An Artificial Antiparallel β-Sheet Containing a New Peptidomimetic Template

Journal of Organic Chemistry

Volumn 62, Issue 23, 1997, Pages 7906-7907

  Smith, Eric M ^a   Holmes, Darren L ^a   Shaka, A J ^a   Nowick, James S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0000522923     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo971431b     Document Type: Article

References (18)

1. Nowick, J. S.; Smith, E. M.; Pairish, M. Chem. Soc. Rev. 1996, 25, 401.
2. Nowick, J. S.; Holmes, D. L.; Mackin, G.; Noronha, G.; Shaka, A. J.; Smith, E. M. J. Am. Chem. Soc. 1996, 118, 2764.
3. We have also reported a dimeric version of the 5-amino-2-methoxybenzamide template that is longer than a dipeptide and forms three hydrogen bonds to a tripeptide: Nowick, J. S.; Pairish, M.; Lee, I. Q.; Holmes, D. L.; Ziller, J. W. J. Am. Chem. Soc. 1997, 119, 5413.
4. Nowick, J. S.; Abdi, M.; Bellamo, K. A.; Love, J. A.; Martinez, E. J.; Noronha, G.; Smith, E. M.; Ziller, J. W. J. Am. Chem. Soc. 1995, 117, 89.
5. Holmes, D. L.; Smith, E. M.; Nowick, J. S. J. Am. Chem. Soc. 1997, 119, 7665.
6. Nowick, J. S.; Holmes, D. L.; Noronha, G.; Smith, E. M.; Nguyen, T. M.; Huang, S.-L. J. Org. Chem. 1996, 61, 3929.
7. These chemical shift studies were performed at 1.0 mM. At this concentration, negligible self-association occurs, and the observed chemical shifts are reflective of the unassociated compounds.
8. Nowick, J. S.; Smith, E. M.; Noronha, G. J. Org. Chem. 1995, 60, 7386.
9. (a) Hwang, T. L.; Shaka, A. J. J. Am. Chem. Soc. 1992, 114, 3157.
10. (b) Hwang, T. L.; Shaka, A. J. J. Magn. Reson. Series B 1993, 102, 155.
11. BX = 7.5 Hz, 1 H, 12), 3.48-3.41 (m, 1 H, 13), 3.56-3.45 (m, 2 H, 14 and 14′), 3.69-3.61 (m, 2 H, 15), 3.92-3.86 (m, 1 H, 16), 4.05 (s, 3 H, 17), 4.44 (td, J = 9.2, 5.7 Hz, 1 H, 18), 4.82 (d, J = 8.4 Hz, 1 H, 19), 4.94 (q, J = 8.2 Hz, 1 H, 20), 5.80 (br q, J = 4.7 Hz, 1 H, 21), 6.96-6.94 (m, 2 H, 22), 6.96 (d, J = 9.0 Hz, 1 H, 22′), 7.15 (appar d, J = 7.0 Hz, 2 H, 23), 7.29-7.23 (m, 3 H, 24), 7.36 (appar t, J = 7.2 Hz, 1 H, 25), 7.40 (appar t, J = 7.1 Hz, 2 H, 26), 8.28 (d, J = 9.2 Hz, 1 H, 27), 8.39 (dd, J = 9.0, 2.8 Hz, 1 H, 28), 8.62 (d, J = 2.8 Hz, 1 H, 29), 9.92 (s, 1 H, 30), 10.44 (d, J = 7.0 Hz, 1 H, 31), 10.97 (d, J = 7.5 Hz, 1 H, 32).
12. 2 dimension.) 1: 5 (m), 6 (s), 7 (s), 18 (m), 27 (w), 29 (w). 2: 5 (m), 6 (m), 7 (s), 18 (s), 27 (w). 3: 9 (m), 10 (s). 4: 9 (m), 10 (s). 5: 1 (s), 2 (m), 6 (s), 7 (m), 18 (m), 27 (m), 29 (w). 6: 1 (s), 2 (s), 5 (s), 18 (m), 27 (m). 7: 1 (s), 2 (s), 5 (m), 18 (m), 27 (m), 29 (w). 8: 14 (s), 14′(s). 9: 3 (m), 4 (m), 21 (s). 10: 3 (s), 4 (s), 31 (m). 11: 12 (s), 19 (s), 20 (s), 23 (m). 12: 11 (s), 19 (m), 20 (s), 23 (m). 13: 15 (s), 30 (m). 14: 8 (s), 14′ (s). 14′: 8(s), 14 (s). 15: 13 (s), 16 (s), 22 (m), 30 (s). 16: 15 (s), 22 (w), 30 (m). 17: 22′ (s). 78: 1 (m), 2 (s), 5 (m), 6 (m), 7 (m), 21 (s), 27 (m). 19: 11 (s), 12 (m), 22 (m), 23 (m), 27 (w), 29 (w). 20: 11 (s), 12 (s), 23 (s), 27(s), 29(m). 21: 9 (s), 18 (s), 27 (w). 22: 19 (s), 26 (s). 22′: 17 (s), 28(s). 23: 11 (s), 12 (s), 19 (m), 20 (s), 24 (s). 24: 23(s).26: 22 (s). 27: 5 (m), 6 (m), 7 (m), 18 (m), 19 (m), 20 (s), 21 (w). 28: 22′ (s), 30 (w). 29: 1 (w), 5 (w), 7 (w), 20 (s), 30 (s). 30: 13 (m), 15 (s), 16 (m), 28 (w), 29 (s). 31: 10 (m). 32: 17 (m).
13. Nowick, J. S.; Mahrus, S.; Smith, E. M.; Ziller, J. W. J. Am. Chem. Soc. 1996, 118, 1066.
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18. Michne, W. F.; Schroeder, J. D. Int. J. Peptide Protein Res. 1996, 47, 2.