Design, synthesis and evaluation of poly-L-proline type-II peptide mimics based on the 3-azabicyclo[3.1.0]hexane system

Journal of Organic Chemistry

Volumn 64, Issue 2, 1999, Pages 330-331

  Zhang, Rui ^a   Madalengoitia, Jose S ^a  

^a UNIVERSITY OF VERMONT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; BICYCLO COMPOUND; PROLINE DERIVATIVE;

AMINO ACID SYNTHESIS; ARTICLE; NUCLEAR OVERHAUSER EFFECT; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

EID: 0033593541     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo981814p     Document Type: Article

References (20)

1. For a recent PPII review see: Siligardi, G.; Drake, A. F. Peptide Sci. 1995, 37, 281.
2. For recent examples of proteins that bind PPII helices see: (a) Raj, P. A.; Marcus, E.; Edgerton, M. Biochemistry 1996, 35, 4314. (b) Lee, C.- H.; Saksela, K.; Mirza, U. A.; Chait, B. T.; Kuriyan, J. Cell 1996, 85, 931. (c) Peng, S.; Kasahara, C.; Rickles, R. J.; Schreiber, S. L. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12408. (d) Jardetzky, T. S.; Brown, J. H.; Gorga, J. C.; Stern, L. J.; Urban, R. G.; Strominger, J. L.; Wiley: D. C. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 734. (e) Zeile, W. L.; Purich, D. L.; Southwick, F. S. J. Cell Biol. 1996, 133, 49.
3. For recent examples of proteins that bind PPII helices see: (a) Raj, P. A.; Marcus, E.; Edgerton, M. Biochemistry 1996, 35, 4314. (b) Lee, C.-H.; Saksela, K.; Mirza, U. A.; Chait, B. T.; Kuriyan, J. Cell 1996, 85, 931. (c) Peng, S.; Kasahara, C.; Rickles, R. J.; Schreiber, S. L. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12408. (d) Jardetzky, T. S.; Brown, J. H.; Gorga, J. C.; Stern, L. J.; Urban, R. G.; Strominger, J. L.; Wiley: D. C. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 734. (e) Zeile, W. L.; Purich, D. L.; Southwick, F. S. J. Cell Biol. 1996, 133, 49.
4. For recent examples of proteins that bind PPII helices see: (a) Raj, P. A.; Marcus, E.; Edgerton, M. Biochemistry 1996, 35, 4314. (b) Lee, C.- H.; Saksela, K.; Mirza, U. A.; Chait, B. T.; Kuriyan, J. Cell 1996, 85, 931. (c) Peng, S.; Kasahara, C.; Rickles, R. J.; Schreiber, S. L. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12408. (d) Jardetzky, T. S.; Brown, J. H.; Gorga, J. C.; Stern, L. J.; Urban, R. G.; Strominger, J. L.; Wiley: D. C. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 734. (e) Zeile, W. L.; Purich, D. L.; Southwick, F. S. J. Cell Biol. 1996, 133, 49.
5. For recent examples of proteins that bind PPII helices see: (a) Raj, P. A.; Marcus, E.; Edgerton, M. Biochemistry 1996, 35, 4314. (b) Lee, C.- H.; Saksela, K.; Mirza, U. A.; Chait, B. T.; Kuriyan, J. Cell 1996, 85, 931. (c) Peng, S.; Kasahara, C.; Rickles, R. J.; Schreiber, S. L. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12408. (d) Jardetzky, T. S.; Brown, J. H.; Gorga, J. C.; Stern, L. J.; Urban, R. G.; Strominger, J. L.; Wiley: D. C. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 734. (e) Zeile, W. L.; Purich, D. L.; Southwick, F. S. J. Cell Biol. 1996, 133, 49.
6. For recent examples of proteins that bind PPII helices see: (a) Raj, P. A.; Marcus, E.; Edgerton, M. Biochemistry 1996, 35, 4314. (b) Lee, C.- H.; Saksela, K.; Mirza, U. A.; Chait, B. T.; Kuriyan, J. Cell 1996, 85, 931. (c) Peng, S.; Kasahara, C.; Rickles, R. J.; Schreiber, S. L. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12408. (d) Jardetzky, T. S.; Brown, J. H.; Gorga, J. C.; Stern, L. J.; Urban, R. G.; Strominger, J. L.; Wiley: D. C. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 734. (e) Zeile, W. L.; Purich, D. L.; Southwick, F. S. J. Cell Biol. 1996, 133, 49.
7. (a) Zhang, R.; Brownewell, F.; Madalengoitia, J. S. J. Am. Chem. Soc. 1998, 120, 3894.
8. (b) Zhang, R.; Madalengoitia, J. S. Tetrahedron Lett. 1996, 37, 6235.
9. For cyclopropane ring constraints of amino acids see: (a) Martin, S. F.; Austin, R. E.; Oalmann, C. J.; Baker, W. R. Condon, S. L. deLara, E.; Rosenberg, S. H.; Spina, K. P.; Stein, H. H.; Cohen, J.; Kleinert, H. D. J. Med. Chem. 1992, 35, 1710. (b) Burgess, K.; Ho, K.-K.; Pettitt, B. M. J. Am. Chem. Soc. 1994, 116, 799.
10. For cyclopropane ring constraints of amino acids see: (a) Martin, S. F.; Austin, R. E.; Oalmann, C. J.; Baker, W. R. Condon, S. L. deLara, E.; Rosenberg, S. H.; Spina, K. P.; Stein, H. H.; Cohen, J.; Kleinert, H. D. J. Med. Chem. 1992, 35, 1710. (b) Burgess, K.; Ho, K.-K.; Pettitt, B. M. J. Am. Chem. Soc. 1994, 116, 799.
11. (a) For the leucine construct: gauche (-) = -60° and trans = 180°. Cα, Cβ, Cγ, and Cδ as well as the nitrogen and carbonyl carbon of leucine were chosen to be overlaid with the corresponding atoms on the PTAA.
12. (b) For PPII helices in which leucine residues have a χ1 angle gauche(-), and χ2 angles, gauche(-) and ∼ trans, see: Feng, S.; Chen, J. K. Yu, H.; Simon, J. A.; Schreiber, S. L. Science 1994, 266, 1241.
13. (c) Yu, H.; Chen, J. K.; Feng, S.; Dalgarno, D. C.; Brauer, A. W.; Schreiber, S. L. Cell 1994, 76, 933.
14. For the synthesis of 2: Zhang, R.; Madalengoitia, J. S. J. Org. Chem. 1999, 64, 547-555.
15. (a) Fujimoto, Y.; Irreverre, F.; Karle, J. M.; Karle, I. L.; Witkop, B. J. Am. Chem. Soc. 1971, 93, 3471.
16. (b) Abraham, R. J.; Gatti, G. Org. Magn. Reson. 1970, 2, 173.
17. Compound 11 exists as 7:3 mixture of trans/cis amide bond rotamers, respectively, while a cis rotamer is not detected in 6.
18. Energy minimization of the trans rotamer of 11 was performed with MMX version 6.0, Serena Software, Box 3076, Bloomington, IN 47402.
19. The -75° ± 30° tolerance for φ in the PPII conformation is according to: Adzhubei, A. A.; Sternberg, M. J. Mol. Biol. 1993, 229, 472.
20. The designation i denotes the N-terminal residue.