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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Dynamic glycosylation of liposomes by thioester exchange
Johanna Moratz1, Florian Klepel, Bart Jan Ravoo
1Organic Chemistry Institute, Westfälische Wilhelms-Universität Münster, Corrensstrasse 40, 48149 Münster, Germany. b.j.ravoo@uni-muenster.de.
Abstract:
The interplay of dynamic functionalization and specific molecular recognition on biological membranes is key to numerous physiological processes. In this work we present a simple glycocalyx model based on the covalent yet reversible glycosylation of liposomes and subsequent recognition by a lectin. Reversible thioester exchange of membrane embedded amphiphilic thioesters with thiol-tagged d-mannose in solution is performed at physiologically relevant conditions. Recognition with the lectin concanavalin A is possible directly from this reaction mixture, leading to liposome agglutination. To the best of our knowledge, the dynamic covalent glycosylation of liposomes is so far unprecedented.
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