Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Chemical Papers

Online
ISSN
1336-9075
See all formats and pricing
More options …
Volume 60, Issue 1

Issues

New methods in synthesis of acetylcholinesterase reactivators and evaluation of their potency to reactivate cyclosarin-inhibited AChE

K. Musílek
  • Department of Pharmaceutical Chemistry and Drug Control, Faculty of Pharmacy in Hradec Králové, Charles University in Prague, CZ-500 05, Hradec Králové, Czech Republic
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ L. Lipka
  • Department of Pharmaceutical Chemistry and Drug Control, Faculty of Pharmacy in Hradec Králové, Charles University in Prague, CZ-500 05, Hradec Králové, Czech Republic
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ V. Račáková
  • Department of Pharmaceutical Chemistry and Drug Control, Faculty of Pharmacy in Hradec Králové, Charles University in Prague, CZ-500 05, Hradec Králové, Czech Republic
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ K. Kuča / D. Jun / V. Dohnal
  • Department of Food Technology, Mendel University of Agriculture and Forestry Brno, CZ-613 00, Brno, Czech Republic
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ M. Doležal
  • Department of Pharmaceutical Chemistry and Drug Control, Faculty of Pharmacy in Hradec Králové, Charles University in Prague, CZ-500 05, Hradec Králové, Czech Republic
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-02-01 | DOI: https://doi.org/10.2478/s11696-006-0008-x

Abstract

Nine potential AChE reactivators were synthesized using modification of currently known synthetic pathways. Their potency to reactivate AChE inhibited by cyclosarin nerve agent was tested in vitro. According to the previous results, 1,4-bis(2-hydroxyiminomethylpyridinium)butane dibromide seems to be the most potent AChE reactivator. The reactivation potency of these compounds depends on structural factors such as presence of quaternary nitrogens, length of the linking chain between both pyridinium rings, and position of the oxime moiety at the pyridinium ring.

  • [1] Bajgar, J., Adv. Clin. Chem. 38, 151 (2004). http://dx.doi.org/10.1016/S0065-2423(04)38006-6CrossrefGoogle Scholar

  • [2] Marrs, T. C., Pharmacol. Ther. 58, 51 (1993). http://dx.doi.org/10.1016/0163-7258(93)90066-MCrossrefGoogle Scholar

  • [3] Patočka, J., Kuča, K., and Jun, D., Acta Med. (Hradec Králové) 47, 215 (2004). Google Scholar

  • [4] Kuča, K., Bielavský, J., Cabal, J., and Kassa, J., Bioorg. Med. Chem. Lett. 13, 3545 (2003). http://dx.doi.org/10.1016/S0960-894X(03)00751-0CrossrefGoogle Scholar

  • [5] Kassa, J., J. Toxicol., Clin. Toxicol. 40, 803 (2002). http://dx.doi.org/10.1081/CLT-120015840CrossrefGoogle Scholar

  • [6] Kuča, K., Bielavský, J., Cabal, J., and Bielavská, M., Tetrahedron Lett. 44, 3123 (2003). http://dx.doi.org/10.1016/S0040-4039(03)00538-0CrossrefGoogle Scholar

  • [7] Wilson, I. B., Ginsburg, S., and Meilisch, E. K., J. Am. Chem. Soc. 77, 4286 (1955). http://dx.doi.org/10.1021/ja01621a035CrossrefGoogle Scholar

  • [8] Poziomek, E. J., Hackley, B. E., and Steinberg, G. M., J. Org. Chem. 23, 714 (1958). http://dx.doi.org/10.1021/jo01099a019CrossrefGoogle Scholar

  • [9] Krejčová, G. and Kassa, J., Toxicology 185, 129 (2003). http://dx.doi.org/10.1016/S0300-483X(02)00599-1CrossrefGoogle Scholar

  • [10] Rousseaux, C. G. and Gua, A. K., Can. J. Physiol. Pharmacol. 67, 1183 (1989). CrossrefGoogle Scholar

  • [11] Kassa, J., Cabal, J., Bajgar, J., and Szinicz, L., ASA Newslett. 97-4, 16 (1997). Google Scholar

  • [12] Krejčová, G., Ševelová, L., and Kuča, K., Zprav. Voj. Farm. 14, 5 (2004). Google Scholar

  • [13] Hampl, F., Mazač, J., Liška, F., Šrogl, J., Kábrt, L., and Suchánek, M., Collect. Czech. Chem. Commun. 60, 883 (1995). http://dx.doi.org/10.1135/cccc19950883CrossrefGoogle Scholar

  • [14] Kuča, K., Cabal, J., Patočka, J., and Kassa, J., Lett. Org. Chem. 1, 84 (2004). http://dx.doi.org/10.2174/1570178043488761CrossrefGoogle Scholar

  • [15] Pang, Y. P., Kollmeyer, T. M., Hong, F., Lee, J. C., Hammond, P. I., Haugabouk, S. P., and Brimijoin, S., Chem. Biol. 10, 491 (2003). http://dx.doi.org/10.1016/S1074-5521(03)00126-1CrossrefGoogle Scholar

  • [16] Kuča, K. and Kassa, J., J. Enzyme Inhib. Med. Chem. 18, 529 (2003). http://dx.doi.org/10.1080/14756360310001605552CrossrefGoogle Scholar

  • [17] Kuča, K. and Patočka, J., J. Enzyme Inhib. Med. Chem. 19, 39 (2004). http://dx.doi.org/10.1080/1475636031000163850CrossrefGoogle Scholar

  • [18] Kuča, K., Patočka, J., and Cabal, J., J. Appl. Biomed. 1, 207 (2003). Google Scholar

  • [19] Ginsburg, S. and Wilson, I. B., J. Am. Chem. Soc. 79, 481 (1957). http://dx.doi.org/10.1021/ja01559a067CrossrefGoogle Scholar

  • [20] Waysbort, D., Balderman, D., and Amitai, G., Org. Magn. Reson. 16, 7 (1981). http://dx.doi.org/10.1002/mrc.1270160103CrossrefGoogle Scholar

  • [21] Sikder, A. K., Ghosh, A. K., and Jaiswal, D. K., J. Pharm. Sci. 82, 258 (1993). http://dx.doi.org/10.1002/jps.2600820308CrossrefGoogle Scholar

About the article

Published Online: 2006-02-01

Published in Print: 2006-02-01


Citation Information: Chemical Papers, Volume 60, Issue 1, Pages 48–51, ISSN (Online) 1336-9075, DOI: https://doi.org/10.2478/s11696-006-0008-x.

Export Citation

© 2006 Institute of Chemistry, Slovak Academy of Sciences. Copyright Clearance Center

Comments (0)

Please log in or register to comment.
Log in