| Abstract
| - Four glycodendrons and a glycocluster were synthesized from carbohydrate building blocks to formpaucivalent (di- to tetravalent) structures of controlled scaffold architectures. Enzymatic sialylationof the functionalized cluster and dendrons, terminated in lactose residues, generated a library ofpaucivalent synthetic sialosides displaying sialic acids with different dispositions. These newlyconstructed bioactive sialic acid-based structures were differentially recognized by sialoadhesin, amammalian macrophage sialic acid binding protein. The binding of the sialosides to sialoadhesinwas evaluated by an enzyme-linked immunosorbant assay to investigate the complementarity ofscaffold structure and binding to sialoadhesin. Modulating the interaction between sialoadhesinand its sialic acid ligands has important implications in immunobiology.
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