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. 2018 Nov 28;16(46):8899-8903.
doi: 10.1039/c8ob01664j.

The study of multivalent carbohydrate-protein interactions by bio-layer interferometry

Eugénie Laigre  1 , David Goyard, Claire Tiertant, Jérôme Dejeu, Olivier Renaudet
Affiliations

The study of multivalent carbohydrate-protein interactions by bio-layer interferometry

Eugénie Laigre et al. Org Biomol Chem. .

Abstract

The study of complex multivalent carbohydrate-protein interactions remains highly complicated and sometimes rendered impossible due to aggregation problems. In this study, we demonstrate that bio-layer interferometry is an excellent complementary method to standard techniques such as SPR and ITC. Using tetra- and hexadecavalent GalNAc glycoconjugates and Helix pomatia agglutinin (HPA) as a model lectin, we were able to measure reliable kinetic and thermodynamic parameters of multivalent interactions going from the micro to the nanomolar range.

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Figures

Fig. 1
Fig. 1. Structures of tetravalent glycoclusters and hexadecavalent glycodendrimers.–
Fig. 2
Fig. 2. Sensorgrams obtained for the tetravalent glycoconjugates 1–4.
Fig. 3
Fig. 3. Sensorgrams obtained for the hexadecavalent glycoconjugates 5–8.
Fig. 4
Fig. 4. Thermodynamic dissociation constants determined for the multivalent glycoconjugates 1–8 and HPA interactions.
Fig. 5
Fig. 5. Isoaffinity graph plotted from the HPA–glycoconjugate 1–8 interaction.
See this image and copyright information in PMC

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