Mechanism for potent reactivation ability of H oximes analyzed by reactivation kinetic studies with cholinesterases from different species

Chemico-Biological Interactions

Volumn 187, Issue 1-3, 2010, Pages 185-190

  Luo, Chunyuan ^a   Chambers, Carolyn ^a   Yang, Yerie ^a   Saxena, Ashima ^a  

^a WALTER REED ARMY INSTITUTE OF RESEARCH   (United States)

Author keywords

Guinea pig acetylcholinesterase; H oxime; Human acetylcholinesterase; Nerve agent; Reactivation mechanism; Rhesus monkey acetylcholinesterase

Indexed keywords

1 (4 CARBAMOYLPYRIDINIO) 1' (2 HYDROXYIMINOMETHYLPYRIDINIO)DIMETHYL ETHER; 1 [2,4 BIS(HYDROXYIMINOMETHYL)PYRIDINIO] 1' (4 CARBAMOYLPYRIDINIO)DIMETHYL ETHER DIIODIDE; 1,1' METHYLENEBIS(4 HYDROXYIMINOMETHYLPYRIDINIUM) DICHLORIDE; ALANINE; CHOLINESTERASE; GLUTAMINE; MUTANT PROTEIN; ORGANOPHOSPHATE; ORGANOPHOSPHORUS COMPOUND; OXIME DERIVATIVE; PRALIDOXIME; TRYPTOPHAN; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL REACTION; CHEMICAL STRUCTURE; CHOLINESTERASE INHIBITION; CONTROLLED STUDY; DRUG STRUCTURE; ENZYME REACTIVATION; INHIBITION KINETICS; PROTEIN MODIFICATION; WILD TYPE;

BOVINAE; CAVIA; MACACA MULATTA;

EID: 77955512484     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.01.018     Document Type: Article

References (30)

1. Marrs T.C. Clinical and Experimental Toxicology of Organophosphates and Carbamates 1992, Butterworth & Heinemann, Oxford, pp. 555-577.
2. Saxena A., Viragh C., Frazier D.S., Kovach I.M., et al. The pH dependence of dealkylation in soman-inhibited cholinesterases and their mutants: further evidence for a push-pull mechanism. Biochemistry 1998, 37:15086-15096.
3. Primozic I., Odzak R., Tomic S., Simeon-Rudolf V., Reiner E. Pyridunium, imidazolium, and quinucludinium oximes: synthesis, interaction with native and phosphylated cholinesterases, and antidotes against organophosphorus compounds. J. Med. Chem. Def. 2004, 2:1-32.
4. Musilek K., Kuca K., Jun D., Dohnal V., Dolezal M. Synthesis of the novel series of bispyridinium compounds bearing (E)-but-2-ene linker and evaluation of their reactivation activity against chlorpyrifos-inhibited acetylcholinesterase. Bioorg. Med. Chem. Lett. 2006, 16:622-627.
5. Pang Y.P., Kollmeyer T.M., Hong F., Lee J.C., Hammond P.I., Haugabouk S.P., Brimijoin S. Rational design of alkylene-linked bis-pyridiniumaldoximes as improved acetylcholinesterase reactivators. Chem. Biol. 2003, 10:491-502.
6. Worek F., Aurbek N., Koller M., Becker C., Eyer P., Thiermann H. Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by different phosphoramidates. Biochem. Pharmacol. 2007, 73:1807-1817.
7. Hagedorn I., Stark I., Schoene K., Schenkel H. Reactivation of phosphorylated acetylcholinesterase. Isomeric bisquaternary salts of pyridine aldoximes. Arzneimittel-Forschung 1978, 28:2055-2057.
8. M. Loffler, Quatare Salze von Pyridin-2,4-dialdoxim als Gegenmittel fur Organophosphat-Vergiftungen [Thesis], University of Freiberg, Freiburg, 1986.
9. Luo C., Tong M., Chilukuri N., Brecht K., Maxwell D.M., Saxena A. An in vitro comparative study on the reactivation of nerve agent-inhibited guinea pig and human acetylcholinesterases by oximes. Biochemistry 2007, 46:11771-11779.
10. Worek F., Thiermann H., Szinicz L., Eyer P. Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes. Biochem. Pharmacol. 2004, 68:2237-2248.
11. Lundy P.M., Hansen A.S., Hand B.T., Boulet C.A. Comparison of several oximes against poisoning by soman, tabun and GF. Toxicology 1992, 72:99-105.
12. Eyer P, Hell W., Kawan A., Klehr H. Studies on the decomposition of the oxime HI 6 in aqueous solution. Arch. Toxicol. 1986, 59:266-271.
13. Eyer P., Ladstetter B., Schafer W., Sonnenbichler J. Studies on the stability and decomposition of the Hagedorn-oxime HLo 7 in aqueous solution. Arch. Toxicol. 1989, 63:59-67.
14. Ekstrom F., Pang Y.P., Boman M., Artursson E., Akfur C., Borjegren S. Crystal structures of acetylcholinesterase in complex with HI-6, Ortho-7 and obidoxime: structural basis for differences in the ability to reactivate tabun conjugates. Biochem. Pharmacol. 2006, 72:597-607.
15. Ekstrom F., Astot C., Pang Y. Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes. Clin. Pharmacol. Ther. 2007, 82:282-293.
16. Ekstrom F., Hornberg A., Artursson E., Hammarstrom L.G., Schneider G., Pang Y.P. Structure of HI-6·sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: reactivator mechanism and design. PLoS ONE [Electronic Resource] 2009, 4:e5957.
17. Sanson B., Nachon F., Colletier J.P., Froment M.T., Toker L., Greenblatt H.M., Sussman J.L., Ashani Y., Masson P., Silman I., Weik M. Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime. J. Med. Chem. 2009, 52:7593-7603.
18. Worek F., Reiter G., Eyer P., Szinicz L. Reactivation kinetics of acetylcholinesterase from different species inhibited by highly toxic organophosphates. Arch. Toxicol. 2002, 76:523-529.
19. Worek F., Aurbek N., Wetherell J., Pearce P., Mann T., Thiermann H. Inhibition, reactivation and aging kinetics of highly toxic organophosphorus compounds: pig versus minipig acetylcholinesterase. Toxicology 2008, 244:35-41.
20. Levy D., Ashani Y. Synthesis and in vitro properties of a powerful quaternary methylphosphonate inhibitor of acetylcholinesterase. A new marker in blood-brain barrier research. Biochem. Pharmacol. 1986, 35:1079-1085.
21. Luo C., Chambers C., Tong M., Maxwell D.M., Brecht K., Tipparaju P., Doctor B.P., Saxena A. Development of a broad-spectrum oxime for the treatment of nerve agent toxicity. 25th Army Science Conference 2006.
22. Gan K.N., Smolen A., Eckerson H.W., La Du B.N. Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 1991, 19:100-106.
23. Cohen O., Kronman C., Velan B., Shafferman A. Amino acid domains control the circulatory residence time of primate acetylcholinesterases in rhesus macaques (Macaca mulatta). Biochem. J. 2004, 378:117-128.
24. Ellman G.L., Courtney K.D., Andres V., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 1961, 7:88-95.
25. Wong L., Radic Z., Bruggemann R.J., Hosea N., Berman H.A., Taylor P. Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis. Biochemistry 2000, 39:5750-5757.
26. Luo C., Saxena A., Smith M., Garcia G., Radic Z., Taylor P., Doctor B.P. Phosphoryl oxime inhibition of acetylcholinesterase during oxime reactivation is prevented by edrophonium. Biochemistry 1999, 38:9937-9947.
27. Luo C., Tong M., Maxwell D.M., Saxena A. In vitro comparison of oxime reactivation and aging of different monkeys and human acetylcholinesterases inhibited by nerve agents with bulky side-chains. Chem. Biol. Interact. 2008, 175:261-266.
28. de Jong L.P.A., Worling G.Z. Stereospecific reactivation by some Hagedorn-oximes of acetylcholinesterases from various species including man, inhibited by soman. Biochem. Pharmacol. 1984, 33:1119-1125.
29. Connolly M.L. Computation of molecular volume. J. Am. Chem. Soc. 1985, 107:1118-1124.
30. Ashani Y., Radic Z., Tsigelny I., Vellom D.C., Pickerring N.A., Quinn D.M., Doctor B.P., Taylor P. Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- and bisquaternary oximes. J. Biol. Chem. 1995, 270:6370-6380.