Chemically Defined Sialoside Scaffolds for Investigation of Multivalent Interactions with Sialic Acid Binding Proteins

Stacey A. Kalovidouris, Ola Blixt, Alshakim Nelson, Sébastien Vidal, W. Bruce Turnbull, James C. Paulson, J. Fraser Stoddart*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

46 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)8485-8493
Number of pages9
JournalJournal of Organic Chemistry
Volume68
Issue number22
DOIs
StatePublished - Oct 31 2003

ASJC Scopus subject areas

  • Organic Chemistry

Fingerprint Dive into the research topics of 'Chemically Defined Sialoside Scaffolds for Investigation of Multivalent Interactions with Sialic Acid Binding Proteins'. Together they form a unique fingerprint.

Cite this