Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration

Tai-Chih Kuo, Ching Wei Tsai, Peng Chen Lee, Wen Yih Chen

Research output: Contribution to journalBook/Film/Article review

5 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)125-128
Number of pages4
JournalJournal of Molecular Recognition
Issue number3
Publication statusPublished - 2015



  • Affinity constant measurement
  • Ligand-displacement isothermal titration calorimetry
  • Streptavidin-biotin binding
  • Thermodynamic parameters

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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