CFG Subgroup: Chemical synthesis and glycan microarray group: topic
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Glycan Arrays: the Question of Polyvalent Presentation
M.G. Finn
Tuesday, 15 July 2008 18:21 UTC
As we all know, polyvalent binding of glycans to protein receptors is crucial to their biological functions. Many lectins, as well as anti-glycan antibodies, are each able to bind more than one glycan unit at a time.
It is therefore important to take polyvalency into account when designing or interpreting results from glycan arrays. Does the density of glycan deposition on an array surface make a substantial difference in absolute or relative affinities? If you have cautionary tales, literature citations, advice, or thoughts on this matter, here’s a place to discuss them with others in the field.
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Replies
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Is polyvalency related in any way to the fact that glycosaminoglycans are polyelectrolytes?
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In our experience, density on the array can have a major effect on binding affinity. The effect depends on the particular lectin or protein. Variations in density have also been very useful for detecting and distinguishing subpopulations of serum antibodies. For more details, se Oyelaran, O.; Li, Q.; Farnsworth, D.; Gildersleeve, J.C.* “Microarrays with Varying Carbohydrate Density Reveal Distinct Subpopulations of Serum Antibodies” J. Proteome Res. 2009, 8, 3529-38;
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