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Name: Charles Thompson

Title: Professor


Phone: 406-243-4643

Office: SB 477A

Lab Phone: 406-243-4125

Lab: SB 471


After completing undergraduate studies in chemistry at Rutgers University in New Jersey, Professor Thompson earned a M.S. and Ph.D. under the auspices of Professor T. Roy Fukuto at the University of California, Riverside. He also conducted post-doctoral training under the supervision of Professor E.J. Corey at Harvard University in 1982, and also with Professor Henry Rapoport at the University of California at Berkeley from 1983-1985. Professor Thompson is a medicinal and bioorganic chemist with interests in biologically active compounds. Additionally, he is the director of the Mass Spectrometry and Proteomics Facility located in the new addition of the Skaggs Building.


Research Statement

Medicinal and bioorganic chemistry, synthesis and investigation of novel probes of enzyme structure and function, protein mass spectrometry & proteomics, enzyme inhibition and binding kinetics, pharmacophore development and computational modeling of proteins, immunoorganic chemistry.

Glutamate Neurotransmitter System:

We design and synthesize custom-tailored glutamate analogs to study and differentiate the pharmacology of the glutamate neurotransmitter system proteins, in particular, the excitatory amino acid transporters (EAAT) and glutamate vesicular transporter (VGLUT1). Research in our group also has focused on solving the proteome (the protein complement of the gene) complement of the neuronal vesicle. Using 2D electrophoresis and mass spectrometric fingerprinting techniques (trypsin digest), proteins in the vesicle system are identified via bioinformatics databases.

Mechanism of Toxicity of Organophosphate Insecticides:

We treated a neuroblastoma cell line (model system) with reactive and non-reactive OPs and are isolating and identifying OP-modified proteins using mass spectrometry. Since OPs modify acetylcholinesterase (AChE) at an essential serine, we selected an AChE active site sequence and chemically phosphorylated it at the catalytically important serine hydroxyl group. The native peptide sequence and phosphorylated sequence were used as haptens for antibody production. Our goal is to characterize and utilize polyclonal antibodies to differentiate between native and OP-modified AChE.

Other Areas of Interest:

a. Synthesis of phosphorus-containing analogs of alpha amino acids and their utility as inhibitors of matrix metalloproteinases.

b. Synthesis and utility of novel protein probes (fluorescent, UV-Vis, spin label, etc.).

For further research details see:



Bharate, S. B., Guo, L., Reeves, T. E., Cerasoli, D. M., and Thompson, C. M. (2009) New series of monoquaternary pyridinium oximes: Synthesis and reactivation potency for paraoxon-inhibited electric eel and recombinant human acetylcholinesterase, Bioorg Med Chem Lett 19, 5101-5104.

Diaz, P., Phatak, S. S., Xu, J., Fronczek, F. R., Astruc-Diaz, F., Thompson, C. M., Cavasotto, C. N., and Naguib, M. (2009) 2,3-Dihydro-1-benzofuran derivatives as a series of potent selective cannabinoid receptor 2 agonists: design, synthesis, and binding mode prediction through ligand-steered modeling, ChemMedChem 4, 1615-1629.

Grigoryan, H., Schopfer, L. M., Peeples, E. S., Duysen, E. G., Grigoryan, M., Thompson, C. M., and Lockridge, O. (2009) Mass spectrometry identifies multiple organophosphorylated sites on tubulin, Toxicol Appl Pharmacol 240, 149-158.

Guo, L., Thompson, C. M., and Twamley, B. (2009) Diastereomers (R(C),S(P))- and (R(C),R(P))-S-methyl P-(3-azidopropyl)-N-[(1R)-1-phenylethyl]phosphonamidothioate, Acta Crystallogr C 65, o179-182.

Li, B., Schopfer, L. M., Grigoryan, H., Thompson, C. M., Hinrichs, S. H., Masson, P., and Lockridge, O. (2009) Tyrosines of human and mouse transferrin covalently labeled by organophosphorus agents: a new motif for binding to proteins that have no active site serine, Toxicol Sci 107, 144-155.

Mullins, J. E., Etoga, J. L., Gajewski, M., Degraw, J. I., and Thompson, C. M. (2009) Unexpected Formation of Highly Functionalized Dihydropyrans via Addition-Cyclization Reactions Between Dimethyl Oxoglutaconate and alpha,beta-Unsaturated Hydrazones, Tetrahedron Lett 50, 2298-2300.

Bharate, S. B., Guo, L., Reeves, T. E., Cerasoli, D. M., and Thompson, C. M. (2010) Bisquaternary pyridinium oximes: Comparison of in vitro reactivation potency of compounds bearing aliphatic linkers and heteroaromatic linkers for paraoxon-inhibited electric eel and recombinant human acetylcholinesterase, Bioorg Med Chem 18, 787-794.

Etoga, J. L., Ahmed, S. K., Patel, S., Bridges, R. J., and Thompson, C. M. (2010) Conformationally-restricted amino acid analogues bearing a distal sulfonic acid show selective inhibition of system x(c)(-) over the vesicular glutamate transporter, Bioorg Med Chem Lett 20, 2680-2683.

Guo, L., Suarez, A. I., Braden, M. R., Gerdes, J. M., and Thompson, C. M. (2010) Inhibition of acetylcholinesterase by chromophore-linked fluorophosphonates, Bioorg Med Chem Lett 20, 1194-1197.

Guo, L., Suarez, A. I., and Thompson, C. M. (2010) Inactivation of acetylcholinesterase by various fluorophores, J Enzyme Inhib Med Chem 25, 116-120.

Proskocil, B. J., Bruun, D. A., Thompson, C. M., Fryer, A. D., and Lein, P. J. (2010) Organophosphorus pesticides decrease M2 muscarinic receptor function in guinea pig airway nerves via indirect mechanisms, PLoS ONE 5, e10562.

Thompson, C. M., Prins, J. M., and George, K. M. (2010) Mass spectrometric analyses of organophosphate insecticide oxon protein adducts, Environ Health Perspect 118, 11-19.

Ye, R., Rhoderick, J. F., Thompson, C. M., and Bridges, R. J. (2010) Functional expression, purification and high sequence coverage mass spectrometric characterization of human excitatory amino acid transporter EAAT2, Protein Expression and Purification, 74, 49-59.

Bharate, S. B., Prins, J. M., George, K. M., and Thompson, C. M. (2010) Thionate versus Oxon: Comparison of Stability, Uptake, and Cell Toxicity of (14CH3O)2-Labeled Methyl Parathion and Methyl Paraoxon with SH-SY5Y Cells, J. Agric. Food Chem. 58, 8460-8466.

Prins, J.; Brooks, D.; Thompson, C.M.; Lurie, D. (2010) Chronic low-level Pb exposure during development decreases the expression of the voltage dependent anion channel in auditory neurons of the brainstem. Neurotoxicology. 31, 662-673.

Prins, J.M.; George, K.M.; Thompson, C.M. (2010) Paraoxon-induced protein expression changes to SH-SY5Y cells. Chem. Res. Toxicol. 23, 1656–1662.

Bharate, S.B.; Thompson, C.M. (2010) Antimicrobial, antimalarial and antileishmanial activities of mono- and bisquaternary pyridinium compounds. Chem. Biol. Drug Design. 76, 546-551.

The University of Montana-Missoula
The Department of Biomedical & Pharmaceutical Sciences
32 Campus Drive, Skaggs 395
Missoula, MT 59812-1552
Phone 406.243.4767 Fax: 406.243.5228

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