Cis-configured aziridines are new pseudo-irreversible dual-mode inhibitors of Candida albicans secreted aspartic protease 2

ChemMedChem

Volumn 3, Issue 2, 2008, Pages 302-315

  Degel, Björn ^a   Staib, Peter ^a,c   Rohrer, Sebastian ^a,b   Scheiber, Josef ^a   Martina, Erika ^a   Büchold, Christian ^a   Baumann, Knut ^a,b   Morschhüser, Joachim ^a   Schirmeister, Tanja ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

^b TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^c LAUSANNE UNIVERSITY HOSPITAL   (Switzerland)

Author keywords

Aspartic proteases; Aziridines; Candida albicans; Epoxides; Inhibitors

Indexed keywords

AMINO ACID; AMINOALCOHOL; ANTIFUNGAL AGENT; ASPARTIC PROTEINASE; AZIRIDINE DERIVATIVE; CYSTEINE PROTEINASE INHIBITOR; EPOXIDE; FUNGAL PROTEIN; SAP2 PROTEIN, CANDIDA;

ARTICLE; BINDING SITE; CANDIDA ALBICANS; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; ENZYME SPECIFICITY; ENZYMOLOGY; HYDROLYSIS; HYDROPHOBICITY; KINETICS; METABOLISM; PH; STEREOISOMERISM; SYNTHESIS; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; AMINO ALCOHOLS; ANTIFUNGAL AGENTS; ASPARTIC ENDOPEPTIDASES; AZIRIDINES; BINDING SITES; CANDIDA ALBICANS; CRYSTALLOGRAPHY, X-RAY; CYSTEINE PROTEINASE INHIBITORS; EPOXY COMPOUNDS; FUNGAL PROTEINS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; HYDROPHOBICITY; KINETICS; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 45449097623     PISSN: 18607179     EISSN: 18607187     Source Type: Journal    
DOI: 10.1002/cmdc.200700101     Document Type: Article

References (74)

1. M. Nucci, K. A. Marr, Clin. Infect. Dis. 2005, 41, 521-526.
2. M. D. Richardson, J. Antimicrob. Chemother. 2005, 56, i5-i11.
3. K. Stewart, C. Abad-Zapatero, Curr. Med. Chem. 2001, 8, 941-948.
4. J. R. Naglik, S. J. Challacombe, B. Hube, Microbiol. Mol. Biol. Rev. 2003, 67, 400-428.
5. S. M. Cutfield, E. J. Dodson, B. F. Anderson, P. C. Moody, C. J. Marshall, P. A. Sullivan, J. F. Cutfield, Structure 1995, 3, 1261-1271.
6. C. Abad-Zapatero, R. Goldman, S. W. Muchmore, C. Hutchins, K. Stewart, J. Navaza, C. D. Payne, T. L. Ray, Protein Sci. 1996, 5, 640-652.
7. I. Pichova, L. Pavlickova, J. Dostal, E. Dolejsi, O. Hruskova- Heidingsfeldova, J. Weber, T. Ruml, M. Soucek, Eur. J. Biochem. 2001, 268, 2669-2677.
8. D. Backman, U. H. Danielson, Biochim. Biophys. Acta Proteins Proteomics 2003, 1646, 184-195.
9. A. Tossi, F. Benedetti, S. Norbedo, D. Skrbec, F. Berti, D. Romeo, Bioorg. Med. Chem. 2003, 11, 4719-4727.
10. C. Abad-Zapatero, R. Goldman, S. W. Muchmore, C. Hutchins, T. Oie, K. Stewart, S. M. Cutfield, J. F. Cutfield, S. I. Foundling, T. L. Ray, Adv. Exp. Med. Biol. 1998, 436, 297-313.
11. S. K. Pranav Kumar, V. M. Kulkarni, Bioorg. Med. Chem. 2002, 10, 1153-1170.
12. M. C. Bursavich, D. H. Rich, J. Med. Chem. 2002, 45, 541-558.
13. B. M. Dunn, Chem. Rev. 2002, 102, 4431-4458.
14. K. C. S. Chen, J. Tang, J. Biol. Chem. 1972, 247, 2566-2574.
15. R. B. Rose, J. R. Rose, R. Salto, C. S. Craik, R. M. Stroud, Biochemistry 1993, 32, 12498-12507.
16. R. Salto, L. M. Babe, J. Li, J. R. Rose, Z. Yu, A. Burlingame, J. J. De Voss, Z. Sui, P. Ortiz de Montellano, C. S. Craik, J. Biol. Chem. 1994, 269, 10691-10698.
17. C. S. Lee, N. Choy, C. Park, H. Choi, Y. C. Son, S. Kim, J. H. Ok, H. Yoon, S. C. Kim, Bioorg. Med. Chem. Lett. 1996, 6, 589-594.
18. Z. Yu, P. Caldera, F. McPhee, J. J. De Voss, P. R. Jones, A. L. Burlingame, I. D. Kuntz, C. S. Craik, P. R. Ortiz de Montellano, J. Am. Chem. Soc. 1996, 118, 5846-5856.
19. S. Ro, S.-G. Baek, B. Lee, J. H. Ok, J. Pept. Res. 1999, 54, 242-248.
20. A. D. Abell, D. A. Hoult, D. A. Bergman, D. P. Fairlie, Bioorg. Med. Chem. Lett. 1997, 7, 2853-2856.
21. C. Park, J. S. Koh, Y. C. Son, H. Choi, C. S. Lee, N. Choy, K. Y. Moon, W. H. Jung, S. C. Kim, H. Yoon, Bioorg. Med. Chem. Lett. 1995, 5, 1843-1848.
22. S. K. Grant, M. L. Moore, S. A. Fakhoury, T. A. Tomaszek, Jr., T. D. Meek, Bioorg. Med. Chem. Lett. 1992, 2, 1441-1445.
23. P. S. Caldera, Z. Yu, R. M. A. Knegtel, F. McPhee, A. L. Burlingame, C. S. Craik, I. D. Kuntz, P. R. Ortiz de Montellano, Bioorg. Med. Chem. 1997, 5, 2019-2027.
24. S. C. Piper, Z. Amtul, L. Galinanes-Garcia, V. G. Howard, C. Ziani-Cherif, C. McLendon, M. J. Rochette, A. Fauq, T. E. Golde, M. P. Murphy, Biochem. Biophys. Res. Commun. 2003, 305, 529-533.
25. J. C. Powers, J. L. Asgian, O. D. Ekici, K. E. James, Chem. Rev. 2002, 102, 4639-4750.
26. R. Vicik, V. Hoerr, M. Glaser, M. Schultheis, E. Hansell, J. H. McKerrow, U. Holzgrabe, C. R. Caffrey, A. Ponte-Sucre, H. Moll, A. Stich, T. Schirmeister, Bioorg. Med. Chem. Lett. 2006, 16, 2753-2757.
27. a) C. Clark, P. Hermans, O. Methcohn, C. Moore, H. C. Taljaard, G. J. Vanvuuren, Chem. Soc. Chem. Commun. 1986, 1378-1380;
28. b) O. Meth-Cohn, C. Moore, H. C. Taljaard, J. Chem. Soc. Perkin Trans. 1 1988, 2663-2674.
29. D. Häbich, W. Hartwig, Tetrahedron Lett. 1987, 28, 781-784.
30. a) K. Ando, T. Oishi, M. Hirama, H. Ohno, T. Ibuka, J. Org. Chem. 2000, 65, 4745-4749;
31. b) P. M. Pihko, T. M. Salo, Tetrahedron Lett. 2003, 44, 4361-4364.
32. K. J. Ando, J. Org. Chem. 1997, 62, 1934-1939.
33. a) A. Jenmalm, W. Berts, Y. L. Li, K. Luthman, I. Croregh, U. Hacksell, J. Org. Chem. 1994, 59, 1139-1148;
34. b) D. Scholz, A. Billich, B. Charpiot, P. Ettmayer, P. Lehr, B. Rosenwirth, E. Schreiner, H. Gstach, J. Med. Chem. 1994, 37, 3079-3089.
35. a) J. M. Domagala, R. D. Bach, J. Org. Chem. 1979, 44, 3168-3174;
36. b) K. Kimata, M. Kobayashi, K. Hosoya, T. Araki, N. Tanaka, J. Am. Chem. Soc. 1996, 118, 759-762.
37. a) P. Davoli, A. Forni, I. Moretti, F. Prati, G. Torre, Tetrahedron 2001, 57, 1801-1812;
38. b) P. Davoli, I. Moretti, F. Prati, H. J. Alper, J. Org. Chem. 1999, 64, 518-521.
39. K. Mori, H. Iwasawa, Tetrahedron 1980, 36, 87-90.
40. F. B. Charvillon, R. Amouroux, Synth. Commun. 1997, 27, 395-403.
41. P. Pöchlauer, E. P. Muller, P. Peringer, Helv. Chim. Acta 1984, 67, 1238-1247.
42. a) M. Rodriguez, M. Llinares, S. Doulut, A. Heitz, J. Martinez, Tetrahedron Lett. 1991, 32, 923-926;
43. b) M. Ihara, A. Katsumata, F. Setsu, Y. Tokunaga, K. Fukumoto, J. Org. Chem. 1996, 61, 677-684;
44. c) E. Medina, A. Moyano, M. A. Pericas, A. J. Riera, J. Org. Chem. 1998, 63, 8574-8578;
45. d) T. Isobe, K. Fukuda, K. Yamaguchi, H. Seki, T. Tokunaga, T. Ishikawa, J. Org. Chem. 2000, 65, 7779-7785.
46. G. Koelsch, J. Tang, J. A. Loy, M. Monod, K. Jackson, S. I. Foundling, X. L. Lin, Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 2000, 1480, 117-131.
47. M. Fusek, E. A. Smith, M. Monod, B. Dunn, S. I. Foundling, Biochemistry 1994, 33, 9791-9799.
48. D. Skrbec, D. Romeo, Biochem. Biophys. Res. Commun. 2002, 297, 1350-1353.
49. N. Goldfarb, M. T. Lam, A. K. Bose, A. M. Patel, A. J. Duckworth, B. M. Dunn, Biochemistry 2005, 44, 15725-15733.
50. B. Hube, M. Monod, D. A. Schofield, A. J. Brown, N. A. Gow, Mol. Microbiol. 1994, 14, 87-99.
51. B. Hube, D. Sanglard, F. C. Odds, D. Hess, M. Monod, W. Schafer, A. J. Brown, N. A. Gow, Infect. Immunol. 1997, 65, 3529-3538.
52. P. Staib, M. Kretschmar, T. Nichterlein, H. Hof, J. Morschhäuser, Mol. Microbiol. 2002, 44, 1351-1366.
53. 50 of 0.042 mm against SAP2.
54. L. J. Copp in Enzyme Kinetics, a Modern Approach (Ed.: E. G. Marangoni), Wiley, New York, 2003, ch. 13, p. 158-173.
55. H. Helten, T. Schirmeister, B. Engels, J. Phys. Chem. A 2004, 108, 7691-7701.
56. a) V. Martichonok, C. Plouffe, A. Storer, R. Menard, J. B. Jones, J. Med. Chem. 1995, 38, 3078-3085;
57. b) T. Schirmeister, M. Peric, Bioorg. Med. Chem. 2000, 8, 1281-1291.
58. Glide, Schrödinger, LLC, New York, NY, USA, 2007.
59. MOE Molecular Operating Environment, Chemical Computing Group, Inc., Montreal, Canada, 2006.
60. A. J. Barrett, N. D. Rawlings, Biol. Chem. 2001, 382, 727-733.
61. R. Kitz, I. B. Wilson, J. Biol. Chem. 1962, 237, 3245-3249.
62. P. J. F. Henderson, Biochem. J. 1972, 127, 321-333.
63. Y. Y. Liu, W. Kati, C. M. Chen, R. Tripathi, A. Molla, W. Kohlbrenner, Anal. Biochem. 1999, 267, 331-335.
64. GraFit, Version 5.0.13, Erithacus Software Ltd., London, UK, 2006.
65. K. Inouye, J. Fruton, Biochemistry 1967, 6, 1765-1777.
66. R. Vicik, M. Busemann, C. Gelhaus, N. Stiefl, J. Scheiber, W. Schmitz, F. Schulz, M. Mladenovic, B. Engels, M. Leippe, K. Baumann, T. Schirmeister, ChemMedChem 2006, 1, 1126-1141.
67. Marvin Sketch, ChemAxon Kft., Budapest, Hungary, 2006.
68. CTFile Formats, MDL Information Systems, Inc., San Ramon, CA, USA, 2005.
69. LigPrep, Schrödinger, LLC, New York, NY, USA, 2005.
70. Maestro, Schrödinger, LLC, New York, NY, USA, 2007.
71. VIDA2, OpenEye Scientific Software, Inc., Santa Fe, NM, USA, 2006.
72. J. O. Capobianco, C. G. Lerner, R. C. Goldman, Anal. Biochem. 1992, 204, 96-102.
73. M. Fusek, E. A. Smith, M. Monod, B. M. Dunn, S. I. Foundling, Biochemistry 1994, 33, 9791-9799.
74. Assays with 10 and 20 μm inhibitor showed that the percentage of residual enzyme activity remained constant at ∼70% over a period of 140 min.