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 × 10(12)  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.
authors.affiliation: Department of Biochemistry, Taipei Medical University, Taipei, Taiwan.
authors.forename: Tai-Chih
authors.initials: TC
authors.lastname: Kuo
authors.forename: Ching-Wei
authors.initials: CW
authors.lastname: Tsai
authors.forename: Peng-Chen
authors.initials: PC
authors.lastname: Lee
authors.forename: Wen-Yih
authors.initials: WY
authors.lastname: Chen
mesh_terms: D052157:Aptamers, Nucleotide / Q000378:metabolism*; D001710:Biotin / Q000737:chemistry* / Q000378:metabolism; D002151:Calorimetry / Q000379:methods*; D011485:Protein Binding; D019809:Streptavidin / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D052157:Aptamers, Nucleotide; D001710:Biotin; D019809:Streptavidin
keywords: Affinity constant measurement; ligand-displacement isothermal titration calorimetry; streptavidin-biotin binding; thermodynamic parameters