Effect of the electric field generated by the helix dipole on photoinduced intramolecular electron transfer in dichromophoric α-helical peptides

Journal of the American Chemical Society

Volumn 118, Issue 9, 1996, Pages 2299-2300

  Galoppini, Elena ^a   Fox, Marye Anne ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ELECTRON TRANSPORT; FLUORESCENCE; NUCLEAR MAGNETIC RESONANCE; PHOTOCHEMISTRY; PROTEIN STRUCTURE;

EID: 0029931828     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja951555a     Document Type: Article

References (40)

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7. 9 V/m is calculated from vacuum electrostatics. For a review on the role of α-helix dipole on protein function and structure, see: (a) Hol, W. G. J. Prog. Biophys. Mol. Biol. 1985, 45, 149. (b) Hol, W. G. J.; van Duijnen, P. T.; Berendsen, H. J. C. Nature 1978, 273, 443. (c) Wada, A. Adv. Biophys. 1976, 9, 1.
8. 9 V/m is calculated from vacuum electrostatics. For a review on the role of α-helix dipole on protein function and structure, see: (a) Hol, W. G. J. Prog. Biophys. Mol. Biol. 1985, 45, 149. (b) Hol, W. G. J.; van Duijnen, P. T.; Berendsen, H. J. C. Nature 1978, 273, 443. (c) Wada, A. Adv. Biophys. 1976, 9, 1.
9. 9 V/m is calculated from vacuum electrostatics. For a review on the role of α-helix dipole on protein function and structure, see: (a) Hol, W. G. J. Prog. Biophys. Mol. Biol. 1985, 45, 149. (b) Hol, W. G. J.; van Duijnen, P. T.; Berendsen, H. J. C. Nature 1978, 273, 443. (c) Wada, A. Adv. Biophys. 1976, 9, 1.
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14. (d) Boxer, S. G.; Goldstein, R. A.; Franzen. S. In Photoinduced Electron Transfer Part B. Experimental Techniques and Medium Effect: Fox. M. A., Chanon, M., Eds.; Elsevier: Amsterdam, 1988: p 163.
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18. (c) See supporting information for details about purification and characterization of 1-4.
19. (Ala)., peptides with n > 4 were nearly insoluble: Fox. M. A.; Meieri M. S.; Wall, C. G.; Miller. J. R. J. Org. Chem. 1991, 56, 5380. (Ala-Aib) peptides were selected for this work because of their solubility in organic solvents and their proclivity to form α -helices when n > 4.
20. 1o-helical. but empirical rules suggest that Ala-Aib peptides with less than 35% Aib content are α-helica (1 and 2 have a 28% Aib content): (a) Oyoda, K.; Kitakawa. Y.; Kimura. S.; Imanishi. Y. Biopolymers 1993, 33, 33. (b) Marshall, G. R.; Hodgkin, E. E.; Langs, D. A.; Smith, G. D., Zabrocky. J.; Leplawy, M. T. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 487. (c) Butters. T.; Hütter, P.; Jung, G.; Pauls, N.; Schmitt, H.; Sheldrick, G. M.; Winter, W. Angew, Chem., Int. Ed. Engl. 1981, 20, 889. (d) Karle, I. L.; Sukuman, M.; Balaram, P. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 9284.
21. 1o-helical. but empirical rules suggest that Ala-Aib peptides with less than 35% Aib content are α-helica (1 and 2 have a 28% Aib content): (a) Oyoda, K.; Kitakawa. Y.; Kimura. S.; Imanishi. Y. Biopolymers 1993, 33, 33. (b) Marshall, G. R.; Hodgkin, E. E.; Langs, D. A.; Smith, G. D., Zabrocky. J.; Leplawy, M. T. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 487. (c) Butters. T.; Hütter, P.; Jung, G.; Pauls, N.; Schmitt, H.; Sheldrick, G. M.; Winter, W. Angew, Chem., Int. Ed. Engl. 1981, 20, 889. (d) Karle, I. L.; Sukuman, M.; Balaram, P. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 9284.
22. 1o-helical. but empirical rules suggest that Ala-Aib peptides with less than 35% Aib content are α-helica (1 and 2 have a 28% Aib content): (a) Oyoda, K.; Kitakawa. Y.; Kimura. S.; Imanishi. Y. Biopolymers 1993, 33, 33. (b) Marshall, G. R.; Hodgkin, E. E.; Langs, D. A.; Smith, G. D., Zabrocky. J.; Leplawy, M. T. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 487. (c) Butters. T.; Hütter, P.; Jung, G.; Pauls, N.; Schmitt, H.; Sheldrick, G. M.; Winter, W. Angew, Chem., Int. Ed. Engl. 1981, 20, 889. (d) Karle, I. L.; Sukuman, M.; Balaram, P. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 9284.
23. 1o-helical. but empirical rules suggest that Ala-Aib peptides with less than 35% Aib content are α-helica (1 and 2 have a 28% Aib content): (a) Oyoda, K.; Kitakawa. Y.; Kimura. S.; Imanishi. Y. Biopolymers 1993, 33, 33. (b) Marshall, G. R.; Hodgkin, E. E.; Langs, D. A.; Smith, G. D., Zabrocky. J.; Leplawy, M. T. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 487. (c) Butters. T.; Hütter, P.; Jung, G.; Pauls, N.; Schmitt, H.; Sheldrick, G. M.; Winter, W. Angew, Chem., Int. Ed. Engl. 1981, 20, 889. (d) Karle, I. L.; Sukuman, M.; Balaram, P. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 9284.
24. Walton, A. G. Polypeptides and Protein Structure: Elsevier: New York, 1981; Chapter 6.
25. 1H NMR spectra were recorded in CDCl; using a General Electric GN-500 500 MHz spectrometer.
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27. max of exciplex emission of the system pyrene-dimethylaniline reported in the literature (450 nm). and it did not disappear upon dilution. Therefore, we conclude that the observed emission is due to an intramolecular exciplex.
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33. References 13b and 14b conclude that in peptide-appended chromophores electron transfer occurs through-space rather than through-bonds.
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35. The fluorescence quantum yields of 1 and 2 were calculated using the formula reported in the following: Eaton, D. F. Pure Appl. Chem. 1988, 60, 1107.
36. Short (5-15 amino acids) peptides can adopt rapidly interconverting conformations in solution, and biexponential decays were observed in some of the studies of electron transfer in peptides (refs 13a.b. 14b).
37. Although this effect has been observed in oligopeptides (n = 21 - 40), we have not tested the presence of a boundary effect in 1 and 2. for instance with a solvatochromic dye molecule tethered to the peptides in the same positions as the donor or acceptor.
38. (a) Hino, T.; Akazawa, H.; Masuhara, H.; Mataga, N. J. Phys. Chem. 1976, 80, 33.
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40. oxdma2 = 0.43 V.