678968-49-5Relevant academic research and scientific papers
From disulfide- to thioether-linked glycoproteins
Bernardes, Goncalo J. L.,Grayson, Elizabeth J.,Thompson, Sam,Chalker, Justin M.,Errey, James C.,El Oualid, Farid,Claridge, Timothy D. W.,Davis, Benjamin G.
experimental part, p. 2244 - 2247 (2009/02/07)
(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).
REAGENTS AND METHODS FOR THE FORMATION OF DISULFIDE BONDS AND THE GLYCOSYLATION OF PROTEINS
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Page/Page column 57, (2010/02/10)
Methods and reagents for the formation of disulfide bonds, particularly in proteins, peptides and amino acids. The methods and reagents are particularly useful for the controlled glycosylation of proteins, peptides and amino acids. The methods utilise thiosulfonate or selenenylsulfide compounds as reagents or intermediates. Some proteins and peptides comprising selenenylsulfide groups also form part of the invention.
Glyco-SeS: Selenenylsulfide-mediated protein glycoconjugation - A new strategy in post-translational modification
Gamblin, David P.,Garnier, Philippe,Van Kasteren, Sander,Oldham, Neil J.,Fairbanks, Antony J.,Davis, Benjamin G.
, p. 828 - 833 (2007/10/03)
Site-selective glycosylation by Se-S-mediated ligation has led to the efficient formation of a wide variety of conjugates 1 without the need for a large excess of the carbohydrate reagent. By this convergent method it was possible to introduce a heptasaccharide glycan selectively, and to perform a multiple site-selective chemical glycosylation of protein. A chemically Cysglycosylated glycoprotein was elaborated enzymatically.
