Glycomimetics: A programmed approach toward neoglycopeptide libraries

Journal of Combinatorial Chemistry

Volumn 2, Issue 2, 2000, Pages 120-126

  Arya, Prabhat ^a   Kutterer, Kristina M K ^a,b   Barkley, Angela ^a  

^a NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^b PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; PEPTIDE LIBRARY;

ARTICLE; CARBOHYDRATE ANALYSIS; CHEMISTRY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC CHEMISTRY; SYNTHESIS;

CARBOHYDRATE SEQUENCE; CHEMISTRY, ORGANIC; GLYCOPEPTIDES; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY;

EID: 0034149935     PISSN: 15204766     EISSN: None     Source Type: Journal    
DOI: 10.1021/cc990023d     Document Type: Article

References (37)

1. (a) Bertozzi, C. R. Chem. Biol. 1995, 2, 703-708.
2. (b) Bill, R. M.; Flitsch, S. L. Chem. Biol. 1996, 3, 145-149.
3. (c) Kiessling, L. L.; Pohl, N. L. Chem. Biol. 1996, 3, 71-77.
4. (d) Lee, Y. C.; Lee, R. T. Acc. Chem. Res. 1995, 28, 321-327.
5. (e) Sharon, N.; Lis, H. Sci. Am. 1993, 82-89.
6. (f) Sears, P.; Wong, C.-H. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 12086-12093.
7. (g) Sears, P.; Wong, C.-H. Chem. Commun. 1998, 1161-1170.
8. (h) Mammen, M.; Choi, S.-K.; Whitesides, G. M. Angew. Chem., Int. Ed. Engl. 1998, 37, 2754-2794.
9. (a) Imperials, B. Acc. Chem. Res. 1997, 30, 452-459.
10. (b) O'Connor, S. E.; Imperiali, B. Chem. Biol. 1996, 3, 803-812.
11. (c) Mehta, A.; Zitzmann, N.; Rudd, P. M.; Block, T. M.; Dwek, R. A. FEBS Lett. 1998, 430, 17-22.
12. (d) Imperial;, B.; O'Connor, S. E. Pure Appl. Chem. 1998, 70, 33-40.
13. (e) Helenius, A.; Trombetta, E. S.; Hebert, D. N.; Simons, J. F. Trends Cell Biol. 1997, 7, 193-200.
14. (a) Seeberger, P. H.; Danishefsky, S. J. Acc. Chem. Res. 1998, 31, 685-695.
15. (b) Roberge, J. Y.; Beebe, X.; Danishefsky, S. J. J. Am. Chem. Soc. 1998, 120, 3915-3927.
16. Roberge, J. Y.; Beebe, X.; Danishefsky, S. J. Science 1995, 269, 202-204.
17. (d) Danishefsky, S. J.; Bilodeau, M. T. Angew. Chem., Int. Ed. Engl. 1996, 35, 1380-1419.
18. (e) Danishefsky, S. J.; Roberge, J. Y. Pure Appl. Chem. 1995, 67, 1647-1662.
19. Simanek, E. E.; McGarvey, G. J.; Jablonowski, J. A.; Wong, C.-H. Chem. Rev. 1998, 98, 833-862.
20. (a) Wang, Z.-G.; Hindsgaul, O. Glycoimmunology 2 1998, 219-236.
21. (b) Sofia, M. J. Mol. Diversity 1998, 3, 75-94.
22. (a) Meldal, M.; St. Hilaire, P. M. Curr. Opin. Chem. Biol. 1997, 1, 552-563.
23. (b) Kihlberg, J.; Elofsson, M. Curr. Med. Chem. 1997, 4, 85-116.
24. (c) Marcaurelle, L. A.; Bertozzi, C. R. Chem Eur. J. 1999, 5, 1384-1390.
25. Schleyer, A.; Meldal, M.; Manat, R.; Paulsen, H.; Bock, K. Angew. Chem., Int. Ed. Engl. 1997, 36, 1976-1978.
26. St. Hilaire, P. M.; Lowary, T. L.; Meldal, M.; Bock, K. J. Am. Chem. Soc. 1998, 120, 13312-13320
27. (a) Kutterer, K. M. K.; Barnes, M. L.; Arya, P. J. Comb. Chem. 1999, 1, 28-31.
28. (b) For solution phase synthesis of N-di-α-glycosylglycine, see: Arya, P.; Dion, S.; Shimizu, G. K. H. Bioorg. Med. Chem. Lett. 1997, 7, 1537-1542.
29. Arya, P.; Kutterer, K. M. K.; Qin, H.; Roby, J.; Barnes, M. L.; Lin, S.; Lingwood, C. A.; Peter, M. G. Bioorg. Med. Chem. 1999, 7 (12), 2823-2833.
30. (a) Jones, D. H.; Lingwood, C. A.; Barber, K. R.; Grant, C. W. M. Biochemistry 1997, 36, 8539.
31. (b) Nyholm, P.-G.; Magnusson, G.; Zheng, Z.; Norel, R.; Boyd, B. B.; Lingwood, C. A. Chem. Biol. 1996, 3, 263-275.
32. (c) Boyd, B.; Magnusson, G.; Zhiuyan, Z.; Lingwood, C. A. Eur. J. Biochem. 1994, 223, 873-878 and references therein.
33. (d) St. Hilaire, P. M.; Boyd, M. K.; Toone, E. J. Biochemistry 1994, 33, 14452-14463.
34. (e) Ling, H.; Boodhoo, A.; Hazes, B.; Cummings, M. D.; Armstrong, G. D.; Brunton, J. L.; Reed, R. J. Biochemistry 1998, 37, 1777-1788.
35. (f) Carbohydrate-based natural ligands are known to bind to lectin-based receptor molecules in millimolar/submillimolar region. For the study of the binding measurements between Gb3 and Shiga/Shiga-like toxins, see ref 12d.
36. Unlike with simple aldehydes, reductive amination reaction with carbon-linked glycoside aldehydes is not trivial. The reaction is dependent upon the nature of the amino acid/peptide and of the glycoside moiety. Several attempts have been made to optimize reaction conditions for all the steps before the methodology was transferred to a programmed synthesizer.
37. In our study, no significant difference in reaction yields was noticed between Rink amide MBHA and TentaGel resin. Neoglycopeptides 24 and 25 were synthesized using TentaGel resin only.