Design and synthesis of novel 2-(indol-5-yl)thiazole derivatives as xanthine oxidase inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 25, Issue 6, 2015, Pages 1254-1258

  Song, Jeong Uk ^a,b   Choi, Sung Pil ^b   Kim, Tae Hun ^b   Jung, Cheol Kyu ^b   Lee, Joo Youn ^b   Jung, Sang Hun ^a   Kim, Geun Tae ^b  

^a Chungnam National University   (South Korea)

^b LG Chemical Ltd   (South Korea)

Author keywords

2 (Indol 5 yl)thiazole; Gout; Hyperuricemia; Xanthine oxidase inhibitors

Indexed keywords

2 (3 CYANO 2 ISOPROPYLINDOL 5 YL) 4 METHYLTHIAZOLE 5 CARBOXYLIC ACID; FEBUXOSTAT; INDOLE DERIVATIVE; THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; URIC ACID; XANTHINE OXIDASE; XANTHINE OXIDASE INHIBITOR; 2-(3-CYANO-2-ISOPROPYLINDOL-5-YL)-4-METHYLTHIAZOLE-5-CARBOXYLIC ACID; ENZYME INHIBITOR; INDOLE; PROTEIN BINDING;

ANIMAL CELL; ANIMAL EXPERIMENT; AREA UNDER THE CURVE; ARTICLE; CONTROLLED STUDY; CYTOTOXICITY; DRUG BIOAVAILABILITY; DRUG DESIGN; DRUG EFFICACY; DRUG SYNTHESIS; ENZYME INHIBITION; GOUT; HYDROGEN BOND; HYDROPHOBICITY; IC50; LIVER CELL; MALE; MAXIMUM PLASMA CONCENTRATION; MOLECULAR DOCKING; MOLECULAR MODEL; NONHUMAN; RAT; STRUCTURE ACTIVITY RELATION; URIC ACID BLOOD LEVEL; ANIMAL; ANTAGONISTS AND INHIBITORS; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; HALF LIFE TIME; LIVER MICROSOME; METABOLISM; PROTEIN TERTIARY STRUCTURE; SPRAGUE DAWLEY RAT; SYNTHESIS;

ANIMALS; BINDING SITES; DRUG DESIGN; ENZYME INHIBITORS; HALF-LIFE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INDOLES; MICROSOMES, LIVER; MOLECULAR DOCKING SIMULATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; RATS, SPRAGUE-DAWLEY; STRUCTURE-ACTIVITY RELATIONSHIP; THIAZOLES; URIC ACID; XANTHINE OXIDASE;

EID: 84923792506     PISSN: 0960894X     EISSN: 14643405     Source Type: Journal    
DOI: 10.1016/j.bmcl.2015.01.055     Document Type: Article

References (22)

1. E. Suresh Postgrad. Med. J. 81 2005 572
2. A. Shoji, H. Yamanaka, and N. Kamatani Arthritis Rheum. 51 2004 321
3. J.U. Adams Nat. Biotech. 27 2009 309
4. B.T. Emmerson N. Engl. J. Med. 334 1996 445
5. K. Okamoto, B.T. Eger, T. Nishino, E.F. Pai, and T. Nishino Nucleosides Nucleotides Nucleic Acids 27 2008 888
6. P. Pacher, A. Nivorozhkin, and C. Szabó Pharmacol. Rev. 58 2006 87
7. K. Okamoto, B.T. Eger, T. Nishino, S. Kondo, E.F. Pai, and T. Nishino J. Biol. Chem. 2003 1848 278
8. Y. Takano, K. Hase-Aoki, H. Horiuchi, L. Zhao, Y. Kasahara, S. Kondo, and M.A. Becker Life Sci. 2005 1835 76
9. M.E. Ernst, and M.A. Fravel Clin. Ther. 31 2009 2503
10. R.J. Johnson, D.-H. Kang, D. Feig, S. Kivlighn, J. Kanellis, S. Watanabe, K.R. Tuttle, B. Rodriguez-Iturbe, J. Herrera-Acosta, and M. Mazzali Hypertension 41 2003 1183
11. C. Li, M.-C. Hsieh, and S.-J. Chang Curr. Opin. Rheumatol. 25 2013 210
12. T. Sato, N. Ashizawa, T. Iwanaga, H. Nakamura, K. Matsumoto, T. Inoue, and O. Nagata Bioorg. Med. Chem. Lett. 19 2009 184
13. S. Khanna, S. Burudkar, K. Bajaj, P. Shah, A. Keche, U. Ghosh, B-Rao. Chandrika, R. Sharma, and H. Sivaramakrishnan Bioorg. Med. Chem. Lett. 22 2012 7543
14. K. Bajaj, S. Burudkar, P. Shah, A. Keche, U. Ghosh, P. Tannu, S. Khanna, B-Rao. Chandrika, R. Sharma, and H. Sivaramakrishnan Bioorg. Med. Chem. Lett. 23 2013 834
15. J. Evenas, F. Edfeldt, M. Lepisto, N. Svitacheva, A. Synnergren, B. Lundquist, M. Granse, A. Tjornebo, and F. Narjes Bioorg. Med. Chem. Lett. 24 2014 1315
16. G. Biagi, A. Costantini, L. Costantino, I. Giorgi, O. Livi, B. Lundquist, P. Pecorari, M. Rinaldi, and V. Scartoni J. Med. Chem. 39 1996 2529
17. M.-Z. Zhang, N. Mulholland, D. Beattie, D. Irwin, Y.-C. Gu, Q. Chen, G.-F. Yang, and J. Clough Eur. J. Med. Chem. 63 2013 22
18. J.J. Acton, T.E. Akiyama, C.H. Chang, L. Colwell, S. Debenham, T. Doebber, M. Einstein, K. Liu, M.E. McCann, D.E. Moller, E.S. Muise, Y. Tan, J.R. Thompson, K.K. Wong, M. Wu, L. Xu, P.T. Meinke, J.P. Berger, and H.B. Wood J. Med. Chem. 52 2009 3846
19. I.K. Hwang, K.Y. Yoo, H. Li, O.K. Park, C.H. Lee, J.H. Choi, and M.-H. Won J. Neurosci. Res. 87 2009 2126
20. Y. Osada, M. Tsuchimoto, H. Fukushima, K. Takahashi, S. Kondo, M. Hasegawa, and K. Komoriya Eur. J. Pharmacol. 241 1993 183
21. Hachioji, S. K.; Hino, H. F.; Hino, M. H.; Hino, M. T.; Hino, I. N.; Hino, Y. O.; Hachioji, K. K.; Hino, H. Y. U.S. Patent 5,614,520, 1997.
22. The docking study of 6k was performed using the X-ray crystal structure of bovine milk XO (PDB code 1N5X). Flexible docking was carried out using the Schrödinger Glide program with standard precision mode (http://www.schrodinger.com). Docking results were visualized using PyMol (http://www.pymol.org).