Abstract
Four glycodendrons and a glycocluster were synthesized from carbohydrate building blocks to form paucivalent (di- to tetravalent) structures of controlled scaffold architectures. Enzymatic sialylation of the functionalized cluster and dendrons, terminated in lactose residues, generated a library of paucivalent synthetic sialosides displaying sialic acids with different dispositions. These newly constructed bioactive sialic acid-based structures were differentially recognized by sialoadhesin, a mammalian macrophage sialic acid binding protein. The binding of the sialosides to sialoadhesin was evaluated by an enzyme-linked immunosorbant assay to investigate the complementarity of scaffold structure and binding to sialoadhesin. Modulating the interaction between sialoadhesin and its sialic acid ligands has important implications in immunobiology.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Carbohydrate Sequence
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Cell Adhesion Molecules / chemistry
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Enzyme-Linked Immunosorbent Assay
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Enzymes / chemistry
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Galactose / chemistry
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Glucose / chemistry
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Immunoglobulin Fc Fragments / chemistry
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Lactose / chemistry
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Lectins / chemistry*
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Ligands
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Membrane Glycoproteins / chemistry*
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Molecular Sequence Data
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Receptors, Immunologic / chemistry*
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Sialic Acid Binding Ig-like Lectin 1
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Sialic Acid Binding Immunoglobulin-like Lectins
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Sialic Acids / chemical synthesis*
Substances
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Cell Adhesion Molecules
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Enzymes
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Immunoglobulin Fc Fragments
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Lectins
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Ligands
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Membrane Glycoproteins
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Receptors, Immunologic
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Sialic Acid Binding Ig-like Lectin 1
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Sialic Acid Binding Immunoglobulin-like Lectins
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Sialic Acids
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Glucose
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Lactose
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Galactose