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Science 14 July 1995:
Vol. 269. no. 5221, pp. 202 - 204
DOI: 10.1126/science.7618080
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Articles

Science, Vol 269, Issue 5221, 202-204
Copyright © 1995 by American Association for the Advancement of Science

articles

A strategy for a convergent synthesis of N-linked glycopeptides on a solid support

JY Roberge, X Beebe, and SJ Danishefsky

Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, New York, NY 10021, USA.

Oligosaccharides and glycopeptides are of considerable importance in molecular biology and pharmacology. However, their synthesis is complicated by the large number of different linking sites between each saccharide unit, the need for stereochemical control, the chemical sensitivity of the glycopeptide bonds, and the need to harmonize diverse protecting groups. Here, an efficient solid-phase synthesis of three N-linked glycopeptides based on glycal assembly is presented. The peptide domain can be extended while the ensemble remains bound to the polymer. The glycopeptides synthesized here are among the largest N-linked glycopeptides ever accessed by either solution- or solid-phase synthesis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding.
D. H. Live, R. A. Kumar, X. Beebe, and S. J. Danishefsky (1996)
PNAS 93, 12759-12761
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