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Institut de Chimie Organique et Analytique (ICOA) – Université d'Orléans – UMR CNRS 7311, rue de Chartres, BP 6759, 45067 Orléans cedex 2, France
E-mail: richard.daniellou@univ-orleans.fr
; Fax: +33-2-38-41-72-81
; Tel: +33-2-38-49-49-78
Nat. Prod. Rep., 2012,29, 729-738
DOI:
10.1039/C2NP20030A
Received
06 Mar 2012,
First published online
18 Apr 2012
Glycosylation represents the most complex co- and post-translational modification of proteins. In addition to N- and O-glycans, almost all combinations, including the nature of the carbohydrate moiety and the amino-acid involved, but also the type of the chemical linkage, can be isolated from natural glycoconjugates. This diversity correlates with the importance and the variety of the biological processes (and consequently the diseases) glycosides are involved in. This review focuses on rare and unusual glycosylation of peptides and proteins.
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