Acetylcholinesterase: Mechanisms of covalent inhibition of H447I mutant determined by computational analyses

Chemico-Biological Interactions

Volumn 175, Issue 1-3, 2008, Pages 196-199

  Cheng, Y H ^a   Cheng, X L ^a   Radic Z ^a   McCammon, J A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Ab initio QM MM; Charge relayer; Free energy calculations; Molecular dynamics

Indexed keywords

ACETYLCHOLINESTERASE; MUTANT PROTEIN; WATER;

AB INITIO CALCULATION; ACYLATION; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; CHOLINESTERASE INHIBITION; ENERGY; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; MOUSE; NONHUMAN; QUANTUM MECHANICS;

ACETYLCHOLINESTERASE; ANIMALS; CATALYSIS; CHOLINESTERASE INHIBITORS; MICE; MODELS, MOLECULAR; MUTATION; QUANTUM THEORY;

EID: 50649114879     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.04.044     Document Type: Article

References (24)

1. Rosenberry T.L. Acetylcholinesterase. Adv. Enzymol. Relat. Areas Mol. Biol. 43 (1975) 103-218
2. Schumacher M., Camp S., Maulet Y., Newton M., Macpheequigley K., Taylor S.S., Friedmann T., and Taylor P. Primary structure of acetylcholinesterase-implications for regulation and function. Fed. Proc. 45 (1986) 2976-2981
3. Taylor P. The Pharmacological Basis of Therapeutics (1985), McMillan, New York
4. Contestabile A., Fila T., Bartesaghi R., Contestabile A., and Ciani E. Choline acetyltransferase activity at different ages in brain of ts65dn mice, an animal model for Down's syndrome and related neurodegenerative diseases. J. Neurochem. 97 (2006) 515-526
5. Piazzi L., Rampa A., Bisi A., Gobbi S., Belluti F., Cavalli A., Bartolini M., Andrisano V., Valenti P., and Recanatini M. 3-(4-{[Benzyl(methyl)amino]methyl}-phenyl)-6,7-dimethoxy-2H-2-chromenone (ap2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation: a dual function lead for Alzheimer's disease therapy. J. Med. Chem. 46 (2003) 2279-2282
6. Bachurin S.O. Medicinal chemistry approaches for the treatment and prevention of Alzheimer disease Med. Res. Rev. 23 (2003) 48-88
7. Sramek J.J., Zarotsky V., and Cutler N.R. Review of drug development and therapeutic role of cholinesterase inhibitors in Alzheimer's disease. Drug Dev. Res. 56 (2002) 347-353
8. Kryger G., Silman I., and Sussman J.L. Structure of acetylcholinesterase complexed with e2020 (aricept (r)): implications for the design of new anti-Alzheimer drugs. Struct. Fold. Des. 7 (1999) 297-307
9. Egan T.M., and North R.A. Acetylcholine hyperpolarizes central neurons by acting on an m2 muscarinic receptor. Nature 319 (1986) 405-407
10. Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., and Silman I. Atomic-structure of acetylcholinesterase from torpedo-californica-a prototypic acetylcholine-binding protein. Science 253 (1991) 872-879
11. Bazelyansky M., Robey E., and Kirsch J.F. Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry 25 (1986) 125-130
12. Hasinoff B.B. Kinetics of acetylthiocholine binding to electric-eel acetylcholinesterase in glycerol water solvents of increased viscosity-evidence for a diffusion-controlled reaction. Biochim. Biophys. Acta 704 (1982) 52-58
13. Nolte H.J., Rosenberry T.L., and Neumann E. Effective charge on acetylcholinesterase active-sites determined from the ionic-strength dependence of association rate constants with cationic ligands. Biochemistry 19 (1980) 3705-3711
14. Amino acids and numbers refer to mouse or human AChE, and the numbers in parentheses refer to the positions of analogous residues in TcAChE.
15. Kua J., Zhang Y.K., and McCammon J.A. Studying enzyme binding specificity in acetylcholinesterase using a combined molecular dynamics and multiple docking approach. J. Am. Chem. Soc. 124 (2002) 8260-8267
16. G.M. Morris, D.S. Goodsell, R.S. Halliday, R. Huey, W.E. Hart, R.K. Belew, A.J. Olson, Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function, 19 (1998) 1639-1662.
17. Eriksson M.A.L., and Nilsson L. Structural and dynamic differences of the estrogen receptor DNA binding domain, binding as a dimer and as a monomer to DNA: molecular dynamics simulation studies. Eur. Biophys. J. Biophys. Lett. 28 (1999) 102-111
18. Sheu S.Y., Yang D.Y., Selzle H.L., and Schlag E.W. Energetics of hydrogen bonds in peptides. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 12683-12687
19. Zhang Y.K., Liu H.Y., and Yang W.T. Free energy calculation on enzyme reactions with an efficient iterative procedure to determine minimum energy paths on a combined ab initio QM/MM potential energy surface. J. Chem. Phys. 112 (2000) 3483-3492
20. Zhang Y.K., Lee T.S., and Yang W.T. A pseudobond approach to combining quantum mechanical and molecular mechanical methods. J. Chem. Phys. 110 (1999) 46-54
21. 0, respectively; [X-Y] and [X·Y] represent the covalent and noncovalent complexes of the X enzyme and Y ligand, respectively.
22. Radić Z., Quinn D.M., McCammon J.A., and Taylor P. J. Biol. Chem. 272 (1997) 23265-23277
23. Radić Z., and Taylor P. J. Biol. Chem. 276 (2001) 4622-4633
24. Cheng Y.H., Cheng X.L., Radić Z., and McCammon J.A. J. Am. Chem. Soc. 129 (2007) 6562-6570