., Chaloupka J., Steegborn C., Fu M.S., Moyrand F., Klengel T., Pearson D.S., Geeves M.A., Buck J., Levin L.R., and Mühlschlegel F.A. Eukaryot. Cell 5 (2006) 103
21. Bahn Y.S., and Mühlschlegel F.A. Curr. Opin. Microbiol. 9 (2006) 572
22. Steegborn C., Litvin T.N., Levin L.R., Buck J., and Wu H. Nat. Struct. Mol. Biol. 12 (2005) 32
23. Fridkin S., and Jarvis W.R. Clin. Microbiol. Rev. 9 (1996) 499
24. Cannon R.D., Lamping E., Holmes A.R., Niimi K., Tanabe K., Niimi M., and Monk B.C. Microbiology 153 (2007) 3211
25. Powderly W.G. Curr. Infect. Dis. Rep. 2 (2000) 352
26. Abadi J., Nachman S., Kressel A.B., and Pirofski L. Clin. Infect. Dis. 28 (1999) 309
27. Janbon G. FEMS Yeast Res. 4 (2004) 765
28. Vullo D., Franchi M., Gallori E., Pastorek J., Scozzafava A., Pastorekova S., and Supuran C.T. J. Enzyme Inhib. Med. Chem. 18 (2003) 403
29. Franchi M., Vullo D., Gallori E., Antel J., Wurl M., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 13 (2003) 2857
30. Innocenti A., Lehtonen J.M., Parkkila S., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 14 (2004) 5435
31. Innocenti A., Vullo D., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 15 (2005) 567
32. Innocenti A., Zimmerman S., Ferry J.G., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 14 (2004) 4563
33. Zimmerman S., Innocenti A., Ferry J.G., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 14 (2004) 6001
34. Zimmerman S.A., Ferry J.G., and Supuran C.T. Curr. Top. Med. Chem. 7 (2007) 901
35. Nishimori I., Minakuchi T., Kohsaki T., Onishi S., Takeuchi H., Vullo D., Scozzafava A., and Supuran C.T. Bioorg. Med. Chem. Lett. 17 (2007) 3585
36. 8,9
37. 2 concentrations ranged from 1.7 to 17 mM for the determination of the kinetic parameters and inhibition constants. For each inhibitor at least six traces of the initial 5-10% of the reaction have been used for determining the initial velocity. The uncatalyzed rates were determined in the same manner and subtracted from the total observed rates. Stock solutions of inhibitor (100 mM) were prepared in distilled-deionized water and dilutions up to 0.01 μM were done thereafter with distilled-deionized water. Inhibitor and enzyme solutions were preincubated together for 15 min at room temperature prior to assay, in order to allow for the formation of the E-I complex. The inhibition constants were obtained by non-linear least-squares methods using PRISM 3, whereas the kinetic parameters for the uninhibited enzymes from Lineweaver-Burk plots, as reported earlier, Refs. 14, 15 and represent the mean from at least three different determinations.
38. Strop P., Smith K.S., Iverson T.M., Ferry J.G., and Rees D.C. J. Biol. Chem. 276 (2001) 10299
39. Smith K.S., and Ferry J.G. J. Bacteriol. 181 (1999) 6247
40. Smith K.S., Cosper N.J., Stalhandske C., Scott R.A., and Ferry J.G. J. Bacteriol. 182 (2000) 6605
41. Smith K.S., Ingram-Smith C., and Ferry J.G. J. Bacteriol. 184 (2002) 4240
42. Ilies M.A., and Banciu M.D. Nonsulfonamide carbonic anhydrase inhibitors. In: Supuran C.T., Scozzafava A., and Conway J. (Eds). Carbonic Anhydrase-Its Inhibitors and Activators (2004), CRC Press, Boca Raton (FL), USA 209
43. The sequence alignments were performed using the following web site http://www.ebi.ac.uk/Tools/clustalw/index.html.
44. Supuran C.T., and Scozzafava A. Matrix metalloproteinases (MMPs). In: Smith H.J., and Simons C. (Eds). Proteinase and Peptidase Inhibition Recent Potential Targets for Drug Development (2002), Taylor & Francis, London and New York 35-61
45. Supuran C.T., and Scozzafava A. Bioorg. Med. Chem. 15 (2007) 4336
46. Supuran C.T. Curr. Pharm. Des. 14 (2008) 603
47. Mastrolorenzo A., Rusconi S., Scozzafava A., Barbaro G., and Supuran C.T. Curr. Med. Chem. 14 (2007) 2734