Sequence-specific peptide-carbohydrate interactions in an asparagine-linked glycopeptide

Journal of Organic Chemistry

Volumn 61, Issue 13, 1996, Pages 4198-4199

  Lee, Kwun Chi ^a   Falcone, Margaret L ^a   Davis, Jeffery T ^a  

^a Bldg 142   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE;

ARTICLE; GLYCOSYLATION; MODEL; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0030057256     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo960590c     Document Type: Article

References (26)

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4. For NMR of N-glycopeptides: (a) Ishii, H.; Inoue, Y.; Chujo, R. Int. J. Pept. Protein Res. 1984, 24, 421. (b) Ishii, H.; Inoue, Y.; Chujo, R. Polym. J. (Tokyo) 1985, 17, 693. (c) Wormald, M. R.; Wooten, E. W.; Bazzo, R.; Edge, C.; Feinstein, A.; Rademacher, T. W.; Dwek, R. A. Eur. J. Biochem. 1991, 198, 131. (d) Davis, J. T.; Hirani, S.; Bartlett, C.; Reid, B. R. J. Biol. Chem. 1994, 269, 3331.
5. For NMR of N-glycopeptides: (a) Ishii, H.; Inoue, Y.; Chujo, R. Int. J. Pept. Protein Res. 1984, 24, 421. (b) Ishii, H.; Inoue, Y.; Chujo, R. Polym. J. (Tokyo) 1985, 17, 693. (c) Wormald, M. R.; Wooten, E. W.; Bazzo, R.; Edge, C.; Feinstein, A.; Rademacher, T. W.; Dwek, R. A. Eur. J. Biochem. 1991, 198, 131. (d) Davis, J. T.; Hirani, S.; Bartlett, C.; Reid, B. R. J. Biol. Chem. 1994, 269, 3331.
6. For NMR of N-glycopeptides: (a) Ishii, H.; Inoue, Y.; Chujo, R. Int. J. Pept. Protein Res. 1984, 24, 421. (b) Ishii, H.; Inoue, Y.; Chujo, R. Polym. J. (Tokyo) 1985, 17, 693. (c) Wormald, M. R.; Wooten, E. W.; Bazzo, R.; Edge, C.; Feinstein, A.; Rademacher, T. W.; Dwek, R. A. Eur. J. Biochem. 1991, 198, 131. (d) Davis, J. T.; Hirani, S.; Bartlett, C.; Reid, B. R. J. Biol. Chem. 1994, 269, 3331.
7. For NMR of N-glycopeptides: (a) Ishii, H.; Inoue, Y.; Chujo, R. Int. J. Pept. Protein Res. 1984, 24, 421. (b) Ishii, H.; Inoue, Y.; Chujo, R. Polym. J. (Tokyo) 1985, 17, 693. (c) Wormald, M. R.; Wooten, E. W.; Bazzo, R.; Edge, C.; Feinstein, A.; Rademacher, T. W.; Dwek, R. A. Eur. J. Biochem. 1991, 198, 131. (d) Davis, J. T.; Hirani, S.; Bartlett, C.; Reid, B. R. J. Biol. Chem. 1994, 269, 3331.
8. N-glycosylation can alter Pro cis/trans and Cys thiol/disulfide equilibria: Rickert, K. W.; Imperiali, B. Chem. Biol. 1995, 2, 751.
9. O-Glycosylation influences peptide conformation: (a) Andreotti, A. H.; Kahne, D. J. Am. Chem. Soc. 1993, 115, 3352. (b) Liang, R.; Andreotti, A. H.; Kahne, D. J. Am. Chem. Soc. 1995, 117, 10395.
10. O-Glycosylation influences peptide conformation: (a) Andreotti, A. H.; Kahne, D. J. Am. Chem. Soc. 1993, 115, 3352. (b) Liang, R.; Andreotti, A. H.; Kahne, D. J. Am. Chem. Soc. 1995, 117, 10395.
11. Imperiali, B.; Rickert, K. W. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 97.
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16. (c) Bothner-By, A. A.; Stephens, R. L.; Lee, J.; Warren, C. D.; Jeanloz, R. W. J. Am. Chem. Soc. 1984, 106, 811.
17. 1 conformation, diaxial interproton distances are 3.0-3.1 Å. With a 200 ms spin-locking time NOEs were not observed between the GlcNAc H1 (σ 4.60 ppm) and GlcNAc H2 (σ 3.57 ppm). Thus, a 3.1 Å upper limit was put on the distance between protons that did show NOEs.
18. Baker, E. N.; Hubbard, R. E. Prog. Bioophys. Molec. Biol. 1984, 44, 97.
19. Abbadi, A.; Mcharfi, M.; Aubry, A.; Premilat, S. Boussard, G.; Marruad, M. J. Am. Chem. Soc. 1991, 113, 2729.
20. (a) Imperiali, B.; Shannon, K. L. Biochemistry 1991, 30, 4374.
21. (b) Imperiali, B.; Shannon, K. L., Rickert, K. W. J. Am. Chem. Soc. 1992, 114, 7942.
22. (c) Imperiali, B.; Spencer, J. R.; Struthers, M. D. J. Am. Chem. Soc. 1994, 116, 8424.
23. - = 7%) were calculated as described by: Kover, K.; Jiao, D.; Fang, S.; Hruby, V. J. J. Org. Chem. 1994, 59, 991.
24. Interpretation of NH temperature coefficients can be problematic in some apolar solvents (Gellman, S. H.; Dado, G. P.; Liang, G.; Adams, B. R. J. Am. Chem. Soc. 1991 113, 1164). However, the use of NH temperature coefficients to identify hydrogen bonds in flexible peptides in DMSO is more reliable; see: Kemp, D. S.; Curran, T. P.; Boyd, J. G.; Allen, T. J. J. Org. Chem. 1991, 56, 6683.
25. Interpretation of NH temperature coefficients can be problematic in some apolar solvents (Gellman, S. H.; Dado, G. P.; Liang, G.; Adams, B. R. J. Am. Chem. Soc. 1991 113, 1164). However, the use of NH temperature coefficients to identify hydrogen bonds in flexible peptides in DMSO is more reliable; see: Kemp, D. S.; Curran, T. P.; Boyd, J. G.; Allen, T. J. J. Org. Chem. 1991, 56, 6683.
26. Boc-Asn-Xaa-Ser-NHMe peptides show an Asx-turn overlapped by a β-turn between the C-terminal NH and the Asn C=O; see ref 12a.