CARB 16 |
| This approach has its foundations in the neoglycolipid (NGL) technology that we introduced in 1985 and further refined. This was devised to address the need for a microscale technology to present oligosaccharides in a clustered form for studies of carbohydrate-protein interactions, in particular assignments of the ligands of carbohydrate-binding receptors and the epitopes recognized by antibodies. The NGL approach, originally developed using sequence-defined O-glycans for antibody binding studies, has also been shown to be a powerful means of generating other types of oligosaccharide probes: from N-glycans, fragments of glycosaminoglycans and polysaccharides, and from diverse chemically synthesized oligosaccharides. Glycolipids, both naturally occurring and synthetic are included in the repertoire of probes. A key development has been to combine carbohydrate-protein interaction studies with mass spectrometry in situ to gain information on monosaccharide composition, sequence and branching pattern, as well as sulphate and phosphate substitution of the immobilized oligosaccharide probes at low picomole levels. NGL probes generated as mixtures from whole cells and tissues and probed with carbohydrate-recognizing proteins can be deconvoluted by TLC combined with mass spectrometry. Our state-of-the-art microarray system, currently with almost 300 sequence-defined oligosaccharide probes, is continually expanding and has provision for generating ‘designer' microarrays from targeted tissues and macromolecules. This versatile platform shows considerable promise as a novel approach to surveying entire glycomes and proteomes for the molecular definition of carbohydrate-recognition systems. |
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Carbohydrate Recognition Mechanisms and Applications
2:00 PM-4:30 PM, Monday, 27 March 2006 Georgia World Congress Center -- B409, Oral
Division of Carbohydrate Chemistry |