Advertisement

Chemistry of Heterocyclic Compounds

, Volume 55, Issue 11, pp 1050–1059 | Cite as

New 3,4-bis(indol-1-yl)maleimides as protein kinase inhibitors

  • Alexey A. PanovEmail author
  • Sergey A. Lakatosh
  • Michael H. G. Kubbutat
  • Lyubov G. Dezhenkova
  • Frank Totzke
  • Kristof Schechtel
Article
  • 15 Downloads

Several previously unknown derivatives of 3,4-bis(indol-1-yl)maleimide, as well as 3-(2,3-dihydroindol-1-yl)-4-(indol-1-yl)maleimide were synthesized as potential analogs for a known series of protein kinase inhibitors BIS I, IV, IX containing the structural motif of 3,4-bis(indol-3-yl)maleimide. The activity of these synthesized compounds was characterized with regard to several human protein kinases and their cytotoxicity was determined.

Keywords

indole indolylmaleimides antitumor drugs protein kinases protein kinase inhibitors 

References

  1. 1.
    Goekjian, P. G.; Jirousek, M. R. Expert Opin. Invest. Drugs 2001, 10, 2117.CrossRefGoogle Scholar
  2. 2.
    Fabbro, D.; Ruetz, S.; Buchdunger, E.; Cowan-Jacob, S. W.; Fendrich, G.; Liebetanz, J.; Mestan, J.; O'Reilly, T.; Traxler, P.; Chaudhuri, B.; Fretz, H.; Zimmermann, J.; Meyer, T.; Caravatti, G.; Furet, P.; Manley, P. W. Pharmacol. Ther. 2002, 93, 79.CrossRefGoogle Scholar
  3. 3.
    Davis, P. D.; Elliott, L. H.; Harris, W.; Hill, C. H.; Hurst, S. A.; Keech, E.; Kumar, M. K. H.; Lawton, G.; Nixon, J. S.; Wilkinson, S. E. J. Med. Chem. 1992, 35, 994.CrossRefGoogle Scholar
  4. 4.
    Davis, P. D.; Hill, C. H.; Lawton, G.; Nixon, J. S.; Wilkinson, S. E.; Hurst, S. A.; Keech, E.; Turner, S. E. J. Med. Chem. 1992, 35, 177.CrossRefGoogle Scholar
  5. 5.
    Jirousek, M. R.; Gillig, J. R.; Neel, D. A.; Rito, C. J.; O'bannon, D.; Heath, W. F.; McDonald III, J. H.; Faul, M. M.; Winneroski, L. L.; Melikian-Badalian, A.; Baevsky, M.; Ballas, L. M.; Hall, S. E. Bioorg. Med. Chem. Lett. 1995, 5, 2093.CrossRefGoogle Scholar
  6. 6.
    Jirousek, M. R.; Gillig, J. R.; Gonzalez, C. M.; Heath, W. F.; McDonald III, J. H.; Neel, D. A.; Rito, C. J.; Singh, U.; Stramm, L. E.; Melikian-Badalian, A.; Baevsky, M.; Ballas, L. M.; Hall, S. E.; Winneroski, L. L.; Faul, M. M. J. Med. Chem. 1996, 39, 2664.CrossRefGoogle Scholar
  7. 7.
    Bartlett, S.; Beddard, G. S.; Jackson, R. M.; Kayser, V.; Kilner, C.; Leach, A.; Nelson, A.; Oledzki, P. R.; Parker, P.; Reid, G. D.; Warriner, S. L. J. Am. Chem. Soc. 2005, 127, 11699.CrossRefGoogle Scholar
  8. 8.
    Grodsky, N.; Li, Y.; Bouzida, D.; Love, R.; Jensen, J.; Nodes, B.; Nonomiya, J.; Grant, S. Biochemistry 2006, 45, 13970.CrossRefGoogle Scholar
  9. 9.
    Simonov, A. Yu.; Lakatosh, S. A.; Luzikov, Yu. N.; Reznikova, M. I.; Susova, O. Yu.; Shtil’, A. A.; Elizarov, S. M.; Danilenko, V. N.; Preobrazhenskaya, M. N. Russ. Chem. Bull., Int. Ed. 2008, 57, 2011. [Izv. Akad. Nauk, Ser. Khim. 2008, 1977.]Google Scholar
  10. 10.
    Lakatosh, S. A.; Luzikov, Y. N.; Preobrazhenskaya, M. N. Org. Biomol. Chem. 2003, 1, 826.CrossRefGoogle Scholar
  11. 11.
    Simonov, A. Yu.; Bykov, E. E.; Lakatosh, S. A.; Luzikov, Yu. N.; Korolev, A. M.; Reznikova, M. I.; Preobrazhenskaya, M. N. Tetrahedron 2014, 70, 625.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Alexey A. Panov
    • 1
    Email author
  • Sergey A. Lakatosh
    • 1
  • Michael H. G. Kubbutat
    • 2
  • Lyubov G. Dezhenkova
    • 3
  • Frank Totzke
    • 2
  • Kristof Schechtel
    • 2
  1. 1.Gause Institute of New AntibioticsMoscowRussia
  2. 2.ProQinase GmbH, Tumor Biology Centre in FreiburgFreiburgGermany
  3. 3.N. N. Blokhin Russian Cancer Research CenterMoscowRussia

Personalised recommendations