Dose-response relations for unnatural amino acids at the agonist binding site of the nicotinic acetylcholine receptor: Tests with novel side chains and with several agonists

Molecular Pharmacology

Volumn 50, Issue 5, 1996, Pages 1401-1412

  Kearney, Patrick C ^a   Nowak, Mark W ^a   Zhong, Wenge ^b   Silverman, Scott K ^b   Lester, Henry A ^a   Dougherty, Dennis A ^b  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b California Institute of Technology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINIC AGENT; NICOTINIC RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING SITE; DOSE RESPONSE; DRUG RECEPTOR BINDING; NONHUMAN; PRIORITY JOURNAL; STOP CODON; STRUCTURE ACTIVITY RELATION; XENOPUS LAEVIS;

AMINO ACIDS; ANIMALS; BINDING SITES; KINETICS; MICE; MUTAGENESIS, SITE-DIRECTED; NICOTINIC AGONISTS; QUATERNARY AMMONIUM COMPOUNDS; RECEPTORS, NICOTINIC; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS LAEVIS;

EID: 0029811223     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (35)

1. Nowak, M. W., P. C. Kearney, J. R. Sampson, M. E. Saks, C. G. Labarca, S. K. Silverman, W. Zhong, J. Thorson, J. N. Abelson, N. Davidson, P. G. Schultz, D. A. Dougherty, and H. A. Lester. Nicotinic receptor binding site probed with unnatural amino-acid incorporation in intact cells. Science (Wash. D. C.) 268:439-442 (1995).
2. Noren, C. J., S. J. Anthony-Cahill, M. C. Griffith, and P. G. Schultz. A general method for site-specific incorporation of unnatural amino acids into proteins. Science (Wash. D. C.) 244:182-188 (1989).
3. Cornish, V. W., D. Mendel, and P. G. Schultz. Probing protein structure and Function with an expanded genetic code. Angew. Chem. Int. Ed. Engl. 34:621-633 (1995).
4. Karlin, A. Structure of nicotinic acetylcholine receptors. Curr. Opin. Neurobiol. 8:299-309 (1993).
5. Devillers-Thiéry, A., J. L. Galzi, J. L. Eiselé, S. Bertrand, D. Bertrand, and J. P. Changeux. Functional architecture of the nicotinic acetylcholine receptor: a prototype of ligand-gated ion channels. J. Membr. Biol. 136: 97-112 (1993).
6. Lester, H. A. The permeation pathway of neurotransmitter-gated ion channels. Ann. Rev. Biophys. Biomol. Struct. 21:267-292 (1992).
7. Labarca, C., M. W. Nowak, H. Zhang, L. Tang, P. Deshpande, and H. A. Lester. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature (Lond.) 376:514-516 (1995).
8. Sussman, J. L., M. Harel, F. Frolow, C. Oefner, A. Goldman, L. Toker, and I. Silman. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science (Wash. D. C.) 253:872-879 (1991).
9. Silman, I., M. Harel, P. Axelsen, M. Raves, and J. L. Sussman. Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents. Biochem. Soc. Trans. 22:745-749 (1994).
10. Dougherty, D. A., and D. A. Stauffer. Acetylcholine binding by a synthetic receptor: implications for biological recognition. Science (Wash. D. C) 250:1558-1560 (1990).
11. Dougherty, D. A. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science (Wash. D. C.) 271:163-168 (1996).
12. Tomaselli, G. F., J. T. McLaughlin, M. E. Jurman, E. Hawrot, and G. Yellen. Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys. J. 60:721-727 (1991).
13. Aylwin, M. L., and M. M. White. Ligand-receptor interactions in the nicotinic acetylcholine receptor probed using multiple substitutions at conserved tyrosines on the a subunit. FEBS Lett. 349:99-103 (1994).
14. Chen, J., Y. Zhang, G. Akk, S. Sine, and A. Auerbach. Activation kinetics of recombinant mouse nicotinic acetylcholine receptors: mutations of α-subunit tyrosine 190 affect both binding and gating. Biophys. J. 69:849-859 (1995).
15. Sine, S. M., P. Quiram, F. Papanikolaou, H.-J. Kreienkamp, and P. Taylor. Conserved tyrosines in the a subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists. J. Biol. Chem. 269:8808-8816 (1994).
16. Grodberg, J., and J. J. Dunn. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J. Bacteriol. 170:1245-1253 (1988).
17. Davanloo, P., A. H. Rosenberg, J. J. Dunn, and F. W. Studier. Cloning and expression of the gene for bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 81:2035-2039 (1984).
18. Gln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. J. Biol. Chem. 271:23169-23175 (1996).
19. Sampson, J. R., and O. C. Uhlenbeck. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. USA 85:1033-1037 (1988).
20. Quick, M. W., and H. A. Lester. Methods for the expression of excitability proteins in Xenopus oocytes, in Ion Channels of Excitable Cells (T. Narahashi, ed.). Academic Press, San Diego, 261-279 (1994).
21. England, T. E., A. G. Bruce, and O. C. Uhlenbeck. Specific labeling of 3′ termini of RNA with T4 RNA ligase. Methods Enzymol. 65:65-74 (1980).
22. Ellman, J., D. Mendel, S. Anthonycahill, C. J. Noren, and P. G. Schultz. Biosynthetic method for introducing unnatural amino-acids site-specifically into proteins. Methods Enzymol. 202:301-336 (1991).
23. Knittel, J. J., and X. He. Synthesis and resolution of novel 3′-substituted phenylalanine amides. Pept. Res. 3:176-181 (1990).
24. Cabri, W., I. Candiani, A. Bedeschi, S. Penco, and R. Santi. Alpha-regioselectivity in palladium-catalyzed arylation of acyclic enol ethers. J. Org. Chem. 57:1481-1486 (1992).
25. Myers, A. G., J. L. Gleason, and T. Y. Yoon. A practical method for the synthesis of D-alpha-amino or L-alpha-amino acids by the alkylation of (+)-pseudoephedrine or (-)-pseudoephedrine glycinamide. J. Am. Chem. Soc. 117:8488-8489 (1995).
26. Mecozzi, S., A. P. West, Jr., and D. A. Dougherty. Cation-π interactions in simple aromatics: electrostatics provide a predictive tool. J. Am. Chem. Soc. 118:2307-2308 (1996).
27. Mecozzi, S., A. P. West, Jr., and D. A. Dougherty. Cation-π interactions in aromatics of biological and medicinal interest: electrostatic potential surfaces as a useful qualitative guide. Proc. Natl. Acad. Sci. USA 98:10566-10571 (1996).
28. Charnet, P., C. Labarca, R. J. Leonard, N. J. Vogelaar, L. Czyzyk, A. Gouin, N. Davidson, and H. A. Lester. An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor. Neuron 2:87-95 (1990).
29. Revah, F., D. Bertrand, J.-L. Galzi, A. Devillers-Thiéry, C. Mulle, N. Hussy, S. Bertrand, M. Ballivet, and J.-P. Changeux. Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor. Nature (Lond.) 353:846-849 (1991).
30. Filatov, G. N., and M. M. White. The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating. Mol. Pharmacol. 48:379-384 (1995).
31. Unwin, N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1101-1124 (1993).
32. Unwin, N. Acetylcholine receptor channel imaged in the open state. Nature (Lond.) 373:37-43 (1995).
33. Thorson, J. S., E. Chapman, E. C. Murphy, P. G. Schultz, and J. K. Judice. Linear free energy analysis of hydrogen bonding in proteins. J Am. Chem. Soc. 117:1157-1158 (1995).
34. Thorson, J. S., E. Chapman, and P. G. Schultz. Analysis of hydrogen bonding strengths in proteins using unnatural amino acids. J. Am. Chem. Soc. 117:9361-9362 (1995).
35. Satow, Y., G. H. Cohen, E. A. Padlan, and D. R. Davies. Phosphocholine-binding immunoglobulin Fab McPC603. J. Mol. Biol. 190:593-604 (1986).