@article{36309c94eca04db197acc2a2116fb48b,
title = "Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration",
abstract = "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.",
keywords = "Affinity constant measurement, Ligand-displacement isothermal titration calorimetry, Streptavidin-biotin binding, Thermodynamic parameters",
author = "Tai-Chih Kuo and Tsai, {Ching Wei} and Lee, {Peng Chen} and Chen, {Wen Yih}",
note = "Publisher Copyright: Copyright {\textcopyright} 2015 John Wiley & Sons, Ltd.",
year = "2015",
month = mar,
doi = "10.1002/jmr.2366",
language = "English",
volume = "28",
pages = "125--128",
journal = "Journal of Molecular Recognition",
issn = "0952-3499",
publisher = "John Wiley and Sons Ltd",
number = "3",
}