Design and campaign synthesis of piperidine- and thiazole-based histone deacetylase inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 18, Issue 8, 2008, Pages 2580-2584

  Andrews, David M ^a   Stokes, Elaine S E ^a   Carr, Greg R ^a   Matusiak, Zbigniew S ^a   Roberts, Craig A ^a   Waring, Michael J ^a   Brady, Madeleine C ^a   Chresta, Christine M ^a   East, Simon J ^a  

^a ASTRAZENECA   (United Kingdom)

Author keywords

Anticancer; Benzamide; Deacetylase; HDAC; Histone

Indexed keywords

BENZAMIDE; HISTONE DEACETYLASE INHIBITOR; PIPERIDINE DERIVATIVE; POTASSIUM CHANNEL HERG; THIAZOLE DERIVATIVE;

AMINATION; ANIMAL EXPERIMENT; AREA UNDER THE CURVE; ARTICLE; CANCER INHIBITION; CONTROLLED STUDY; DOSE RESPONSE; DRUG BLOOD LEVEL; DRUG CONFORMATION; DRUG DESIGN; DRUG EFFICACY; DRUG HALF LIFE; DRUG POTENCY; DRUG SCREENING; DRUG SOLUBILITY; DRUG SYNTHESIS; HEART ARRHYTHMIA; HUMAN; HUMAN CELL; IN VIVO STUDY; LONG QT SYNDROME; NONHUMAN; PATCH CLAMP; REDUCTION KINETICS; SUZUKI REACTION; TUMOR; TUMOR XENOGRAFT;

ANIMALS; ANTINEOPLASTIC AGENTS; CELL LINE, TUMOR; CRYSTALLOGRAPHY, X-RAY; DOGS; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG DESIGN; ENZYME INHIBITORS; HISTONE DEACETYLASES; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PIPERIDINES; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; THIAZOLES; XENOGRAFT MODEL ANTITUMOR ASSAYS;

EID: 41949123642     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.03.041     Document Type: Article

References (26)

1. Beato M. J. Mol. Med. 74 (1996) 711
2. Wolffe A.P. Nature 387 (1997) 16
3. Grant S., Easley C., and Kirkpatrick P. Nat. Rev. Drug Disc. 6 (2007) 21
4. Marchion D.C., Bicaku E., Daud A.I., Sullivan D.M., and Munster P.N. Cancer Res. 65 (2005) 3815
5. Lindemann R.K., Gabrielli B., and Johnstone R.W. Cell Cycle 3 (2004) 779
6. Brittain D., Weinmann H., and Ottow E. Annu. Rep. Med. Chem. 42 (2007) 337
7. Suzuki T., Ando T., Tsuchiya K., Fukazawa N., Saito A., Mariko Y., Yamashita T., and Nakanishi O. J. Med. Chem. 42 (1999) 3001
8. Olsen E.A., Kim Y.H., Kuzel T.M., Pacheco T.R., Foss F.M., Parker S., Frankel S.R., Chen C., Ricker J.L., Arduino J.M., and Duvic M. J. Clin. Oncol. 25 (2007) 3109
9. O'Connor O.A., Heaney M.L., Schwartz L., Richardson S., Willim R., MacGregor-Cortelli B., Curly T., Moskowitz C., Portlock C., Horwitz S., Zelenetz A.D., Frankel S., Richon V., Marks P., and Kelly W.K. J. Clin. Oncol. 24 (2006) 166
10. Kelly W.K., Richon V.M., and O'Connor O. Clin. Cancer Res. 9 (2003) 3578
11. Kummar S., Gutierrez M., Gardner E.R., Donovan E., Hwang K., Chung E.J., Lee M.J., Maynard K., Kalnitskiy M., Chen A., Melillo G., Ryan Q.C., Conley B., Figg W.D., Trepel J.B., Zwiebel J., Doroshow J.H., and Murgo A.J. Clin. Cancer Res. 13 (2007) 5411
12. Paris, M.; Porcelloni, M.; Binaschi, M.; Fattori, D. J. Med. Chem., 2008. doi:10.1021/jm7011408.
13. Younes A., Fanale M., Pro B., McLaughlin P., Neelapu S., Fayad L., Wedgwood A., Dubay M., Backstrom J., and Martell R.E. J. Clin. Oncol. (Meeting Abstracts) 25 (2007) 8000
14. Kabanos T.A., and Tsangaris J.M. J. Coord. Chem. 13 (1984) 89
15. 50 values for HDAC enzyme inhibitors were determined by performing dose-response curves with individual compounds and determining the concentration of inhibitor producing 50% decrease in the maximal signal (no inhibitor control).
16. 50 values for HDAC inhibitors were determined by performing dose-response curves with individual compounds and determining the concentration of inhibitor producing 50% decrease in maximal signal (diluent control). For other examples of the use of HCT116 cells in the evaluation of HDAC inhibitors, see also:. Nagaoka Y., Maeda T., Kawai Y., Nakashima D., Oikawa T., Shimoke K., Ikeuchi T., Kuwajima H., and Uesato S. Eur. J. Med. Chem. 41 (2006) 697
17. Remiszewski S.W., Sambucetti L.C., Bair K.W., Bontempo J., Cesarz D., Chandramouli N., Chen R., Cheung M., Cornell-Kennon S., Dean K., France G.D., Green M.A., Howell K.L., Kashi R., Kwon P., Lassota P., Martin M.S., Mou Y., Perez L.B., Sharma S., Smith T., Sorensen E., Taplin F., Trogani N., Versace R., Walker H., Weltchek-Engler S., Wood A., Wu A., and Atadja P. J. Med. Chem. 46 (2003) 4609
18. Kim D.-K., Lee J.Y., Kim J.-S., Ryu J.-H., Choi J.-Y., Lee J.W., Im G.-J., Kim T.-K., Seo J.W., Park H.-J., Yoo J., Park J.-H., Kim T.-Y., and Bang Y.-J. J. Med. Chem. 46 (2003) 5745
19. Moradei O.M., Mallais T.C., Frechette S., Paquin I., Tessier P.E., Leit S.M., Fournel M., Bonfils C., Trachy-Bourget M.-C., Liu J., Yan T.P., Lu A.-H., Rahil J., Wang J., Lefebvre S., Li Z., Vaisburg A.F., and Besterman J.M. J. Med. Chem. 50 (2007) 5543
20. Finnin M.S., Donigian J.R., Cohen A., Richon V.M., Rifkind R.A., Marks P.A., Breslow R., and Pavletich N.P. Nature 401 (1999) 188
21. 2) was mixed with either buffer alone (10 μL) or buffer containing compound (10 μL) for 30 min at ambient temperature. The reaction was initiated by addition of 25 μL of acetylated histone H4 peptide (25 μM) (KI 174 Biomol) diluted in buffer and incubated for one hour at ambient temperature. The remaining protocol is as for the pooled enzyme (vide supra).
22. Andrews, D. M.; Gibson, K. M.; Graham, M. A.; Matusiak, Z. M.; Roberts, C. A.; Stokes, E. S. E.; Brady, M. C.; Chresta C. M. Bioorg. Med. Chem. Lett., in press.
23. Eastwood P.R. Tetrahedron Lett. 41 (2000) 3705
24. Thai K.-M., and Ecker G.F. Bioorg. Med. Chem. 18 (2008) 1359
25. Schroeder K., Neagle B., Trezise D.J., and Worley J. J. Biomol. Screen. 8 (2003) 50
26. + 457.