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Sialoside analogue arrays for rapid identification of high affinity siglec ligands.

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.

SUBMITTER: Blixt O

PROVIDER: S-EPMC2614358 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

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Sialoside analogue arrays for rapid identification of high affinity siglec ligands.

Blixt Ola O Han Shoufa S Liao Liang L Zeng Ying Y Hoffmann Julia J Futakawa Satoshi S Paulson James C JC

Journal of the American Chemical Society 20080502 21

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 si ...[more]

PMID: 18452295

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