Design, synthesis, and biological evaluation of 1, 3-disubstituted-pyrazole derivatives as new class i and IIb histone deacetylase inhibitors

European Journal of Medicinal Chemistry

Volumn 86, Issue , 2014, Pages 639-652

  Yao, Yiwu ^a   Liao, Chenzhong ^b   Li, Zheng ^c   Wang, Zhen ^a   Sun, Qiao ^a   Liu, Chunping ^a   Yang, Yang ^b   Tu, Zhengchao ^a   Jiang, Sheng ^a  

^a GUANGZHOU INSTITUTES OF BIOMEDICINE AND HEALTH   (China)

^b HEFEI UNIVERSITY OF TECHNOLOGY   (China)

^c HOUSTON METHODIST RESEARCH INSTITUTE   (United States)

Author keywords

HDAC; Isoforms selectivity; Scaffold hopping; Structureeactivity relationship

Indexed keywords

5 (1 BENZYL 1H PYRAZOL 3 YL) N HYDROXYPENTANAMIDE; 5 [1 (4 BROMOBENZYL) 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; 5 [1 (4 FLUOROBENZYL) 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; 5 [1 [(1,1' BIPHENYL) 3 YLMETHYL] 1H IMIDAZOL 2 YL] N HYDROXYPENTANAMIDE; 5 [1 [(1,1' BIPHENYL) 3 YLMETHYL] 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; 5 [1 [(1,1' BIPHENYL) 3 YLMETHYL] 1H PYRAZOL 4 YL] N HYDROXYPENTANAMIDE; 5 [1 [(1,1' BIPHENYL) 3 YLMETHYL] 1H PYRAZOL 5 YL] N HYDROXYPENTANAMIDE; 5 [1 [(1,1' BIPHENYL) 3 YLMETHYL] 1H PYRROL 2 YL] N HYDROXYPENTANAMIDE; 5 [1 [(1,1' BIPHENYL) 4 YLMETHYL] 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; 5 [1 [4 (1H INDOL 1 YL)BENZYL] 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; 5 [1 [4 (BENZYLOXY)BENZYL] 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; 5 [1 [4 (TERT BUTYL)BENZYL] 1H PYRAZOL 3 YL] N HYDROXYPENTANAMIDE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 2B; HISTONE DEACETYLASE INHIBITOR; MOLECULAR SCAFFOLD; N HYDROXY 5 (1 PHENYL 1H PYRAZOL 3 YL)PENTANAMIDE; N HYDROXY 5 (5H IMIDAZO[5,1 A]ISOINDOL 3 YL) PENTANAMIDE; N HYDROXY 5 (5H PYRROLO[2,1 A]ISOINDOL 3 YL) PENTANAMIDE; N HYDROXY 5 [1 (4 METHYLBENZYL) 1H PYRAZOL 3 YL] PENTANAMIDE; N HYDROXY 5 [1 (4 MORPHOLINOBENZYL) 1H PYRAZOL 3 YL]PENTANAMIDE; N HYDROXY 5 [1 (4 NITROBENZYL) 1H PYRAZOL 3 YL]PENTANAMIDE; N HYDROXY 5 [1 (4 PHENOXYBENZYL) 1H PYRAZOL 3 YL]PENTANAMIDE; N HYDROXY 5 [1 [3 (PHENYLAMINO)BENZYL] 1H PYRAZOL 3 YL)PENTANAMIDE; N HYDROXY 5 [1 [4 (PHENYLAMINO)BENZYL] 1H PYRAZOL 3 YL]PENTANAMIDE; N HYDROXY 5 [1 [4 (TRIFLUOROMETHYL)BENZYL] 1H PYRAZOL 3 YL]PENTANAMIDE; PYRAZOLE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VORINOSTAT; ANTINEOPLASTIC AGENT; PYRAZOLE;

ANTINEOPLASTIC ACTIVITY; ANTIPROLIFERATIVE ACTIVITY; ARTICLE; CANCER CELL LINE; CELL MEDIATED CYTOTOXICITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEPROTONATION; DRUG DESIGN; DRUG SCREENING; DRUG SELECTIVITY; DRUG STRUCTURE; DRUG SYNTHESIS; HUMAN; HUMAN CELL; HYDROGEN BOND; IC50; MOLECULAR DOCKING; MOLECULAR MODEL; PROTON TRANSPORT; WESTERN BLOTTING; ANTAGONISTS AND INHIBITORS; CELL PROLIFERATION; CELL SURVIVAL; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; DRUG EFFECTS; HELA CELL LINE; K562 CELL LINE; MCF 7 CELL LINE; METABOLISM; STRUCTURE ACTIVITY RELATION; SYNTHESIS; TUMOR CELL CULTURE; U937 CELL LINE; X RAY CRYSTALLOGRAPHY;

ANTINEOPLASTIC AGENTS; CELL PROLIFERATION; CELL SURVIVAL; CRYSTALLOGRAPHY, X-RAY; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG DESIGN; DRUG SCREENING ASSAYS, ANTITUMOR; HELA CELLS; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE INHIBITORS; HUMANS; K562 CELLS; MCF-7 CELLS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PYRAZOLES; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR CELLS, CULTURED; U937 CELLS;

EID: 84907859411     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2014.09.024     Document Type: Article

References (40)

1. C.B. Yoo, P.A. Jones, Epigenetic therapy of cancer: past, present and future, Nat. Rev. Drug Discov. 5 (2006) 37e50.
2. G. Giannini, W. Cabri, C. Fattorusso, M. Rodriquez, Histone deacetylase inhibitors in the treatment of cancer: overview and perspectives, Future Med. Chem. 4 (2012) 1439e1460.
3. P. Marks, R.A. Rifkind, V.M. Richon, R. Breslow, T. Miller, W.K. Kelly, Histone deacetylases and cancer: causes and therapies, Nat. Rev. Cancer 1 (2001) 194e202.
4. R.W. Johnstone, Histone-deacetylase inhibitors: novel drugs for the treatment of cancer, Nat. Rev. Drug Discov. 1 (2002) 287e299.
5. A.J. de Ruijter, A.H. van Gennip, H.N. Caron, S. Kemp, A.B. van Kuilenburg, Histone deacetylases (HDACs): characterization of the classical HDAC family, Biochem. J. 370 (2003) 737e749.
6. P. Bertrand, Inside HDAC with HDAC inhibitors, Eur. J. Med. Chem. 45 (2010) 2095e2116.
7. W. Weichert, A. Roske, V. Gekeler, T. Beckers, C. Stephan, K. Jung, F.R. Fritzsche, S. Niesporek, C. Denkert, M. Dietel, G. Kristiansen, Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy, Br. J. Cancer 98 (2008) 604e610.
8. W. Weichert, A. Roske, S. Niesporek, A. Noske, A.C. Buckendahl, M. Dietel, V. Gekeler, M. Boehm, T. Beckers, C. Denkert, Class I histone deacetylase expression has independent prognostic impact in human colorectal cancer: specific role of class I histone deacetylases in vitro and in vivo, Clin. Cancer Res. 14 (2008) 1669e1677.
9. T. Rikimaru, A. Taketomi, Y. Yamashita, K. Shirabe, T. Hamatsu, M. Shimada, Y. Maehara, Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma, Oncology 72 (2007) 69e74.
10. K. Miyake, T. Yoshizumi, S. Imura, K. Sugimoto, E. Batmunkh, H. Kanemura, Y. Morine, M. Shimada, Expression of hypoxia-inducible factor-1alpha, histone deacetylase 1, and metastasis-associated protein 1 in pancreatic carcinoma: correlation with poor prognosis with possible regulation, Pancreas 36 (2008) e1e9.
11. W. Weichert, HDAC expression and clinical prognosis in human malignancies, Cancer Lett. 280 (2009) 168e176.
12. S. Ropero, M. Esteller, The role of histone deacetylases (HDACs) in human cancer, Mol. Oncol. 1 (2007) 19e25.
13. S. Grant, C. Easley, P. Kirkpatrick, Vorinostat, Nat. Rev. Drug Discov. 6 (2007) 21e22.
14. S. Minucci, P.G. Pelicci, Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer, Nat. Rev. Cancer 6 (2006) 38e51.
15. M. Paris, M. Porcelloni, M. Binaschi, D. Fattori, Histone deacetylase inhibitors: from bench to clinic, J. Med. Chem. 51 (2008) 1505e1529.
16. C.H. Arrowsmith, C. Bountra, P.V. Fish, K. Lee, M. Schapira, Epigenetic protein families: a new frontier for drug discovery, Nat. Rev. Drug Discov. 11 (2012) 384e400.
17. O. Bruserud, C. Stapnes, E. Ersvaer, B.T. Gjertsen, A. Ryningen, Histone deacetylase inhibitors in cancer treatment: a review of the clinical toxicity and the modulation of gene expression in cancer cell, Curr. Pharm. Biotechnol. 8 (2007) 388e400.
18. K.T. Thurn, S. Thomas, A. Moore, P.N. Munster, Rational therapeutic combinations with histone deacetylase inhibitors for the treatment of cancer, Future Oncol. 7 (2011) 263e283.
19. N. Noureen, H. Rashid, S. Kalsoom, Identification of type-specific anticancer histone deacetylase inhibitors: road to success, Cancer Chemother. Pharmacol. 66 (2010) 625e633.
20. A.P. Kozikowski, S. Tapadar, D.N. Luchini, K.H. Kim, D.D. Billadeau, Use of the nitrile oxide cycloaddition (NOC) reaction for molecular probe generation: a new class of enzyme selective histone deacetylase inhibitors (HDACIs) showing picomolar activity at HDAC6, J. Med. Chem. 51 (2008) 4370e4373.
21. C. Salmi-Smail, A. Fabre, F. Dequiedt, A. Restouin, R. Castellano, S. Garbit, P. Roche, X. Morelli, J.M. Brunel, Y. Collette, Modified cap group suberoylanilide hydroxamic acid histone deacetylase inhibitor derivatives reveal improved selective antileukemic activity, J. Med. Chem. 53 (2010) 3038e3047.
22. Y. Zhang, H. Fang, J. Feng, Y. Jia, X. Wang, W. Xu, Discovery of a tetrahydroisoquinoline-based hydroxamic acid derivative (ZYJ-34c) as histone deacetylase inhibitor with potent oral antitumor activities, J. Med. Chem. 54 (2011) 5532e5539.
23. D. Moffat, S. Patel, F. Day, A. Belfield, A. Donald, M. Rowlands, J. Wibawa, D. Brotherton, L. Stimson, V. Clark, J. Owen, L. Bawden, G. Box, E. Bone, P. Mortenson, A. Hardcastle, S. van Meurs, S. Eccles, F. Raynaud, W. Aherne, Discovery of 2-(6-{ [(6-fluoroquinolin-2-yl)methyl]amino}bicyclo [3.1.0]hex-3-yl)-N-hydroxypyrim idine-5-carboxamide (CHR-3996), a class I selective orally active histone deacetylase inhibitor, J. Med. Chem. 53 2010) 8663e8678.
24. X. Zeng, B. Yin, Z. Hu, C. Liao, J. Liu, S. Li, Z. Li, M.C. Nicklaus, G. Zhou, S. Jiang, Total synthesis and biological evaluation of largazole and derivatives with promising selectivity for cancers cells, Org. Lett. 12 (2010) 1368e1371.
25. X. Li, Z. Tu, H. Li, C. Liu, Z. Li, Q. Sun, Y. Yao, J. Liu, S. Jiang, Biological evaluation of new largazole analogues: alteration of macrocyclic scaffold with click chemistry, ACS Med. Chem. Lett. 4 (2012) 132e136.
26. J. Hou, Z. Li, Q. Fang, C. Feng, H. Zhang, W. Guo, H. Wang, G. Gu, Y. Tian, P. Liu, R. Liu, J. Lin, Y.K. Shi, Z. Yin, J. Shen, P.G. Wang, Discovery and extensive in vitro evaluations of NK-HDAC-1: a chiral histone deacetylase inhibitor as a promising lead, J. Med. Chem. 55 (2012) 3066e3075.
27. C. Blackburn, C. Barrett, J. Chin, K. Garcia, K. Gigstad, A. Gould, J. Gutierrez, S. Harrison, K. Hoar, C. Lynch, R.S. Rowland, C. Tsu, J. Ringeling, H. Xu, Potent histone deacetylase inhibitors derived from 4-(aminomethyl)-N-hydroxybenzamide with high selectivity for the HDAC6 isoform, J. Med. Chem. 56 (2013) 7201e7211.
28. C.W. Yu, P.T. Chang, L.W. Hsin, J.W. Chern, Quinazolin-4-one derivatives as selective histone deacetylase-6 inhibitors for the treatment of Alzheimer's disease, J. Med. Chem. 56 (2013) 6775e6791.
29. C.M. Marson, C.J. Matthews, E. Yiannaki, S.J. Atkinson, P.E. Soden, L. Shukla, N. Lamadema, N.S. Thomas, Discovery of potent, isoform-selective inhibitors of histone deacetylase containing chiral heterocyclic capping groups and a N-(2-aminophenyl)benzamide binding unit, J. Med. Chem. 56 (2013) 6156e6174.
30. D.E. Olson, F.F. Wagner, T. Kaya, J.P. Gale, N. Aidoud, E.L. Davoine, F. Lazzaro, M. Weiwer, Y.L. Zhang, E.B. Holson, Discovery of the first histone deacetylase 6/8 dual inhibitors, J. Med. Chem. 56 (2013) 4816e4820.
31. F.F. Wagner, D.E. Olson, J.P. Gale, T. Kaya, M. Weiwer, N. Aidoud, M. Thomas, E.L. Davoine, B.C. Lemercier, Y.L. Zhang, E.B. Holson, Potent and selective inhibition of histone deacetylase 6 (HDAC6) does not require a surface-binding motif, J. Med. Chem. 56 (2013) 1772e1776.
32. Q. Sun, Y. Yao, C. Liu, H. Li, H. Yao, X. Xue, J. Liu, Z. Tu, S. Jiang, Design, synthesis, and biological evaluation of novel histone deacetylase 1 inhibitors through click chemistry, Bioorg. Med. Chem. Lett. 23 (2013) 3295e3299.
33. C. Liao, M. Sitzmann, A. Pugliese, M.C. Nicklaus, Software and resources for computational medicinal chemistry, Future Med. Chem. 3 (2011) 1057e1085.
34. C.J. Millard, P.J. Watson, I. Celardo, Y. Gordiyenko, S.M. Cowley, C.V. Robinson, L. Fairall, J.W. Schwabe, Class I HDACs share a common mechanism of regulation by inositol phosphates, Mol. Cell. 51 (2013) 57e67.
35. B.E. Lauffer, R. Mintzer, R. Fong, S. Mukund, C. Tam, I. Zilberleyb, B. Flicke, A. Ritscher, G. Fedorowicz, R. Vallero, D.F. Ortwine, J. Gunzner, Z. Modrusan, L. Neumann, C.M. Koth, P.J. Lupardus, J.S. Kaminker, C.E. Heise, P. Steiner, Histone deacetylase (HDAC) inhibitor kinetic rate constants correlate with cellular histone acetylation but not transcription and cell viability, J. Biol. Chem. 288 (2013) 26926-26943.
36. D. Wang, P. Helquist, O. Wiest, Zinc binding in HDAC inhibitors: a DFT study, J. Org. Chem. 72 (2007) 5446e5449.
37. K. Chen, L. Xu, O. Wiest, Computational exploration of zinc binding groups for HDAC inhibition, J. Org. Chem. 78 (2013) 5051e5055.
38. C. Liao, M.C. Nicklaus, Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study, ChemMedChem 5 (2010) 1053e1066.
39. C.Z. Liao, R.S. Yao, Diversity evolution and jump of Polo-like kinase 1 inhibitors, Sci. China Chem. 56 (2013) 1392e1401.
40. A. Schuetz, J. Min, A. Allali-Hassani, M. Schapira, M. Shuen, P. Loppnau, R. Mazitschek, N.P. Kwiatkowski, T.A. Lewis, R.L. Maglathin, T.H. McLean, A. Bochkarev, A.N. Plotnikov, M. Vedadi, C.H. Arrowsmith, Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity, J. Biol. Chem. 283 (2008) 11355-11363.