Synthesis of Bifunctional Azobenzene Glycoconjugates for Cysteine-Based Photosensitive Cross-Linking with Bioactive Peptides
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Updated: Apr 5, 2026

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
Published on: July 20, 2016
Anne Müller1, Hauke Kobarg1, Vijayanand Chandrasekaran1
1Otto Diels Institute of Organic Chemistry, Christiana Albertina University of Kiel, Otto-Hahn-Platz 3/4, 24118 Kiel (Germany), Fax: (+49) 431-8807410.
Abstract:
Azobenzene linker molecules can be utilized to control peptide/protein function when they are ligated to appropriately spaced amino acid side chains of the peptide. This is because the photochemical E/Z isomerization of the azobenzene N=N double bond allows to switch peptide conformation between folded and unfolded. In this context, we have introduced carbohydrate-functionalized azobenzene derivatives in order to advance the biocompatible properties of azobenzene peptide linkers. Chloroacetamide-functionalized and O-allylated carbohydrate derivatives were synthesized and conjugated with azobenzene to achieve new bifunctional cross-linkers, in order to allow ligation to cysteine side chains by nucleophilic substitution or thiol-ene reaction, respectively. The photochromic properties of the new linker glycoconjugates were determined and first ligation reactions performed.
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