A biomimetic approach to asymmetric acyl transfer catalysis

Journal of the American Chemical Society

Volumn 121, Issue 50, 1999, Pages 11638-11643

  Jarvo, Elizabeth R ^a   Copeland, Gregory T ^a   Papaioannou, Nikolaos ^a   Bonitatebus Jr , Peter J ^a   Miller, Scott J ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; OCTAPEPTIDE; TETRAPEPTIDE;

ACYLATION; ARTICLE; CATALYSIS; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; ENANTIOMER; HYDROGEN BOND; MODEL; MOLECULAR INTERACTION; NUCLEAR OVERHAUSER EFFECT; PROTON NUCLEAR MAGNETIC RESONANCE; RIGIDITY; STEREOCHEMISTRY; STRUCTURE ANALYSIS; X RAY ANALYSIS;

EID: 0033596302     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9931776     Document Type: Article

References (65)

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16. For representative examples, see: (a) Jeong, K.-S.; Muhldorf, A. V.; Rebek, J., Jr. J. Am. Chem. Soc. 1990, 112, 6144-6145. (b) Liu, R.; Sanderson, P. E. J.; Still, W. C. J. Org. Chem. 1990, 55, 5184-5186. (c) Cristofaro, M. F.; Chamberlin, A. R. J. Am. Chem. Soc. 1994, 116, 5089- 5098. (d) Garcia-Tellado, F.; Albert, J.; Fan, E.; Hamilton, A. D. J. Chem. Soc., Chem. Commun. 1991, 1761-1763. (e) Wilcox, C. S. Chem. Soc. Rev. 1993, 22, 383-395.
17. For representative examples, see: (a) Jeong, K.-S.; Muhldorf, A. V.; Rebek, J., Jr. J. Am. Chem. Soc. 1990, 112, 6144-6145. (b) Liu, R.; Sanderson, P. E. J.; Still, W. C. J. Org. Chem. 1990, 55, 5184-5186. (c) Cristofaro, M. F.; Chamberlin, A. R. J. Am. Chem. Soc. 1994, 116, 5089- 5098. (d) Garcia-Tellado, F.; Albert, J.; Fan, E.; Hamilton, A. D. J. Chem. Soc., Chem. Commun. 1991, 1761-1763. (e) Wilcox, C. S. Chem. Soc. Rev. 1993, 22, 383-395.
18. For representative enantioselective catalysts that rely exclusively on peptide or a peptide-like functionality, see: (a) Sigman, M. S.; Jacobsen, E. N. J. Am. Chem. Soc. 1998, 120, 4901-4902. (b) Iyer, M. S.; Gigstad, K. M.; Namdev, N. D.; Lipton, M. J. Am. Chem. Soc. 1996, 118, 4910- 4911. (c) Cleij, M. C.; Drenth, W.; Nolte, R. J. M. J. Org. Chem. 1991, 56, 3883-3891. (d) Tanaka, K.; Mori, A.; Inoue, S. J. Org. Chem. 1990, 55, 181-185. (e) Agami, C.; Puchot, C.; Sevestre, H. Tetrahedron Lett. 1986, 27, 1501-1504. (f) For a representative approach that involves a de novo designed protein, see: Broo, K. S.; Brive, L.; Ahlberg, P.; Baltzer, L. J. Am. Chem. Soc. 1997, 119, 11362-11372.
19. For representative enantioselective catalysts that rely exclusively on peptide or a peptide-like functionality, see: (a) Sigman, M. S.; Jacobsen, E. N. J. Am. Chem. Soc. 1998, 120, 4901-4902. (b) Iyer, M. S.; Gigstad, K. M.; Namdev, N. D.; Lipton, M. J. Am. Chem. Soc. 1996, 118, 4910-4911. (c) Cleij, M. C.; Drenth, W.; Nolte, R. J. M. J. Org. Chem. 1991, 56, 3883-3891. (d) Tanaka, K.; Mori, A.; Inoue, S. J. Org. Chem. 1990, 55, 181-185. (e) Agami, C.; Puchot, C.; Sevestre, H. Tetrahedron Lett. 1986, 27, 1501-1504. (f) For a representative approach that involves a de novo designed protein, see: Broo, K. S.; Brive, L.; Ahlberg, P.; Baltzer, L. J. Am. Chem. Soc. 1997, 119, 11362-11372.
20. For representative enantioselective catalysts that rely exclusively on peptide or a peptide-like functionality, see: (a) Sigman, M. S.; Jacobsen, E. N. J. Am. Chem. Soc. 1998, 120, 4901-4902. (b) Iyer, M. S.; Gigstad, K. M.; Namdev, N. D.; Lipton, M. J. Am. Chem. Soc. 1996, 118, 4910- 4911. (c) Cleij, M. C.; Drenth, W.; Nolte, R. J. M. J. Org. Chem. 1991, 56, 3883-3891. (d) Tanaka, K.; Mori, A.; Inoue, S. J. Org. Chem. 1990, 55, 181-185. (e) Agami, C.; Puchot, C.; Sevestre, H. Tetrahedron Lett. 1986, 27, 1501-1504. (f) For a representative approach that involves a de novo designed protein, see: Broo, K. S.; Brive, L.; Ahlberg, P.; Baltzer, L. J. Am. Chem. Soc. 1997, 119, 11362-11372.
21. For representative enantioselective catalysts that rely exclusively on peptide or a peptide-like functionality, see: (a) Sigman, M. S.; Jacobsen, E. N. J. Am. Chem. Soc. 1998, 120, 4901-4902. (b) Iyer, M. S.; Gigstad, K. M.; Namdev, N. D.; Lipton, M. J. Am. Chem. Soc. 1996, 118, 4910- 4911. (c) Cleij, M. C.; Drenth, W.; Nolte, R. J. M. J. Org. Chem. 1991, 56, 3883-3891. (d) Tanaka, K.; Mori, A.; Inoue, S. J. Org. Chem. 1990, 55, 181-185. (e) Agami, C.; Puchot, C.; Sevestre, H. Tetrahedron Lett. 1986, 27, 1501-1504. (f) For a representative approach that involves a de novo designed protein, see: Broo, K. S.; Brive, L.; Ahlberg, P.; Baltzer, L. J. Am. Chem. Soc. 1997, 119, 11362-11372.
22. For representative enantioselective catalysts that rely exclusively on peptide or a peptide-like functionality, see: (a) Sigman, M. S.; Jacobsen, E. N. J. Am. Chem. Soc. 1998, 120, 4901-4902. (b) Iyer, M. S.; Gigstad, K. M.; Namdev, N. D.; Lipton, M. J. Am. Chem. Soc. 1996, 118, 4910- 4911. (c) Cleij, M. C.; Drenth, W.; Nolte, R. J. M. J. Org. Chem. 1991, 56, 3883-3891. (d) Tanaka, K.; Mori, A.; Inoue, S. J. Org. Chem. 1990, 55, 181-185. (e) Agami, C.; Puchot, C.; Sevestre, H. Tetrahedron Lett. 1986, 27, 1501-1504. (f) For a representative approach that involves a de novo designed protein, see: Broo, K. S.; Brive, L.; Ahlberg, P.; Baltzer, L. J. Am. Chem. Soc. 1997, 119, 11362-11372.
23. For representative enantioselective catalysts that rely exclusively on peptide or a peptide-like functionality, see: (a) Sigman, M. S.; Jacobsen, E. N. J. Am. Chem. Soc. 1998, 120, 4901-4902. (b) Iyer, M. S.; Gigstad, K. M.; Namdev, N. D.; Lipton, M. J. Am. Chem. Soc. 1996, 118, 4910- 4911. (c) Cleij, M. C.; Drenth, W.; Nolte, R. J. M. J. Org. Chem. 1991, 56, 3883-3891. (d) Tanaka, K.; Mori, A.; Inoue, S. J. Org. Chem. 1990, 55, 181-185. (e) Agami, C.; Puchot, C.; Sevestre, H. Tetrahedron Lett. 1986, 27, 1501-1504. (f) For a representative approach that involves a de novo designed protein, see: Broo, K. S.; Brive, L.; Ahlberg, P.; Baltzer, L. J. Am. Chem. Soc. 1997, 119, 11362-11372.
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31. For representative, nonenzymatic enantioselective nucleophilic catalysts, see: (a) Vedejs, E.; Chen, X. J. Am. Chem. Soc. 1996, 118, 1809- 1810. (b) Vedejs, E.; Daugulis, O. J. Am. Chem. Soc. 1999, 121, 5813- 5814. (c) Tao, B.; Ruble, J. C.; Hoic, D. A.; Fu, G. C. J. Am. Chem. Soc. 1999, 121, 5091-5092. (d) Kawabata, T.; Nagato, M.; Takasu, K.; Fuji, K. J. Am. Chem. Soc. 1997, 119, 3169-3170. (e) Oriyama, T.; Imai, K.; Hosoya, T.; Sano, T. Tetrahedron Lett. 1998, 39, 397-400.
32. For representative, nonenzymatic enantioselective nucleophilic catalysts, see: (a) Vedejs, E.; Chen, X. J. Am. Chem. Soc. 1996, 118, 1809- 1810. (b) Vedejs, E.; Daugulis, O. J. Am. Chem. Soc. 1999, 121, 5813- 5814. (c) Tao, B.; Ruble, J. C.; Hoic, D. A.; Fu, G. C. J. Am. Chem. Soc. 1999, 121, 5091-5092. (d) Kawabata, T.; Nagato, M.; Takasu, K.; Fuji, K. J. Am. Chem. Soc. 1997, 119, 3169-3170. (e) Oriyama, T.; Imai, K.; Hosoya, T.; Sano, T. Tetrahedron Lett. 1998, 39, 397-400.
33. For representative, nonenzymatic enantioselective nucleophilic catalysts, see: (a) Vedejs, E.; Chen, X. J. Am. Chem. Soc. 1996, 118, 1809- 1810. (b) Vedejs, E.; Daugulis, O. J. Am. Chem. Soc. 1999, 121, 5813- 5814. (c) Tao, B.; Ruble, J. C.; Hoic, D. A.; Fu, G. C. J. Am. Chem. Soc. 1999, 121, 5091-5092. (d) Kawabata, T.; Nagato, M.; Takasu, K.; Fuji, K. J. Am. Chem. Soc. 1997, 119, 3169-3170. (e) Oriyama, T.; Imai, K.; Hosoya, T.; Sano, T. Tetrahedron Lett. 1998, 39, 397-400.
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42. Crystallographic data may be found in the Supporting Information.
43. Peptide 4 does not catalyze acyl transfer under the present conditions at an appreciable rate. This experiment rules out amide catalysis as the sole source of the reactivity and selectivity we observe: Titskii, G. D.; Litvinenko, L. M. Zh. Obshch. Khim. 1970, 40, 2680-2688.
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45. 8 See the Supporting Information for details.
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48. For comparative examples of the conformational influence of L-Pro vs D-Pro residues in short peptides, see: (a) Haque, T. S.; Little, J. C.; Gellman, S. H. J. Am. Chem. Soc. 1996, 118, 6975-6985. (b) Karle, I. L.; Awasthi, S. K.; Balaram, P. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 8189-8193. (c) Ragohothama, S. R.; Awasthi, S. K.; Balaram, P. J. Chem. Soc., Perkin Trans. 2 1998, 137-143.
49. For comparative examples of the conformational influence of L-Pro vs D-Pro residues in short peptides, see: (a) Haque, T. S.; Little, J. C.; Gellman, S. H. J. Am. Chem. Soc. 1996, 118, 6975-6985. (b) Karle, I. L.; Awasthi, S. K.; Balaram, P. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 8189- 8193. (c) Ragohothama, S. R.; Awasthi, S. K.; Balaram, P. J. Chem. Soc., Perkin Trans. 2 1998, 137-143.
50. Peptides were prepared according to standard solid-phase peptide synthesis protocols and purified by silica gel chromatography, or preparative HPLC. See the Supporting Information for details.
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61. Kinetic experiments were also carried out on the single enantiomers. Pseudo-first-order kinetics were observed in these experiments as well.
62. Under more concentrated conditions (200 mM in substrate), DMAP is more active than tetrapeptide 7. Since absolute selectivities are also lower with peptide catalysis at higher concentrations, we tentatively attribute this phenomenon to peptide-catalyst deactivation through aggregation. See the Supporting Information for details.
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