D-Amino acids in protein de novo design. II. Protein-diastereomerism versus protein-enantiomerism

Letters in Peptide Science

Volumn 4, Issue 4-6, 1997, Pages 377-386

  Haack, Thomas ^a   González, Ma José ^a   Sánchez, Yolanda ^a   Giralt, Ernest ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

Author keywords

D Amino acids; De novo design; Diastereoproteins; Peptides; Proteins

Indexed keywords

EID: 1642411877     PISSN: 09295666     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02442903     Document Type: Article

References (36)

1. Among these exceptions, in prokaryotes, the use of D-amino acids in bacterial cell-walls is well known. In eukaryotes, recently, several receptor agonists and neuroactive tetrapeptides containing a D-amino acid residue have been isolated from amphibian and mollusc. These peptides are synthesized via post-translational enzymatic epimerization from an all-L precursor: Heck, S.D., Faraci, W.S., Kelbaugh, P.R., Saccomano, N.A., Thadeio, P.F. and Volkmann, R.A., Proc. Natl. Acad. Sci. USA, 93 (1996) 4036; reviews: Lamzin, V.S., Dauter, Z. and Wilson, K.S., Curr. Opin. Struct. Biol., 5 (1995) 830; Mor, A., Amiche, M. and Nicolas, P., Trends Biochem. Sci., 17 (1992) 481. For other examples of racemases, but from prokaryotic origin, see References 3 and 4.
2. Among these exceptions, in prokaryotes, the use of D-amino acids in bacterial cell-walls is well known. In eukaryotes, recently, several receptor agonists and neuroactive tetrapeptides containing a D-amino acid residue have been isolated from amphibian and mollusc. These peptides are synthesized via post-translational enzymatic epimerization from an all-L precursor: Heck, S.D., Faraci, W.S., Kelbaugh, P.R., Saccomano, N.A., Thadeio, P.F. and Volkmann, R.A., Proc. Natl. Acad. Sci. USA, 93 (1996) 4036; reviews: Lamzin, V.S., Dauter, Z. and Wilson, K.S., Curr. Opin. Struct. Biol., 5 (1995) 830; Mor, A., Amiche, M. and Nicolas, P., Trends Biochem. Sci., 17 (1992) 481. For other examples of racemases, but from prokaryotic origin, see References 3 and 4.
3. Among these exceptions, in prokaryotes, the use of D-amino acids in bacterial cell-walls is well known. In eukaryotes, recently, several receptor agonists and neuroactive tetrapeptides containing a D-amino acid residue have been isolated from amphibian and mollusc. These peptides are synthesized via post-translational enzymatic epimerization from an all-L precursor: Heck, S.D., Faraci, W.S., Kelbaugh, P.R., Saccomano, N.A., Thadeio, P.F. and Volkmann, R.A., Proc. Natl. Acad. Sci. USA, 93 (1996) 4036; reviews: Lamzin, V.S., Dauter, Z. and Wilson, K.S., Curr. Opin. Struct. Biol., 5 (1995) 830; Mor, A., Amiche, M. and Nicolas, P., Trends Biochem. Sci., 17 (1992) 481. For other examples of racemases, but from prokaryotic origin, see References 3 and 4.
4. Mason, S.F., Nature, 311 (1984) 19.
5. Matthew, E., Zhi, J.Z. and Freundlich, M., J. Bacteriol., 178 (1996) 7234.
6. Yohda, M., Endo, I., Abe, Y., Ohta, T., Lida, T., Maruyama, T. and Kagawa, Y., J. Biol. Chem., 271 (1996) 22017.
7. All the genetically coded amino acids have only one stereogenic atom (the α-carbon atom), with the exception of isoleucine and threonine. In these two cases, the β-carbon is also stereogenic. The configuration of natural L-isoleucine is 2S, 3S and that of L-threonine 2S, 3R. The configuration of D-isoleucine is 2R, 3R and that of D-threonine is 2R, 3S.
8. Milton, R.C.D., Milton, S.C.F. and Kent, S.B.H., Science, 256 (1992) 1445.
9. Fitzgerald, M.C., Chermushevich, I., Standing, K.G., Kent, S.B.H. and Whitman, C.P., J. Am. Chem. Soc., 117 (1995) 11075.
10. Canne, L.E., Figliozzi, G.M., Robson, B., Siani, M.A., Thompson, D.A., Kent, S. and Simon, R.J., In Proceedings of the 24th European Peptide Symposium, 1996, in press.
11. Zawadzke, L.E. and Berg, J.M., J. Am. Chem. Soc., 114 (1992) 4002.
12. Zawadzke, L.E. and Berg, J.M., Protein Struct. Funct. Genet., 16 (1993) 301.
13. Nielsen, K.J., Alewood, D., Andrews, J., Kent, S.B.H. and Craik, D.J., Protein Sci., 2 (1994) 291.
14. From a strict point of view, in the case of amino acids with two stereogenic centers, the appropriate replacement for the native L-amino acid is not the D-amino acid but the D-allo amino acid. Thus, D-allo-isoleucine has a 2R, 3S configuration and D-allo-threonine has a 2R, 3R configuration, i.e. they have the same configuration as native L-isoleucine and L-threonine at the side-chain atoms and opposite configuration at the backbone. For recent examples of the synthesis of protected D-allo-threonine and D-allo-isoleucine, see References 13 and 14.
15. Lloyd-Williams, P., Monerris, P., González, I., Jou, G. and Giralt, E., J. Chem. Soc., Perkin Trans. 1 (1994) 1969.
16. Lloyd-Williams, P., Sánchez, A., Carulla, N., Ochoa, T. and Giralt, E., Tetrahedron, 53 (1997) 3369.
17. Chorev, M. and Goodman, M., Trends Biotechnol., 13 (1995) 438.
18. Merrifield, R.B., Juvvadi, P., Andreu, D., Ubach, J., Boman, A. and Boman, H.G., Proc. Natl. Acad. Sci. USA, 92 (1995) 3449.
19. Juvvadi, P., Vunman, S. and Merrifield, R.B., J. Am. Chem. Soc., 38 (1996) 8989.
20. Jameson, B.A., McDonnell, J.M., Marini, J.C. and Korngold, R., Nature, 368 (1994) 744.
21. Brady, L. and Dodson, G., Nature, 368 (1994) 692.
22. Guichard, G., Benkirane, N., Zeder-Lutz, G., Van Regenmortel, M.H.V., Briand, J.P. and Muller, S., Proc. Natl. Acad. Sci. USA, 91 (1994) 9765.
23. Guichard, G., Muller, S., Van Regenmortel, M.H.V., Briand, J.P., Mascagni, P. and Giralt, E., Trends Biotechnol., 14 (1996) 44.
24. Sánchez, Y.M., Haack, T., González, M.J., Ludevid, M.D. and Giralt, E., J. Am. Chem. Soc., submitted.
25. Sánchez, Y.M., Haack, T., Gonzalez, M.J., Ludevid, D. and Giralt, E., In Kaumaya, P. and Hodges, R.S. (Eds.) Peptides: Chemistry, Structure and Biology (Proceedings of the 14th American Peptide Symposium), Mayflower Worldwide, Kingswinford, U.K., 1996, pp. 558-560.
26. Schumacher, T.N.M., Mayr, L.M., Minor Jr., D.L., Milhollen, M.A., Burgess, M.W. and Kim, P.S., Science, 271 (1996) 1854.
27. Deisenhofer, J., Biochemistry, 20 (1981) 2361.
28. However, atropisomers are, in general, enantiomers, not diastereomers. Furthermore, atropisomerism has a kinetic origin e.g. the lack of accessibility of conformations where the two phenyl rings are coplanar.
29. Rabanal, F., Ludevid, M.D., Pons, M. and Giralt, E., Biopolymers, 33 (1993) 1019.
30. Branden, C. and Tooze, J., Introduction to Protein Structure, Garland, New York, NY, 1991.
31. García-Echeverría, C., Albericio, F., Giralt, E. and Pons, M., J. Am. Chem. Soc., 115 (1993) 11663.
32. Ruiz-Gayo, M., Albericio, F., Pons, M., Royo, M., Pedroso, E. and Giralt, E., Tetrahedron Lett., 29 (1988) 3845.
33. Westphal, U., In Gross, F. (Ed.) Steroid-Protein Interactions, Vol. II, Springer, Berlin, 1986, p. 357.
34. With only one disulfide bridge, this compound can also be meso.
35. Contreras, M.A., Haack, T., Royo, M., Giralt, E. and Pons, M., Lett. Pept. Sci., 4 (1997) 29.
36. Miller, M., Schneider, J., Sathyanarayana, B.K., Toth, M.V., Marshall, G.R., Clawson, L., Kent, S.B.H. and Wlodawer, A., Science, 246 (1989) 1149.