Design and evaluation of potent inhibitors of asparagine-linked protein glycosylation

Journal of the American Chemical Society

Volumn 118, Issue 32, 1996, Pages 7636-7637

  Hendrickson, Tamara L ^a   Spencer, Jeffrey R ^a   Kato, Mihoko ^a   Imperiali, Barbara ^a  

^a California Institute of Technology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; OLIGOPEPTIDE;

ANIMAL TISSUE; ARTICLE; DRUG SYNTHESIS; ENZYME INHIBITION; GLYCOSYLATION; LIVER; NONHUMAN; REACTION ANALYSIS; SWINE; YEAST;

EID: 0029777524     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961448w     Document Type: Article

References (29)

1. Silverman, R. B. in The Organic Chemistry of Drug Design and Drug Action; Academic Press, Inc.: San Diego, 1992; pp 147-218.
2. Dwek, R. A. Chem. Rev. 1996, 96, 683-720.
3. Wyss, D. F.; Choi, J. S.; Li, J.; Knoppers, M. H.; Willis, K. J.; Arulanandam, A. R. N.; Smolyar, A.; Reinherz, E. L.; Wagner, G. Science 1995, 269, 1273-1278.
4. Scheiffele, P.; Peranen, J.; Simons, K. Nature 1995, 378, 96-98.
5. Varki, A. Glycobiology 1993, 3, 97-130.
6. Hubbard, S. C.; Ivatt, R. J. Ann. Rev. Biochem. 1981, 50, 555-583.
7. Jentoft, N. Trends Biol. Sci. 1990, 15, 291-294.
8. i for tunicamycin is between 7 and 500 nM against the enzyme UDPGIcNAc:dolichyl phosphate N-acetylglucosamine-1-phosphate transferase (ref 9).
9. Elbein, A. D. Trends in Biol. Sci. 1981, 6, 291-293.
10. Tamura, G. Tunicamycin, Japan Scientific Society Press: 1982.
11. Keller, R. K.; Boon, D. Y.; Cram, F. C. Biochemistry 1979, 18, 3946-3952.
12. Lam, K. S.; Salmon, S. E.; Hersh, E. M.: Hruby, V. J.; Kazmierski, W. M.; Knapp, R. J. Nature 1991, 354, 82-84.
13. Houghten, R. A.; Pinilla, C.; Blondelle, S. E.; Appel, J. R.; Dooley, C. T.; Cuervo, J. H. Nature 1991, 354, 84-86.
14. Gallop, M. A.; Barrett, R. W.; Dower, W. J.; Fodor, S. P. A.; Gordon, E. M. J. Med. Chem. 1994, 37, 1233-1251.
15. Goss, P. E.; Baker, M. A.; Carver, J. P.; Dennis, J. W. Clin. Can. Res. 1995, 1, 935-944.
16. Marshall, R. D. Biochem. Soc. Symp. 1914, 40, 17-26.
17. This conformation places the asparagine side chain in proximity to the essential hydroxy amino acid. Imperiali, B.; Spencer, J. R.; Struthers, M. D. J. Am. Chem. Soc. 1994, 116, 8424-8425.
18. Gavel, Y.; von Heijne, G. Protein Eng. 1990, 3, 433-442.
19. Imperiali, B.; Shannon, K. L.; Unno, M.; Rickert, K. W. J. Am. Chem. Soc. 1992, 114, 7944-7945.
20. Virgilio, A. A.; Ellman, J. A. J. Am. Chem. Soc. 1994, 116, 11580-11581.
21. Barker, P. L.; Bullens, S.; Bunting, S.; Burdick, D. J.; Chan, K. S.; Deisher, T.; Eigenbrot, C.; Gadek, T. R.; Gantzos, R.; Lipari, M. T.; Muir, C. D.; Napier, M. A.; Pitti, R. M.; Padua, A.; Quan, C.; Stanley, M.; Struble, M.; Tom, J. Y. K.; Burnier, J. P. J. Med. Chem. 1992, 35, 2040-2048.
22. Imperiali, B.; Shannon, K. L. Biochemistry 1991, 30, 4374-4380.
23. Rathod, P. K.; Tashjian, A. H. Jr.; Abeles, R. H. J. Biol. Chem. 1986, 261, 6461-6469.
24. Cha, S. Biochem. Pharmacol. 1975, 24, 2177-2185.
25. Compounds 3 and 4 also demonstrated some slow binding; however, these compounds were less potent than 2 and were not evaluated in detail.
26. Morrsion, J. F.; Walsh, C. T. Adv. Enzymol. 1988, 61, 201-301.
27. Imperiali, B.; Hendrickson, T. L. Bioorg. Med. Chem. 1995, 3, 1565-1578.
28. Wang, Y.; Abernathy, J. L.; Eckhardt, A. E.; Hill, R. L. J. Biol. Chem. 1992, 267, 12709-12716.
29. Segel, I. H. Enzyme Kinetics; John Wiley and Sons: New York, 1975.