Synthesis of peptides containing α, β-didehydroamino acids. Scope and limitations

Letters in Peptide Science

Volumn 9, Issue 2-3, 2002, Pages 135-141

  Jiménez, Jose C ^a   Bayó, Nuria ^a   Chavarría, Bibiana ^a   López Maciàu, Àngel ^a,b   Royo, Miriam ^a   Nicolás, Ernesto ^a   Giralt, Ernest ^a   Albericio, Fernando ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

^b PHARMAMAR S A   (Spain)

Author keywords

Carbodiimides; Dehydroamino acids; Dehydropeptides; Side reactions; Solid phase

Indexed keywords

ALPHA,BETA DIDEHYDROAMINO ACID DERIVATIVE; AMINO ACID DERIVATIVE; COPPER CHLORIDE; CYANAMIDE; UNCLASSIFIED DRUG; WATER;

CHEMICAL REACTION; CHEMICAL STRUCTURE; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; CYCLIZATION; ENZYME DEGRADATION; MARINE ENVIRONMENT; PEPTIDE SYNTHESIS; SOLID STATE; SOLUBILITY; STEREOCHEMISTRY;

EID: 0242500408     PISSN: 09295666     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1024124412866     Document Type: Conference Paper

References (52)

1. Gross, E., Adv. Exp. Med. Biol., 86B (1976) 131.
2. Schmidt, U., Häusler, J., Öhler, E. and Poisel, H., Fortschr. Chem. Org., 37 (1977) 251.
3. Noda, K., Shimohigashi, Y. and Izumiya, N., in The Peptides, Vol. 5, E. Gross and J. Meienhofer (eds), Academic Press, New York, 1983, p. 285.
4. Hamann, M. T. and Scheuer, P. J., J. Am. Chem. Soc., 115 (1993) 5825.
5. Goetz, G., Nakao, Y., and Scheuer, P. J., J. Nat. Prod., 60 (1997) 562.
6. Jung, G., Angew. Chem. Int. Ed. Engl., 30 (1991) 1051.
7. Jain, R. and Chauan, V. S., Biopolymers (Peptide Science), 40 (1996) 105.
8. Inai, Y., Kurokawa, Y., Ida, A. and Hirabayashi, T., Bull. Chem. Soc. Jpn., 71 (1999) 55.
9. Shimohigashi, Y., English, M. L., Stammer, C. H. and Costa, T., Biochem. Biophys. Res. Commun., 104 (1982) 583.
10. Brady, S. F., Cochran, D. W., Nutt, R. F., Holly, F. W., Bennett, C. D., Paleveda, W. J., Curley, P. E., Arison, B. H., Saperstein, R. and Veber, D. F., Int. J. Pept. Prot. Res., 23 (1984) 212.
11. Greiner, G., Dornberger, U., Paegelow, I., Scholkens, B. A., Liebmann, C. and Reissmann, S. J., Pept. Sci., 4 (1998) 92.
12. Rzeszotarska, B., Siodlak, D., Broda, M. A., Dybala, I. and Koziol, A. E., J. Pept. Res., 59 (2002) 79.
13. Cativiela, C., Diaz-de-Villegas, M. D. and Jiménez, A. I., Tetrahedron, 50 (1994) 9157.
14. Trost, B. M. and Dake, G. R., J. Am. Chem. Soc., 119 (1997) 7595.
15. Yim, A. M., Vidal, Y., Viallefont, P. and Martinez, J., Tetrahedron Lett., 40 (1999) 4535.
16. Chinchilla, R., Falvello, L. R., Galindo, N. and Nájera, C., J. Org. Chem., 65 (2000) 3034.
17. Burrage, S., Raynham, T., Williams, G., Essex, J. W., Allen, C., Cardno, M., Swali, V. and Bradley, M., Chem. Eur. J., 6 (2000) 1455.
18. Ogura, H., Sato, O. and Takeda, K., Tetrahedron Lett., 22 (1981) 4817.
19. Ferreira, P. M. T., Maia, H. L. S. and Monteiro, L. S., Tetrahedron Lett., 39 (1998) 9575.
20. 2-DDAA-OtBu.
21. López-Macià, A., Ph.D. Dissertation, University of Barcelona, Spain, 2000.
22. Moriya, T., Yoneda, N., Miyoshi, M. and Matsumoto, K., J. Org. Chem., 47 (1982) 94.
23. Shin, C., Yonezawa, Y., Yamada, Y., Chem. Pharm. Bull., 32 (1984) 3934.
24. In the case of residues containing stable double bonds, such as didehydrophenylalanine or didehydroleucine, partial incorporation of the next protected amino acid has been accomplished. W. van den Nest and C. Carreño, unpublished results.
25. α-ketoacid peptide, which shows that the hydrolysis of the enamine has taken place. See Ref. [21] and R. Jacquier and J. Verducci, Tetrahedron Lett., 25 (1984) 2775.
26. Yamada, M., Miyajima, T. and Horikawa, H., Tetrahedron Lett., 38 (1998) 289.
27. Horikawa, E., Kodaka, M., Nakahara, Y., Okuno, H. and Nakamura, K., Tetrahedron Lett., 42 (2001) 8337.
28. Nakamura, K., Ohnishi, Y., Horikawa, E., Kodaka, M., Okuno, H., 27th European Peptide Symposium, Sorrento, Italia, 2002.
29. Thieriet, N., Guibé, F. and Albericio, F., Org. Lett., 2 (2000) 1815.
30. The Cys residue can be used to generate didehydroalanine through activation of either the free thiol or the Smethylcysteine by oxidation to sulfone. S. A. Burrage, T. Raynham and M. Bradley, Tetrahedron Lett., 39 (1998) 2831.
31. Blettner and Bradley have described a method based in the use of Asn as a precursor of didehydroalanine, which is formed by sequential application of a Hofmann-type degradation of the side chain amide of the Asn, followed by a Hofmann elimination reaction. C. Blettner and M. Bradley, Tetrahedron Lett., 35 (1994) 467.
32. Fukase, K., Kitazawa, M., Sano, A., Shimbo, K., Horimoto, S., Fujita, H., Kubo, A., Wakamiya, T. and Shibe, A., Bull. Chem. Soc. Jpn., 65 (1992) 2227.
33. Royo, M., Jiménez, J., López-Macià, A., Giralt, E. and Albericio, F., Eur. J. Org. Chem., (2001) 45.
34. López-Macià, A., Jiménez, J., Royo, M., Giralt, E. and Albericio, F., J. Am. Chem. Soc., 123 (2001) 11398.
35. Bayó, N., Jiménez, J. C., Rivas, L., Nicolás, E. and Albericio, F., Chem. Eur. J., in press.
36. Another soluble carbodiimide [1-cyclohexyl-3-(2morpholinoethyl)-carbodiimide metho-p-toluenosulfonate] has also been used for the dehydration in solution of peptides containing residues of Ala and Cys. M. J. Miller, J. Org. Chem., 45 (1980) 3131.
37. Goodall, K. and Parsons, A., Tetrahedron Lett., 36 (1995) 3259.
38. Li, K. W., Wu, J., Xing, W. and Simon, J. A., J. Am. Chem. Soc., 118 (1996) 7237.
39. Cherney, R. J. and Wang, L. J., Org. Chem., 61 (1996) 2544.
40. Somekh, L. and Shanzer, A., J. Org. Chem., 48 (1983) 907.
41. Alexandre, C. and Rouessac, D., Bull. Soc. Chim. Fr., 5 (1971) 1837.
42. Makowski, M., Rzeszotarska, B., Kubica, Z., Pietrzynski, G. and Hepter, J., Liebigs Ann. Chem., (1986) 980.
43. Carpino, L. A., El-Faham, A., Minor, C. A. and Albericio, F., J. Chem. Soc., Chem. Commun., (1994) 201.
44. Gausepohl, H., Pieles, U. and Frank, R. W., in Peptides - Chemistry and Biology, Proceedings of the 12th American Peptide Symposium, J. A. Smith and J. E. Rivier (eds), ESCOM, Science, Leiden, 1992, p. 523.
45. Story, S. C. and Aldrich, J. V., Int. J. Peptide Protein Res., 43 (1994) 292.
46. Albericio, F., Bofill, J. M., El-Faham, A. and Kates, S. A., J. Org. Chem., 63 (1998) 9678.
47. Del Fresno, M., El-Faham, A., Carpino, L. A., Royo, M. and Albericio, F., Org. Lett., 2 (2000) 3539.
48. The Alloc group is preferred because Alloc-containing compounds are more convenient to use in solution than the Fmoc derivatives. While the Alloc group has always given good results, on some occasions the presence of the Fmoc has not been compatible with the reaction conditions.
49. An orthogonal system is defined as a set of completely independent classes of protecting groups, such that each class of group can be removed in any order and in the presence of all other classes (G. Barany and F. Albericio, J. Am. Chem. Soc., 107 (1985) 4936, and references cited therein).
50. Removal of the methyl group in the presence of the Fmoc group is not always a straightforward operation.
51. This is a sequence of the cyclic tetrapeptide tentoxin. Jiménez, J. C., Chavarría, B., López-Macià, A., Royo, M., Giralt, E. and Albericio, F., 27th European Peptide Symposium, Sorrento, Italia, 2002.
52. Okada, Y. Houben-Weyl, Methods of Organic Chemistry. Vol. E22a. Synthesis of Peptides and Peptidomimetics. M. Goodman, A. Felix, L. Moroder and L. Toniolo (eds), Thieme, Stuttgart, New York, 2002, p. 591.