Isothermal titration calorimetry for drug design: Precision of the enthalpy and binding constant measurements and comparison of the instruments

Vaida Linkuvienė, Georg Krainer, Wen Yih Chen, Daumantas Matulis

研究成果: 雜誌貢獻期刊論文同行評審

28 引文 斯高帕斯(Scopus)

摘要

Isothermal titration calorimetry (ITC) is one of the most robust label- and immobilization-free techniques used to measure protein – small molecule interactions in drug design for the simultaneous determination of the binding affinity (ΔG) and the enthalpy (ΔH), both of which are important parameters for structure-thermodynamics correlations. It is important to evaluate the precision of the method and of various ITC instrument models by performing a single well-characterized reaction. The binding between carbonic anhydrase II and acetazolamide was measured by four ITC instruments – PEAQ-ITC, iTC200, VP-ITC, and MCS-ITC and the standard deviation of ΔG and ΔH was determined. Furthermore, the limit of an approach to reduce the protein concentration was studied for a high-affinity reaction (Kd = 0.3 nM), too tight to be measured by direct (non-displacement) ITC. Chemical validation of the enthalpy measurements is discussed.

原文???core.languages.en_GB???
頁(從 - 到)61-64
頁數4
期刊Analytical Biochemistry
515
DOIs
出版狀態已出版 - 15 12月 2016

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