Mass Spectrometry Method to Identify Aging Pathways of Sp- and Rp-Tabun Adducts on Human Butyrylcholinesterase Based on the Acid Labile P-N Bond

Toxicological Sciences

Volumn 132, Issue 2, 2013, Pages 390-398

  Jiang, Wei ^a   Cashman, John R ^b   Nachon, Florian ^c   Masson, Patrick ^a,c   Schopfer, Lawrence M ^a   Lockridge, Oksana ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b HUMAN BIOMOLECULAR RESEARCH INSTITUTE   (United States)

^c INSTITUT DE RECHERCHE BIOMÉDICALE DES ARMÉES   (France)

Author keywords

Aging; Dealkylation; Deamination; Iso OMPA; Mass spectrometry; Tabun

Indexed keywords

CHOLINESTERASE; ISO OMPA; TABUN; THIOCHOLINE; TRYPSIN;

AGING; ARTICLE; CHEMICAL BOND; DEALKYLATION; DEAMINATION; HUMAN; MASS SPECTROMETRY; PH; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; RACEMIC MIXTURE; STEREOCHEMISTRY; STEREOISOMERISM;

BUTYRYLCHOLINESTERASE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HUMANS; MASS SPECTROMETRY; NITROGEN; PHOSPHORUS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 84875235607     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kft011     Document Type: Article

References (26)

1. Barak, D., Ordentlich, A., Kaplan, D., Barak, R., Mizrahi, D., Kronman, C., Segall, Y., Velan, B., and Shafferman, A. (2000). Evidence for P-N bond scission in phosphoroamidate nerve agent adducts of human acetylcholinesterase. Biochemistry 39, 1156-1161.
2. Barakat, N. H., Zheng, X., Gilley, C. B., MacDonald, M., Okolotowicz, K., Cashman, J. R., Vyas, S., Beck, J. M., Hadad, C. M., and Zhang, J. (2009). Chemical synthesis of two series of nerve agent model compounds and their stereoselective interaction with human acetylcholinesterase and human butyrylcholinesterase. Chem. Res. Toxicol. 22, 1669-1679.
3. Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., Di Nola, A., and Haak, J. R. (1984). Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81, 3684-3690.
4. Carletti, E., Aurbek, N., Gillon, E., Loiodice, M., Nicolet, Y., Fontecilla-Camps, J. C., Masson, P., Thiermann, H., Nachon, F., and Worek, F. (2009). Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun. Biochem. J. 421, 97-106.
5. Carletti, E., Colletier, J. P., Dupeux, F., Trovaslet, M., Masson, P., and Nachon, F. (2010). Structural evidence that human acetylcholinesterase inhibited by tabun ages through O-dealkylation. J. Med. Chem. 53, 4002-4008.
6. Carletti, E., Li, H., Li, B., Ekström, F., Nicolet, Y., Loiodice, M., Gillon, E., Froment, M. T., Lockridge, O., Schopfer, L. M., et al. (2008). Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation. J. Am. Chem. Soc. 130, 16011-16020.
7. Elhanany, E., Ordentlich, A., Dgany, O., Kaplan, D., Segall, Y., Barak, R., Velan, B., and Shafferman, A. (2001). Resolving pathways of interaction of covalent inhibitors with the active site of acetylcholinesterases: MALDITOF/ MS analysis of various nerve agent phosphyl adducts. Chem. Res. Toxicol. 14, 912-918.
8. Ellman, G. L., Courtney, K. D., Andres, V., Jr, and Feather-Stone, R. M. (1961). A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7, 88-95.
9. Eswar, N., Webb, B., Marti-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M. Y., Pieper, U., and Sali, A. (2007). Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. Chapter 2, Unit 2.9.
10. Fidder, A., Hulst, A. G., Noort, D., de Ruiter, R., van der Schans, M. J., Benschop, H. P., and Langenberg, J. P. (2002). Retrospective detection of exposure to organophosphorus anti-cholinesterases: Mass spectrometric analysis of phosphylated human butyrylcholinesterase. Chem. Res. Toxicol. 15, 582-590.
11. Gilley, C., MacDonald, M., Nachon, F., Schopfer, L. M., Zhang, J., Cashman, J. R., and Lockridge, O. (2009). Nerve agent analogues that produce authentic soman, sarin, tabun, and cyclohexyl methylphosphonate-modified human butyrylcholinesterase. Chem. Res. Toxicol. 22, 1680-1688.
12. Hess, B., Bekker, H., Berendsen, H. J. C., and Fraaije, J. G. E. M. (1997). LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463-1472.
13. Hess, B., Kutzner, C., van der Spoel, D., and Lindhal, E. (2008). GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447.
14. Hornak, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A., and Simmerling, C. (2006). Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65, 712-725.
15. Kalisiak, J., Ralph, E. C., and Cashman, J. R. (2012). Nonquaternary reactivators for organophosphate-inhibited cholinesterases. J. Med. Chem. 55, 465-474.
16. Kalisiak, J., Ralph, E. C., Zhang, J., and Cashman, J. R. (2011). Amidineoximes: Reactivators for organophosphate exposure. J. Med. Chem. 54, 3319-3330.
17. Kweon, H. K., and Håkansson, K. (2006). Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis. Anal. Chem. 78, 1743-1749.
18. Liyasova, M., Li, B., Schopfer, L. M., Nachon, F., Masson, P., Furlong, C. E., and Lockridge, O. (2011). Exposure to tri-o-cresyl phosphate detected in jet airplane passengers. Toxicol. Appl. Pharmacol. 256, 337-347.
19. Lockridge, O., Schopfer, L. M., Winger, G., and Woods, J. H. (2005). Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys; a potential new therapeutic for protection against cocaine and nerve agent toxicity. J. Med. Chem. Biol. Radiol. Def. 3, nihms5095.
20. Nachon, F., Carletti, E., Worek, F., and Masson, P. (2010). Aging mechanism of butyrylcholinesterase inhibited by an N-methyl analogue of tabun: Implications of the trigonal-bipyramidal transition state rearrangement for the phosphylation or reactivation of cholinesterases. Chem. Biol. Interact. 187, 44-48.
21. Sielecki, A. R., Fedorov, A. A., Boodhoo, A., Andreeva, N. S., and James, M. N. (1990). Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution. J. Mol. Biol. 214, 143-170.
22. Sporty, J. L., Lemire, S. W., Jakubowski, E. M., Renner, J. A., Evans, R. A., Williams, R. F., Schmidt, J. G., van der Schans, M. J., Noort, D., and Johnson, R. C. (2010). Immunomagnetic separation and quantification of butyrylcholinesterase nerve agent adducts in human serum. Anal. Chem. 82, 6593-6600.
23. Tenberken, O., Thiermann, H., Worek, F., and Reiter, G. (2010a). Chromatographic preparation and kinetic analysis of interactions between tabun enantiomers and acetylcholinesterase. Toxicol. Lett. 195, 142-146.
24. Tenberken, O., Worek, F., Thiermann, H., and Reiter, G. (2010b). Development and validation of a sensitive gas chromatography-ammonia chemical ionization mass spectrometry method for the determination of tabun enantiomers in hemolysed blood and plasma of different species. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 878, 1290-1296.
25. van der Schans, M. J., Fidder, A., van Oeveren, D., Hulst, A. G., and Noort, D. (2008). Verification of exposure to cholinesterase inhibitors: Generic detection of OPCW Schedule 1 nerve agent adducts to human butyrylcholinesterase. J. Anal. Toxicol. 32, 125-130.
26. Wang, J., Wolf, R. M., Caldwell, J. W., Kollman, P. A., and Case, D. A. (2004). Development and testing of a general amber force field. J. Comput. Chem. 25, 1157-1174.