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

生物化學暨細胞分子生物學科

研究成果: 雜誌貢獻 › 書/電影/文章評審 › 同行評審

9 引文斯高帕斯（Scopus）

摘要

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.

原文	英語
頁（從 - 到）	125-128
頁數	4
期刊	Journal of Molecular Recognition
卷	28
發行號	3
DOIs	https://doi.org/10.1002/jmr.2366
出版狀態	已發佈 - 2015

ASJC Scopus subject areas

分子生物學
結構生物學

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10.1002/jmr.2366

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keywords = "Affinity constant measurement, Ligand-displacement isothermal titration calorimetry, Streptavidin-biotin binding, Thermodynamic parameters",

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AU - Kuo, Tai-Chih

AU - Tsai, Ching Wei

AU - Lee, Peng Chen

AU - Chen, Wen Yih

PY - 2015

Y1 - 2015

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

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