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
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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Cites
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Strength in numbers: non-natural polyvalent carbohydrate derivatives
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Cited by
A unified view of propagating and localized surface plasmon resonance biosensors
Haes, A. J., & Van Duyne, R. P. (2004) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-004-2708-9 · Cited by 666
Glycopolymer probes of signal transduction
Kiessling, L. L., & Grim, J. C. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60097a · Cited by 335
Self-citationHigh-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
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Recognition of microbial glycans by human intelectin-1
Wesener, D. A., Wangkanont, K., McBride, R., Song, X., Kraft, M. B., Hodges, H. L., Zarling, L. C., Splain, R. A., Smith, D. F., Cummings, R. D., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3053 · Cited by 163
Self-citationStrausak, D., Howie, M. K., Firth, S. D., Schlicksupp, A., Pipkorn, R., Multhaup, G., & Mercer, J. F. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212437200 · Cited by 71
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
- OpenAlex
- W2038996493
- Cited by
- 277
- References
- 30
- FWCI
- 3.83
- Type
- journal article
- Language
- en
- Open access
- closed
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- Mann, D. A., Kanai, M., Maly, D. J., & Kiessling, L. L. (1998). Probing Low Affinity and Multivalent Interactions with Surface Plasmon Resonance: Ligands for Concanavalin A. Journal of the American Chemical Society. https://doi.org/10.1021/ja9818506
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