Gating as a control element in constrictive binding and guest release by hemicarcerands

Science

Volumn 273, Issue 5275, 1996, Pages 627-629

  Houk, K N ^a   Nakamura, Kensuke ^a   Sheu, Chimin ^a   Keating, Amy E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETONITRILE;

ARTICLE; CHANNEL GATING; CHEMICAL STRUCTURE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

EID: 0029747145     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5275.627     Document Type: Article

References (24)

1. D. J. Cram and J. M. Cram, Container Molecules and Their Guests (Royal Society of Chemistry, Cambridge, 1994). Carcerands are hosts that form complexes that cannot dissociate without breaking a bond in the host. Hemicarcerands form stable complexes (hemicarceplexes), but guest release occurs upon an increase in temperature.
2. S. H. Northrup, F. Zarrin, J. A. McCammon, J. Phys. Chem. 86, 2314 (1982); J. A. McCammon and S. H. Northrup, Nature 293, 316 (1981); R. C. Wade, M. E. Davis, B. A. Luty, J. D. Madura, J. A. McCammon, Biophys. J. 63, 9 (1993); C. Bouzat, N. Bren, S. M. Sine, Neuron 13, 1395 (1994); P. Y. S. Lam et al., Science 263, 380 (1994).
3. S. H. Northrup, F. Zarrin, J. A. McCammon, J. Phys. Chem. 86, 2314 (1982); J. A. McCammon and S. H. Northrup, Nature 293, 316 (1981); R. C. Wade, M. E. Davis, B. A. Luty, J. D. Madura, J. A. McCammon, Biophys. J. 63, 9 (1993); C. Bouzat, N. Bren, S. M. Sine, Neuron 13, 1395 (1994); P. Y. S. Lam et al., Science 263, 380 (1994).
4. S. H. Northrup, F. Zarrin, J. A. McCammon, J. Phys. Chem. 86, 2314 (1982); J. A. McCammon and S. H. Northrup, Nature 293, 316 (1981); R. C. Wade, M. E. Davis, B. A. Luty, J. D. Madura, J. A. McCammon, Biophys. J. 63, 9 (1993); C. Bouzat, N. Bren, S. M. Sine, Neuron 13, 1395 (1994); P. Y. S. Lam et al., Science 263, 380 (1994).
5. S. H. Northrup, F. Zarrin, J. A. McCammon, J. Phys. Chem. 86, 2314 (1982); J. A. McCammon and S. H. Northrup, Nature 293, 316 (1981); R. C. Wade, M. E. Davis, B. A. Luty, J. D. Madura, J. A. McCammon, Biophys. J. 63, 9 (1993); C. Bouzat, N. Bren, S. M. Sine, Neuron 13, 1395 (1994); P. Y. S. Lam et al., Science 263, 380 (1994).
6. S. H. Northrup, F. Zarrin, J. A. McCammon, J. Phys. Chem. 86, 2314 (1982); J. A. McCammon and S. H. Northrup, Nature 293, 316 (1981); R. C. Wade, M. E. Davis, B. A. Luty, J. D. Madura, J. A. McCammon, Biophys. J. 63, 9 (1993); C. Bouzat, N. Bren, S. M. Sine, Neuron 13, 1395 (1994); P. Y. S. Lam et al., Science 263, 380 (1994).
7. S. H. Northrup and J. A. McCammon, J. Am. Chem. Soc. 106, 930 (1984).
8. P. D. Kirchhoff et al., ibid. 118, 3237 (1996).
9. K. Nakamura and K. N. Houk, ibid. 117, 1853 (1995).
10. S. J. Weiner et al., ibid. 106, 765 (1984); S. J. Weiner, P. A. Kollman, D. A. Nguyen, J. Comput. Chem. 7, 230 (1980).
11. S. J. Weiner et al., ibid. 106, 765 (1984); S. J. Weiner, P. A. Kollman, D. A. Nguyen, J. Comput. Chem. 7, 230 (1980).
12. M. J. S. Dewar, E. G. Zoebisch, E. F. Healy, J. Am. Chem. Soc. 107, 3902 (1985).
13. GAUSSIAN94, A.1; M. J. Frisch et al., Gaussian, Pittsburgh, PA.
14. MACROMODEL, 4.5; W. C. Still, Columbia University; F. Mohamadi et al., J. Comput. Chem. 11, 440 (1990).
15. MACROMODEL, 4.5; W. C. Still, Columbia University; F. Mohamadi et al., J. Comput. Chem. 11, 440 (1990).
16. J. C. Sherman and D. J. Cram, J. Am. Chem. Soc. 113, 2194 (1991).
17. R. G. Chapman, N. Chopra, E. D. Cochien, J. C. Sherman, ibid. 116, 369 (1994).
18. Y.-S. Byun, O. Vadhat, M. T. Blanda, C. B. Knobler, D. J. Cram, Chem. Commun. 1995, 1825 (1995).
19. C. Sheu and K. N. Houk, J. Am. Chem. Soc., in press.
20. T. A. Robbins and D. J. Cram, Chem. Commun. 1995, 1515 (1995).
21. The absolute solvation energies of DMF and DMA in chloroform calculated by BOSS Monte Carlo simulations (BOSS, 3.5; W. L. Jorgensen, Yale University) are -7.1 and -5.8 kcal/mol, respectively. From simple addition of the solvation energies to the calculated activation energies for guest loss, ΔE‡, the activation energies for escape are estimated to be 24.6 kcal/mol for DMF and 21.9 kcal/mol for DMA, These values are close to the experimental values, considering that (i) solvation effects at the transition states are less than those of free guest molecules and (ii) the solvent used in the experiment (nitrobenzene) is more polar than that used in the calculation (chloroform).
22. D. J. Cram, M. T. Blanda, K. Paek, C. B. Knobler, J. Am. Chem. Soc. 114, 7765 (1992).
23. R. S. Meissner, J. Rebek Jr., J. de Mendoza, Science 270, 1485 (1995).
24. We are grateful to D. J. Cram and his research group for helpful and inspiring discussions. We thank the National Center for Supercomputing Applications at the University of Illinois at Urbana-Champaign and the UCLA Office of Academic Computing for computer facilities. Supported by NIH and a NSF graduate research fellowship (A.E.K.).