Synthesis of 5-chloro-N-aryl-1H-indole-2-carboxamide derivatives as inhibitors of human liver glycogen phosphorylase a

Bioorganic and Medicinal Chemistry

Volumn 16, Issue 10, 2008, Pages 5452-5464

  Onda, Kenichi ^a   Suzuki, Takayuki ^a   Shiraki, Ryota ^a   Yonetoku, Yasuhiro ^a   Negoro, Kenji ^a   Momose, Kazuhiro ^a   Katayama, Naoko ^a   Orita, Masaya ^a   Yamaguchi, Tomohiko ^a   Ohta, Mitsuaki ^a   Tsukamoto, Shin ichi ^a  

^a ASTELLAS PHARMA INC   (Japan)

Author keywords

Crystallographic determination; Diabetes; Glycogen phosphorylase; Hepatic glucose output

Indexed keywords

5 CHLORO N [4 (1,2 DIHYDROXYETHYL)PHENYL] 1H INDOLE 2 CARBOXAMIDE; AMIDE; DIMER; ENZYME INHIBITOR; GLUCAGON; GLYCOGEN PHOSPHORYLASE; HYDROXYL GROUP; INDOLE DERIVATIVE; POLYCYCLIC AROMATIC HYDROCARBON DERIVATIVE; PYRIDINE DERIVATIVE; SOLVENT;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELL CULTURE; CONTROLLED STUDY; CRYSTALLOGRAPHY; DIABETES MELLITUS; DRUG SYNTHESIS; ELECTRICITY; ENZYME INHIBITION; ENZYME INHIBITOR INTERACTION; IC 50; LIVER CELL; MOUSE; NONHUMAN;

ADMINISTRATION, ORAL; ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIABETES MELLITUS, EXPERIMENTAL; ENZYME INHIBITORS; GLYCOGEN PHOSPHORYLASE, LIVER FORM; HUMANS; HYPOGLYCEMIC AGENTS; INDOLES; INHIBITORY CONCENTRATION 50; LIVER; MICE; MICE, OBESE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; STEREOISOMERISM;

MUS;

EID: 43749087561     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmc.2008.04.010     Document Type: Article

References (34)

1. Kenny, S. J.; Aubert, R. E.; Geiss, J. S. In Diabetes in America, 2nd ed.; Harris, M., Ed.; NIH Publication 95-1468, National Institutes of Health: Bethesda, MD, 1995, pp 47-67.
2. DeFronzo R.A. Ann. Intern. Med. 131 (1999) 281-303
3. Moller D.E. Nature 414 (2001) 821-827
4. DeFronzo R.A. Diabetes 37 (1988) 667-687
5. McCormack J.G., Westergaard N., Kristiansen M., Brand C.L., and Lau J. Curr. Pharm. Des. 7 (2001) 1451-1474
6. Consoli A. Diabetes Care 15 (1992) 430-441
7. Gerich J.E. Horm. Metab. Res. 26 (1992) 18-21
8. Treadway J.L., Mendys P., and Hoover D.J. Exp. Opin. Invest. Drugs 10 (2001) 439-454
9. Oikonomakos N.G. Curr. Protein Pept. Sci. 3 (2002) 561-586
10. Martin W.H., Hoover D.J., Armento S.J., Stock I.A., McPherson R.K., Danley D.E., Stevenson R.W., Barrett E.J., and Treadway J.L. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 1776-1781
11. Fosgerau F., Westergaard N., Quistorff B., Grunnet N., Kristiansen M., and Lundgren K. Arch. Biochem. Biophys. 380 (2000) 274-284
12. Newgard C.B., Hwang P.K., and Fletterick R.J. Crit. Rev. Biochem. Mol. Biol. 24 (1989) 69-99
13. DeFronzo R.A., Bonadonna R.C., and Ferrannini E. Diabetes Care 15 (1992) 318-368
14. Lefebvre P.J., and Scheen A.J. Eur. J. Clin. Invest. 29 (1999) 1-6
15. Tappy L. Diabetes Metabol. 21 (1995) 233-240
16. Sutherland E.W., and Robinson G.A. Diabetes 18 (1969) 797-819
17. Martin J.L., Veluraja K., Ross K., Johnson L.N., Fleet G.W.J., Ramsden N.G., Bruce I., Orchard M.G., Oikonomakos N.G., Papageorgiou A.C., Leonidas D.D., and Tsitoura H.S. Biochemistry 30 (1991) 10101-10116
18. Zographos S.E., Oikonomakos N.G., Tsitsanou K.E., Leonidas D.D., Chrysina E.D., Skamnaki V.T., Bischoff H., Goldmann S., Watson K.A., and Johnson L.N. Structure 5 (1997) 1413-1425
19. Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N., Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., and Pamdit J. Mol. Cell 6 (2000) 139-148
20. Kristiansen M., Andersen B., Iversen L.F., and Westergaard N. J. Med. Chem. 47 (2004) 3537-3545
21. Kosmopoulou M.N., Leonidas D.D., Chrysina E.D., Bischler N., Eisenbrand G., Sakarellos C.E., Pauptit R., and Oikonomakos N.G. Eur. J. Biochem. 271 (2004) 2280-2290
22. Hampson J.J., Arden C., Agius L., Ganotidis M., Kosmopoulou M.N., Tiraidis C., Elemes Y., Sakarellos C., Leonidas D.D., and Oikonomakos N.G. Bioorg. Med. Chem. 14 (2006) 7835-7845
23. Rath V.L., Ammirati M., Danley D.E., Ekstrom J.L., Gibbs E.M., Hynes T.R., Mathiowetz A.M., McPherson R.K., Olson T.V., Treadway J.L., and Hoover D.J. Chem. Biol. 7 (2000) 677-682
24. Oikonomakos N.G., Skamnaki V.T., Tsitsanou K.E., Gavalas N.G., and Johnson L.N. Structure 8 (2000) 575-584
25. Hoover D.J., Lefkowitz-Snow S., Burgess-Henry J.L., Martin W.H., Armento S.J., Stock I.A., McPherson R.K., Genereux P.E., Gibb E.M., and Treadway J.L. J. Med. Chem. 41 (1998) 2934-2938
26. Oikonomakos N.G., Zographos S.E., Skamnaki V.T., and Archontis G. Bioorg. Med. Chem. 10 (2002) 1313-1319 The CP-320626 binding site in the rabbit MGP are highly conserved in hLGP and based on this observation they suggested that the new allosteric site is likely to be the same in the liver enzyme. See Ref. 24
27. Belletire J.L., Walley D.R., and Bast M.J. Synth. Commun. 12 (1982) 469-475
28. Blumenstein J.J., Ukachkwu V.C., Mohan R.S., and Whalen D.L. J. Org. Chem. 58 (1993) 924-932
29. Scott W.J., and Sille J.K. J. Am. Chem. Soc. 108 (1986) 3033-3040
30. Kobayashi, Y.; Mori, H.; Morita, H. WO9628405.
31. Clark, A. K. Ligand interaction diagrams. Chem. Comput. Group Journal, 2006, http://www.chemcomp.com/journal/ligintdia.htm.
32. Pesce M.A., Bodourian S.H., Harris R.C., and Nicholson J.H. Clin. Chem. 23 (1977) 1711-1717
33. Tanaka K., Sato M., Tomita Y., and Ichihara A. J. Biochem. 84 (1978) 937-946
34. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Acta Crystallogr. D54 (1998) 905-921