From disulfide- to thioether-linked glycoproteins.

Journal article

(Chemical Presented) Strengthening the bond: The introduction of a thiol tag in combination with chemoselective ligation to form a disulfide-linked bioconjugate is a selective and useful method for site-selective protein glycosylation. The phosphine-mediated desulfurization of such glycoconjugates to their reductant-resistant thioether-linked counterparts completes a convergent, site-selective synthesis of thioether-linked glycoproteins (see scheme). © 2008 Wiley-VCH Verlag GmbH and Co. KGaA.

Authors: Bernardes, G; Grayson, E; Thompson, S; Chalker, J; Errey, J

• Publication status: Published
• Journal: Angewandte Chemie (International ed. in English)
• Volume: 47
• Issue: 12
• Pages: 2244-2247
• Publication date: 2008-01-01
• DOI: 10.1002/anie.200704381
• EISSN: 1521-3773
• ISSN: 1433-7851
• Language: English
• Keywords: Spectrometry, Mass, Electrospray Ionization; Models, Molecular; Cross-Linking Reagents; Molecular Structure; Sulfides; Sulfhydryl Compounds; Disulfides; Glycoproteins; Amino Acids