Synthesis ofC-Terminal Glycopeptides from Resin-Bound Glycosyl Azides via a Modified Staudinger Reaction

Malkinson, J.P., Falconer, R.A. and Toth, I. (2000) Synthesis ofC-Terminal Glycopeptides from Resin-Bound Glycosyl Azides via a Modified Staudinger Reaction. Journal of Organic Chemistry, 65 (17). pp. 5249-5252. 10.1021/jo000381z.

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DOI: 10.1021/jo000381z

Abstract

The solid-phase synthesis of glycopeptides containing the sugar at the C-terminus is reported. The method is demonstrated on a model, the endogenous antinociceptive peptide Leu-enkephalin. 2,3,4-Tri-O-acetyl-1-azido-1-deoxy-beta-D-glucopyranuronic acid was synthesized and immobilized onto a variety of derivatized resins. Conjugation of the first amino acid was accomplished by reaction of the resin-bound glycosyl azide with an activated amino acid, in one step, via a modified Staudinger reaction. Standard solid-phase peptide synthesis then resulted in the desired amide-linked glycopeptide. Reaction conditions and reagents for the glycosylation were varied to optimize the yield and purity of the product. The optimum conditions were found to be the use of a 4-fold molar excess of activated amino acid and 3-fold excess of tri-n-butylphosphine in tetrahydrofuran. This methodology is generally applicable to most peptide sequences and is compatible with both Boc- and Fmoc- synthetic strategies on a variety of resins.

Item Type:Article
Departments, units and centres:Department of Pharmaceutical and Biological Chemistry > Department of Pharmaceutical and Biological Chemistry
ID Code:2403
Journal or Publication Title:Journal of Organic Chemistry
Deposited By:Library Staff
Deposited On:03 Nov 2011 17:35
Last Modified:03 Nov 2011 17:35

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