Simplified staurosporine analogs as potent JAK3 inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 17, Issue 2, 2007, Pages 326-331

  Yang, Shyh Ming ^a   Malaviya, Ravi ^a   Wilson, Lawrence J ^a   Argentieri, Rochelle ^a   Chen, Xin ^a   Yang, Cangming ^a   Wang, Bingbing ^a   Cavender, Druie ^a   Murray, William V ^a  

^a JOHNSON AND JOHNSON PHARMACEUTICAL RESEARCH AND DEVELOPMENT   (United States)

Author keywords

JAK3; Janus kinases 3; Staurosporine

Indexed keywords

4 [N [1 (2 CYANO 1 OXOETHYL) 4 METHYL 3 PIPERIDINYL] N METHYLAMINO]PYRROLO[2,3 D]PYRIMIDINE; 5,6,7,13 TETRAHYDRO 12 (3 HYDROXYPROPYL) 9 ISOPROPOXYMETHYLINDENO[2,1 A]PYRROLO[3,4 C]CARBAZOL 5(12H) ONE DIMETHYLGLYCINE ESTER; CEP 1347; JANUS KINASE 3; PROTEIN KINASE INHIBITOR; STAUROSPORINE;

ARTICLE; CHEMICAL MODIFICATION; DRUG STRUCTURE; ENZYME INHIBITION; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATE; ENZYME INHIBITORS; INDICATORS AND REAGENTS; JANUS KINASE 3; MODELS, MOLECULAR; PROTEIN BINDING; STAUROSPORINE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33846087418     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2006.10.062     Document Type: Article

References (33)

1. Ihle J.N., and Kerr I.M. Trends Genet. 11 (1995) 69
2. Nosaka T., van Deursen J.M.A., Tripp R.A., Thierfelder W.E., Witthuhn B.A., McMickle A.P., Doherty P.C., Grosveld G.C., and Ihle J.N. Science 270 (1995) 800
3. Thomis D.C., Gurniak C.B., Tivol E., Sharpe A.H., and Berg L.J. Science 270 (1995) 794
4. Villa A., Sironi M., Macchi P., Matteucci C., Notarangelo L.D., Vezzoni P., and Mantovani A. Blood 88 (1996) 817
5. Buckley R.H., Schiff R.I., Schiff S.E., Markert M.L., Williams L.W., Harville T.O., Roberts J.L., Harville T.O., Roberts J.L., and Puck J.M. J. Pediatr. 130 (1997) 378
6. Malaviya R., Zhu D., Dibirdik I., and Uckun F.M. J. Biol. Chem. 274 (1999) 27028
7. Malaviya R., and Uckun F.M. Biochem. Biophys. Res. Commun. 257 (1999) 807
8. Stepowski S.M., Erwin-Cohen R.A., Beheod F., Wang M.-E., Qu X., Tejpal N., Nagy Z.S., Kahan B.D., and Kirken R.A. Blood 99 (2002) 680
9. Hall B.M. Transplantation 51 (1991) 1141
10. Säemann M.D., Diakos C.D., Kelemen P., Kriehuber E., Zeyda M., Böhmig G.A., Hörl W.H., Baumruker T., and Zlabinger G.J. Am. J. Transplant. 3 (2003) 1341
11. For a recent review, see:. Cetkovic-Cvrlje M., and Tibbles H.E. Curr. Pharm. Des. 10 (2004) 1767
12. For recent reviews, see:. Thompson J.E. Drug News Perspect. 18 (2005) 305
13. Sudbeck E.A., and Uckun F.M. IDrugs 2 (1999) 1026
14. Papageorgiou A.C., and Wikman L.E.K. Trends Pharmacol. Sci. 25 (2004) 558
15. For some recent JAK3 inhibitors, see:. Brown G.R., Bamford A.M., Bowyer J., James D.S., Rankine N., Tang E., Torr V., and Culbert E.J. Bioorg. Med. Chem. Lett. 10 (2000) 575
16. Adams C., Aldous D.J., Amendola S., Bamborough P., Bright C., Crowe S., Eastwood P., Fenton G., Foster M., Harrison T.K.P., King S., Lai J., Lawrence C., Letallec J.-P., McCarthy C., Moorcroft N., Page K., Rao S., Redford J., Sadiq S., Smith K., Souness J.E., Thurairatnam S., Vine M., and Wyman B. Bioorg. Med. Chem. Lett. 13 (2003) 3105
17. For selective JAKs inhibitor, see:. Thompson J.E., Cubbon R.M., Cummings R.T., Wicker L.S., Frankshun R., Cunningham B.R., Cameron P.M., Meinke P.T., Liverton N., Weng Y., and DeMartino J.A. Bioorg. Med. Chem. Lett. 12 (2002) 1219
18. For selective JAK3 inhibitor, see:. Changelian P.S., Flanagan M.E., Ball D.J., Kent C.R., Magnuson K.S., Martin W.H., Rizzuti B.J., Sawyer P.S., Perry B.D., Brissette W.H., McCurdy S.P., Kudlacz E.M., Conklyn M.J., Elliott E.A., Koslov E.R., Fisher M.B., Strelevitz T.J., Yoon K., Whipple D.A., Sun J., Munchhof M.J., Doty J.L., Casavant J.M., Blumenkopf T.A., Hines M., Brown M.F., Lillie B.M., Subramanyam C., Chang S.P., Milici A.J., Beckius G.E., Moyer J.D., Su C., Woodworth T.G., Gaweco A.S., Beals C.R., Littman B.H., Fisher D.A., Smith J.F., Zagouras P., Magna H.A., Saltarelli M.J., Johnson K.S., Nelms L.F., Etages S.G.D., Hayes L.S., Kawabata T.T., Finco-Kent D., Baker D.L., Larson M., Si M.S., Paniagua R., Higgins J., Holm B., Reitz B., Zhou Y.-J., R. Morris E., O'Shea J.J., and Borie D.C. Science 302 (2003) 875
19. Omura S., Sasaki Y., Iwai Y., and Takeshima H. J. Antibiot. 48 (1995) 535
20. Fiorucci G., Percario Z.A., Marcolin C., Coccia E.M., Affabris E., and Rpmeo G. J. Virol. 69 (1995) 5833
21. Mucke H.A.M. IDrugs 6 (2003) 377
22. Murakata C., Kaneko M., Gessner G., Angeles T.S., Ator M.A., O'Kane T.M., McKenna B.A.W., Thomas B.A., Mathiasen J.R., Saporito M.S., Bozyczko-Coyne D., and Hudkins R.L. Bioorg. Med. Chem. Lett. 12 (2002) 147
23. Kaneko M., Saito Y., Saito H., Matsumoto T., Matsuda Y., Vaught J.L., Dionne C.A., Angeles T.S., Glicksman M.A., Neff N.T., Rotella D.P., Kauer J.C., Mallamo J.P., Hudkins R.L., and Murakata C. J. Med. Chem. 40 (1997) 1863
24. Gingrich D.E., Reddy D.R., Iqbal M.A., Singh J., Aimone L.D., Angeles T.S., Albom M., Yang S., Ator M.A., Meyer S.L., Robinson C., Ruggeri B.A., Dionne C.A., Vaught J.L., Mallamo J.P., and Hudkins R.L. J. Med. Chem. 46 (2003) 5375
25. Boggon T.J., Li Y., Manley P.W., and Eck M.J. Blood 106 (2005) 996 The structure of AFN941 is presented below{A figure is presented}
26. Faul M.M., Winneroski L.L., and Krumrich C.A. J. Org. Chem. 63 (1998) 6053
27. 4 (50 μL/well) and the optical density was read at 450/650 nm.
28. Alterman M., Andersson H.O., Garg N., Ahlsěn G., Lövgren S., Classon B., Danielson U.H., Kvarnström I., Vrang L., Unge T., Samuelsson B., and Hallberg A. J. Med. Chem. 42 (1999) 3835
29. Lawson E.C., Kinney W.A., Luci D.K., Yabut S.C., Wisnoski D., and Maryanoff B.E. Tetrahedron Lett. 43 (2002) 1951 For compound 22o, the acetic acid salt of 2-(3-propenyl)amino-1-ethoxycarbonyl-4,5-dihydroimidazole was used as the cross-coupling partner
30. Wei B., and Hor T.S.A. J. Mol. Cat. A: Chem. 132 (1998) 223
31. Helquist P. Tetrahedron Lett. 19 (1978) 1913
32. The compound 22r was docked, using the docking program Glide (Glide, Schrodinger, 1500 S. W. First Avenue, Suite 1180, Portland, OR 97201). The molecular mechanism calculations were done with MacroModel (MacroModel, Schrodinger, 1500 S. W. First Avenue, Suite 1180, Portland, OR 97201), using OPLS2001 force field. The effect of aqueous solution was treated by GB/SA model. Polak-Ribiere conjugate gradient method was used for energy minimization, and the derivative convergence criterion was set at 0.05 KJ/Ǻ-Mol.
33. Levitt M., and Perutz M.F. J. Mol. Biol. 201 (1988) 751