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Sialoside analogue arrays for rapid identification of high affinity siglec ligands

Academic Article
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Overview

authors

  • Blixt, O.
  • Han, S. F.
  • Liao, L.
  • Zeng, Y.
  • Hoffmann, J.
  • Futakawa, S.
  • Paulson, James

publication date

  • May 2008

journal

  • Journal of the American Chemical Society  Journal

abstract

  • The siglec family of sialic acid binding proteins participates in diverse cell surface biology that includes regulation of immune cell signaling and the interaction of neuronal cells with glial cells. The weak intrinsic affinity of the natural sialoside ligands has hampered the development of synthetic ligand based probes needed to elucidate their roles in siglec function. In this report, we describe a glycan microarray comprising a library of 9-acyl-substituted sialic acids incorporated into sialosides containing the Neu5Acalpha2-3Gal and Neu5Acalpha-6Gal linkages commonly recognized by the siglecs. The array is demonstrated to exhibit utility for detecting 9-acyl substituents that increase the affinity of siglecs for their ligands. Substituents that increase affinity are anticipated to be useful for the design of high affinity ligand based probes of siglec function.

subject areas

  • Carbohydrate Sequence
  • Kinetics
  • Lectins
  • Ligands
  • Molecular Sequence Data
  • Oligosaccharides
  • Plant Lectins
  • Polysaccharides
  • Sialic Acid Binding Immunoglobulin-like Lectins
  • Sialic Acids
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Identity

PubMed Central ID

  • PMC2614358

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja80l052g

PubMed ID

  • 18452295
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Additional Document Info

start page

  • 6680

end page

  • 6681

volume

  • 130

issue

  • 21

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