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Synthesis 2006(18): 3146-3152  
DOI: 10.1055/s-2006-942509
SPECIALTOPIC
© Georg Thieme Verlag Stuttgart · New York

Chemoenzymatic Synthesis of Triazole-Linked Glycopeptides

Stan Groothuysa, Brian H. M. Kuijpersa, Peter J. L. M. Quaedfliegb, Harlof C. P. F. Roelenb, Roel W. Wiertzb, Richard H. Blaauwc, Floris L. van Delfta, Floris P. J. T. Rutjes*a
a Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands
Fax: +31(24)3653393; e-Mail: F.Rutjes@science.ru.nl;
b DSM Research, Life Sciences-Advanced Synthesis, Catalysis and Development, P.O. Box 18, 6160 MD Geleen, The Netherlands
c Chiralix B.V., Toernooiveld 100, 6525 EC Nijmegen, The Netherlands
Further Information

Publication History

Received 29 March 2006
Publication Date:
25 July 2006 (online)

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Abstract

Triazole-linked glycopeptides are prepared by C-terminal elongation of glycoamino acids with proteinogenic amino acids following a chemical or enzymatic coupling protocol. Two orthogonal routes for a chemoenzymatic strategy were explored, involving a click-reaction before amide bond formation or in reverse order. It was found that enzymatic peptide coupling under the influence of alcalase proceeds cleanly and in high yields, while the resulting dipeptides can be efficiently clicked to acetylene- or azide-containing sugars.

Key words

glycopeptides - azides - alkynes - click chemistry - enzymatic coupling