The association constant of a well-known streptavidin-biotin binding has only been inferred from separately measured kinetic parameters. In a single experiment, we obtained Ka 1 × 1012 M-1 by using a streptavidin-binding aptamer and ligand-displacement isothermal titration calorimetry. This study explores the challenges of determining thermodynamic parameters and the derived equilibrium binding affinity of tight ligand-receptor binding.
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
Kuo, T-C., Tsai, C. W., Lee, P. C., & Chen, W. Y. (2015). Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration. Journal of Molecular Recognition, 28(3), 125-128. https://doi.org/10.1002/jmr.2366