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

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)125-128
Number of pages4
JournalJournal of Molecular Recognition
Volume28
Issue number3
DOIs
Publication statusPublished - 2015

Fingerprint

Calorimetry
Streptavidin
Biotin
Ligands
Thermodynamics

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration. / Kuo, Tai-Chih; Tsai, Ching Wei; Lee, Peng Chen; Chen, Wen Yih.

In: Journal of Molecular Recognition, Vol. 28, No. 3, 2015, p. 125-128.

Research output: Contribution to journalBook/Film/Article review

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