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Revisiting the streptavidin–biotin binding by using an aptamer and displacement isothermal calorimetry titration
Author(s) -
Kuo TaiChih,
Tsai ChingWei,
Lee PengChen,
Chen WenYih
Publication year - 2015
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2366
Subject(s) - isothermal titration calorimetry , streptavidin , titration , aptamer , chemistry , biotin , isothermal process , calorimetry , ligand (biochemistry) , binding constant , equilibrium constant , biophysics , crystallography , binding site , thermodynamics , biochemistry , receptor , microbiology and biotechnology , biology , physics
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 K a 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. Copyright © 2015 John Wiley & Sons, Ltd.