Identification of a potent non-hydroxamate histone deacetylase inhibitor by mechanism-based drug design

Bioorganic and Medicinal Chemistry Letters

Volumn 15, Issue 2, 2005, Pages 331-335

  Suzuki, Takayoshi ^a   Matsuura, Azusa ^a   Kouketsu, Akiyasu ^a   Nakagawa, Hidehiko ^a   Miyata, Naoki ^a  

^a NAGOYA CITY UNIVERSITY   (Japan)

Author keywords

Histone deacetylase inhibitor; Non hydroxamate

Indexed keywords

HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID DERIVATIVE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DEACETYLATION; DRUG DESIGN; DRUG IDENTIFICATION; DRUG MECHANISM; DRUG POTENCY; DRUG STRUCTURE; DRUG SYNTHESIS; ENZYME ASSAY; ENZYME DEGRADATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; MOLECULAR INTERACTION; MOLECULAR MODEL; REACTION ANALYSIS; STRUCTURE ANALYSIS;

ACETAMIDES; ACETYLATION; BINDING SITES; ENZYME INHIBITORS; HISTONE DEACETYLASES; HYDROXAMIC ACIDS; KINETICS; MODELS, MOLECULAR; STRUCTURE-ACTIVITY RELATIONSHIP; SULFHYDRYL COMPOUNDS; ZINC;

EID: 10644239808     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2004.10.074     Document Type: Article

References (25)

1. C.M. Grozinger, and S.L. Schreiber Chem. Biol. 9 2002 3
2. C.A. Hassig, and S.L. Schreiber Curr. Opin. Chem. Biol. 1 1997 300
3. J. Taunton, C.A. Hassig, and S.L. Schreiber Science 272 1996 408
4. M. Yoshida, S. Horinouchi, and T. Beppu BioEssays 17 1995 423
5. V.M. Richon, Y. Webb, R. Merger, T. Sheppard, B. Jursic, L. Ngo, F. Civoli, R. Breslow, R.A. Rifkind, and P.A. Marks Proc. Natl. Acad. Sci. U.S.A. 93 1996 5705
6. V.M. Richon, S. Emiliani, E. Verdin, Y. Webb, R. Breslow, R.A. Rifkind, and P.A. Marks Proc. Natl. Acad. Sci. U.S.A. 95 1998 3003
7. L.A. Cohen, S. Amin, P.A. Marks, R.A. Rifkind, D. Desai, and V.M. Richon Anticancer Res. 19 1999 4999
8. For a review, see: T.A. Miller, D.J. Witter, and S. Belvedere J. Med. Chem. 46 2003 5097
9. M.S. Finnin, J.R. Donigian, A. Cohen, V.M. Richon, R.A. Rifkind, P.A. Marks, R. Breslow, and N.P. Pavletich Nature 401 1999 188
10. J.R. Somoza, R.J. Skene, B.A. Katz, C. Mol, J.D. Ho, A.J. Jennings, C. Luong, A. Arvai, J.J. Buggy, E. Chi, J. Tang, B.-C. Sang, E. Verner, R. Wynands, E.M. Leahy, D.R. Dougan, G. Snell, M. Navre, M.W. Knuth, R.V. Swanson, D.E. McRee, and L.W. Tari Structure 12 2004 1325
11. G.J. Mulder, and J.H. Meerman Environ. Health Perspect. 49 1983 27
12. S. Vassiliou, A. Mucha, P. Cuniasse, D. Georgiadis, K. Lucet-Levannier, F. Beau, R. Kannan, G. Murphy, V. Knaeuper, M.C. Rio, P. Basset, A. Yiotakis, and V. Dive J. Med. Chem. 42 1999 2610
13. A. Mai, S. Massa, R. Rango, I. Cerbara, F. Jesacher, P. Loidl, and G. Brosch J. Med. Chem. 46 2003 512
14. T. Suzuki, Y. Nagano, A. Matsuura, A. Kohara, S. Ninomiya, K. Kohda, and N. Miyata Bioorg. Med. Chem. Lett. 13 2003 4321
15. T.Y.H. Wu, C. Hassig, Y. Wu, S. Ding, and P.G. Schultz Bioorg. Med. Chem. Lett. 14 2004 449
16. D.W. Christianson, and W.N. Lipscomb Acc. Chem. Res. 22 1989 62
17. G.V. Kapstin, G. Fejer, J.L. Gronlund, D.G. McCafferty, E. Seto, and F.A. Etzkorn Org. Lett. 5 2003 3053
18. W.J. Moree, G.A. van der Marel, and R.M.J. Liskamp Tetrahedron Lett. 32 1991 409
19. The HDAC activity assay was performed using an HDAC fluorescent activity assay/drug discovery kit (AK-500, BIOMOL Research Laboratories): HeLa Nuclear Extracts (0.5 μl/well) were incubated (37°C) with 25 μM of Fluor de Lys™ substrate and various concentrations of samples. Reactions were stopped after 30 min. with Fluor de Lys™ Developer and fluorescence was measured on a fluorometric reader with excitation set at 360 nm and emission detection set at 460 nm
20. The reason that compounds 3 and 4 were inactive is unclear, but it is probably because the amino group of 3 is not able to chelate zinc ion due to the protonation under the assay conditions, and because the zinc-chelating ability of hydroxyl group (4) is less than that of sulfhydryl group (5b)
21. C.K. Wada, R.R. Frey, Z. Ji, M.L. Curtin, R.B. Garland, J.H. Holms, J. Li, L.J. Pease, J. Guo, K.B. Glaser, P.A. Marcotte, P.L. Richardson, S.S. Murphy, J.J. Bouska, P. Tapang, T.J. Magoc, D.H. Albert, S.K. Davidsen, and M.R. Michaelides Bioorg. Med. Chem. Lett. 13 2003 3331
22. T. Suzuki, A. Kouketsu, A. Matsuura, A. Kohara, S. Ninomiya, K. Kohda, and N. Miyata Bioorg. Med. Chem. Lett. 14 2004 3313
23. N.A. Rizvi, J.S. Humphrey, E.A. Ness, M.D. Johnson, E. Gupta, K. Williams, D.J. Daly, D. Sonnichsen, D. Conway, J. Marshall, and H. Hurwitz Clin. Cancer Res. 10 2004 1963
24. A.D. Baxter, J. Bird, R. Bhogal, T. Massil, K.J. Minton, J. Montana, and D.A. Owen Bioorg. Med. Chem. Lett. 7 1997 897
25. A. Mai, M. Esposito, G. Sbardella, and S. Massa Org. Prep. Proced. Int. 33 2001 391