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Cited by 277

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Probing Low Affinity and Multivalent Interactions with Surface Plasmon Resonance: Ligands for Concanavalin A

Mann, David A., Kanai, Motomu, Maly, Dustin J., Kiessling, Laura L.·1998·Journal of the American Chemical Society
DOI 10.1021/ja9818506
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Abstract

The affinities of the carbohydrate-binding protein concanavalin A (Con A) for mono- and multivalent ligands were measured by surface plasmon resonance (SPR) detection. Assessing protein−carbohydrate affinities is typically difficult due to weak affinities observed and the complications that arise from the importance of multivalency in these interactions. We describe a convenient method to rapidly evaluate the inhibitory constants for a panel of different ligands, both monovalent and multivalent, for low-affinity receptors, such as the carbohydrate-binding protein Con A. A nonnatural, mannose-substituted glycolipid was synthesized, and self-assembled monolayers of varying carbohydrate density were generated. The synthetic surfaces bind Con A. Competition experiments that employed monovalent ligands in solution yielded K i values similar to equilibrium binding constants obtained in titration microcalorimetry experiments. In addition, this assay could be used to examine various polymeric ligands of defined lengths, generated by ring-opening metathesis polymerization (ROMP). This study demonstrates the utility of this method for rapidly screening ligands that engage in low affinity interactions with their target receptors. Our results emphasize that those molecules that can simultaneously occupy two or more saccharide binding sites within a lectin oligomer are effective inhibitors of protein−carbohydrate interactions.

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Metadata

Authors
Mann, D. A., Kanai, M., Maly, D. J., & Kiessling, L. L.
Venue
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Published
1998-10-01
Volume
120
Issue
41
Pages
10575-10582
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
DOI
10.1021/ja9818506
OpenAlex
W2038996493
Cited by
277
References
30
FWCI
3.83
Type
journal article
Language
en
Open access
closed

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