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Synthetic carbohydrate dendrimers, part 11. Chemically defined sialoside scaffolds for investigation of multivalent interactions with sialic acid binding proteins

Academic Article
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Overview

authors

  • Kalovidouris, S. A.
  • Blixt, O.
  • Nelson, A.
  • Vidal, S.
  • Turnbull, W. B.
  • Paulson, James
  • Stoddart, J. F.

publication date

  • 2003

journal

  • Journal of Organic Chemistry  Journal

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.

subject areas

  • Carbohydrate Sequence
  • Cell Adhesion Molecules
  • Enzyme-Linked Immunosorbent Assay
  • Enzymes
  • Galactose
  • Glucose
  • Immunoglobulin Fc Fragments
  • Lactose
  • Lectins
  • Ligands
  • Membrane Glycoproteins
  • Molecular Sequence Data
  • Receptors, Immunologic
  • Sialic Acid Binding Ig-like Lectin 1
  • Sialic Acid Binding Immunoglobulin-like Lectins
  • Sialic Acids
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Identity

International Standard Serial Number (ISSN)

  • 0022-3263

Digital Object Identifier (DOI)

  • 10.1021/jo030203g

PubMed ID

  • 14575475
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Additional Document Info

start page

  • 8485

end page

  • 8493

volume

  • 68

issue

  • 22

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