Design and synthesis of 1,3-diarylurea derivatives as selective cyclooxygenase (COX-2) inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 18, Issue 4, 2008, Pages 1336-1339

  Zarghi, Afshin ^a   Kakhgi, Samaneh ^a   Hadipoor, Atefeh ^a   Daraee, Bahram ^b   Dadrass, Orkideh G ^c   Hedayati, Mehdi ^a  

^a SHAHID BEHESHTI UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b TARBIAT MODARES UNIVERSITY   (Iran)

^c ISLAMIC AZAD UNIVERSITY   (Iran)

Author keywords

1,3 Diarylurea; COX 2 inhibition; SAR

Indexed keywords

1 (4 METHYLSULFONYLPHENYL) 3 (4 METHOXYPHENYL) UREA; CELECOXIB; CYCLOOXYGENASE 1 INHIBITOR; CYCLOOXYGENASE 2 INHIBITOR; UNCLASSIFIED DRUG; UREA DERIVATIVE;

ARTICLE; CONTROLLED STUDY; DRUG DESIGN; DRUG INHIBITION; DRUG SYNTHESIS; IN VITRO STUDY; PHARMACOPHORE; STRUCTURE ACTIVITY RELATION;

BENZENE DERIVATIVES; BINDING SITES; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITORS; DRUG DESIGN; INHIBITORY CONCENTRATION 50; MODELS, MOLECULAR; UREA;

EID: 38949134834     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2008.01.021     Document Type: Article

References (22)

1. Carter J.S. Expert Opin. Ther. Patents 8 (1998) 21
2. Xie W.L., Chipman J.G., Robertson D.L., Erikson R.L., and Simmons D.L. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 2692
3. Smith W.L., and DeWitt D.L. Adv. Immunol. 62 (1996) 167
4. Herschman H.R. Biochem. Biophys. Acta 1299 (1996) 125
5. Kawamori T., Rao C.V., Seibert K., and Reddy B.S. Cancer Res. 58 (1998) 409
6. Katori M., and Majima M. Inflamm. Res. 295 (2000) 802
7. Vane J.R., and Botting R.M. Inflamm. Res. 47 (1998) S78
8. Penning T.D., Tally J.J., Bertenshaw S.R., Carter J.S., Collins P.W., Docter S., Graneto M.J., Lee L.F., Malecha J.W., Miyashiro J.M., Rogers R.S., Rogier D.J., Yu S.S., Anderson G.D., Burton E.G., Cogburn J.N., Gregory S.A., Koboldt C.M., Perkins W.E., Seibert K., Veenhuizen A.W., Zhang Y.Y., and Isakson P.C. J. Med. Chem. 40 (1997) 1347
9. Riendeau D., Percival M.D., Brideau C., Dube C.S., Ethier D., Falgueyret J.P., Friesen R.W., Gordon R., Greig G., Guay J., Girard Y., Prasit P., Zamboni R., Rodger I.W., Gresser M., Ford-Hutchinson A.W., Young R.N., and Chan C.C. J. Pharmacol. Exp. Ther. 296 (2002) 558
10. Prasit P., Wang Z., Brideau C., Chan C.-C., Charlson S., Cromlish W., Ethier D., Evans J.F., Ford-Hutchinson A.W., Gauthier J.Y., Gordon R., Guay J., Gresser M., Kargman S., Kennedy B., Leblanc Y., Leger S., Mancini J., O_Neil G.P., Quellet M., Percival M.D., Perrier H., Riendeau D., Rodger I., Tagari P., Therien M., Vikers P., Wong E., Xu L.-J., Young R.N., Zamboni R., Boyce S., Rupniak N., Forrest M., Visco D., and Patrick D. Bioorg. Med. Chem. Lett. 9 (1999) 1773
11. Friesen R.W., Dube D., Fortin R., Frenette R., Prescott S., Cromlish W., Greig G.M., Kargman S., Wong E., Chan C.C., Gordon R., and Xu L.J. Bioorg. Med. Chem. Lett. 6 (1996) 2677
12. Talley J.J., Brown D.L., Carter J.S., Graneto M.J., Koboldt C.M., Masferrer J.L., Perkins W.E., Rogers R.S., Shaffer A.F., Zhang Y.Y., Zweifel B.S., and Seibert K.K. J. Med. Chem. 43 (2000) 775
13. Zarghi A., Rao P.N.P., and Knaus E.E. J. Pharm. Pharm. Sci. 10 (2007) 129
14. Zarghi A., Najafnia L., Daraie B., Dadrass O.G., and Hedayati M. Bioorg. Med. Chem. Lett. 17 (2007) 5634
15. Dogné J.M., Supuran C.T., and Pratico D. J. Med. Chem. 48 (2005) 2251
16. Solomon D.H. Arthritis Rheum. 52 (2005) 1968
17. Zarghi A., Arfaee S., Rao P.N.P., and Knaus E.E. Bioorg. Med. Chem. 14 (2006) 2600
18. Zarghi A., Zebardast T., Hakimion F., Shirazi H.F., Rao P.N.P., and Knaus E.E. Bioorg. Med. Chem. 14 (2006) 7044
19. Franz R.A., Applegath F., Morriss F.V., Baiocchi F., and Bolze C. J. Org. Chem. 26 (1961) 3309
20. Docking studies were performed using Autodock software Version 3.0. The coordinates of the X-ray crystal structure of the selective COX-2 inhibitor SC-558 bound to the murine COX-2 enzyme were obtained from the RCSB Protein Data Bank (1cx2) and hydrogens were added. The ligand molecules were constructed using the Builder module and were energy minimized for 1000 iterations reaching a convergence of 0.01 kcal/mol Å. The energy minimized ligands were superimposed on SC-558 in the PDB file 1cx2 after which SC-558 was deleted. The purpose of docking is to search for favorable binding configuration between the small flexible ligands and the rigid protein. Protein residues with atoms greater than 7.5 Å from the docking box were removed for efficiency. Searching is conducted within a specified 3D docking box using annealing based on the Monte Carlo method and MMFF94 molecular mechanics force field for 8000 iterations. These docked structures were very similar to the minimized structures obtained initially. The quality of the docked structures was evaluated by measuring the intermolecular energy of the ligand-enzyme assembly.
21. Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., Stegeman R.A., Pak J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., Seibert K., Isakson P.C., and Stallings W.C. Nature 384 (1996) 644
22. 4S (C,H, N). Satisfactory analysis for C, H, N was obtained for all the compounds within ±0.4% of the theoretical values.