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

doi:10.1002/jmr.2366

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

Department of Biochemistry and Molecular Cell Biology

Research output: Contribution to journal › Book/Film/Article review › peer-review

12 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 K_a 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 language	English
Pages (from-to)	125-128
Number of pages	4
Journal	Journal of Molecular Recognition
Volume	28
Issue number	3
DOIs	https://doi.org/10.1002/jmr.2366
Publication status	Published - Mar 2015

Keywords

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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10.1002/jmr.2366

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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\}",

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year = "2015",

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T1 - Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration

AU - Kuo, Tai-Chih

AU - Tsai, Ching Wei

AU - Lee, Peng Chen

AU - Chen, Wen Yih

PY - 2015/3

Y1 - 2015/3

N2 - 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.

AB - 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.

KW - Affinity constant measurement

KW - Ligand-displacement isothermal titration calorimetry

KW - Streptavidin-biotin binding

KW - Thermodynamic parameters

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UR - https://www.scopus.com/pages/publications/84923362503#tab=citedBy

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DO - 10.1002/jmr.2366

M3 - Book/Film/Article review

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AN - SCOPUS:84923362503

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JO - Journal of Molecular Recognition

JF - Journal of Molecular Recognition

IS - 3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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