tetano
Editor, Senior Moderator
Science. 2013 Jul 26;341(6144):379-83. doi: 10.1126/science.1236231.
A general strategy for the chemoenzymatic synthesis of asymmetrically branched N-glycans.
Wang Z, Chinoy ZS, Ambre SG, Peng W, McBride R, de Vries RP, Glushka J, Paulson JC, Boons GJ.
Source
Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Abstract
A systematic, efficient means of producing diverse libraries of asymmetrically branched N-glycans is needed to investigate the specificities and biology of glycan-binding proteins. To that end, we describe a core pentasaccharide that at potential branching positions is modified by orthogonal protecting groups to allow selective attachment of specific saccharide moieties by chemical glycosylation. The appendages were selected so that the antenna of the resulting deprotected compounds could be selectively extended by glycosyltransferases to give libraries of asymmetrical multi-antennary glycans. The power of the methodology was demonstrated by the preparation of a series of complex oligosaccharides that were printed as microarrays and screened for binding to lectins and influenza-virus hemagglutinins, which showed that recognition is modulated by presentation of minimal epitopes in the context of complex N-glycans.
http://www.ncbi.nlm.nih.gov/pubmed/23888036
A general strategy for the chemoenzymatic synthesis of asymmetrically branched N-glycans.
Wang Z, Chinoy ZS, Ambre SG, Peng W, McBride R, de Vries RP, Glushka J, Paulson JC, Boons GJ.
Source
Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
Abstract
A systematic, efficient means of producing diverse libraries of asymmetrically branched N-glycans is needed to investigate the specificities and biology of glycan-binding proteins. To that end, we describe a core pentasaccharide that at potential branching positions is modified by orthogonal protecting groups to allow selective attachment of specific saccharide moieties by chemical glycosylation. The appendages were selected so that the antenna of the resulting deprotected compounds could be selectively extended by glycosyltransferases to give libraries of asymmetrical multi-antennary glycans. The power of the methodology was demonstrated by the preparation of a series of complex oligosaccharides that were printed as microarrays and screened for binding to lectins and influenza-virus hemagglutinins, which showed that recognition is modulated by presentation of minimal epitopes in the context of complex N-glycans.
http://www.ncbi.nlm.nih.gov/pubmed/23888036