tetano
Editor, Senior Moderator
Adv Exp Med Biol. 2018;1104:259-273. doi: 10.1007/978-981-13-2158-0_13.
[h=1]Quantifying Weak Glycan-Protein Interactions Using a Biolayer Interferometry Competition Assay: Applications to ECL Lectin and X-31 Influenza Hemagglutinin.[/h] Ji Y[SUP]1[/SUP], Woods RJ[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] This chapter introduces two formats using bio-layer interferometry competition assays to determine the solution K [SUB]D[/SUB] values of weak glycan-protein interactions. This approach overcomes the challenge of determining weak interactions while minimizing the amount of reagents required. Accurate solution K [SUB]D[/SUB] values aid in understanding the complex relationships between monomeric versus multimeric interactions and affinity versus avidity. The assays have been applied to a well-studied lectin (Erythrina crista-galli lectin) and influenza hemagglutinin (X-31). The solution K [SUB]D[/SUB] values determined from this approach are in good agreement with previous reported literature values from isothermal titration calorimetry and NMR. Additionally, this approach appears robust and precise.
[h=4]KEYWORDS:[/h] BLI-based inhibition assay; Bio-layer interferometry; ECL; Glycan-protein interaction; Weak interaction; X-31
PMID: 30484253 DOI: 10.1007/978-981-13-2158-0_13
[h=1]Quantifying Weak Glycan-Protein Interactions Using a Biolayer Interferometry Competition Assay: Applications to ECL Lectin and X-31 Influenza Hemagglutinin.[/h] Ji Y[SUP]1[/SUP], Woods RJ[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] This chapter introduces two formats using bio-layer interferometry competition assays to determine the solution K [SUB]D[/SUB] values of weak glycan-protein interactions. This approach overcomes the challenge of determining weak interactions while minimizing the amount of reagents required. Accurate solution K [SUB]D[/SUB] values aid in understanding the complex relationships between monomeric versus multimeric interactions and affinity versus avidity. The assays have been applied to a well-studied lectin (Erythrina crista-galli lectin) and influenza hemagglutinin (X-31). The solution K [SUB]D[/SUB] values determined from this approach are in good agreement with previous reported literature values from isothermal titration calorimetry and NMR. Additionally, this approach appears robust and precise.
[h=4]KEYWORDS:[/h] BLI-based inhibition assay; Bio-layer interferometry; ECL; Glycan-protein interaction; Weak interaction; X-31
PMID: 30484253 DOI: 10.1007/978-981-13-2158-0_13