NDLI: Binding interactions between prazosin and α<sub>1A</sub>-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography

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Binding interactions between prazosin and α_1A-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography

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Binding interactions between prazosin and α_1A-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography

Content Provider	Royal Society of Chemistry (RSC)
Author	Li, Qian Zhao, Xinfeng Zhang, Youyi Zheng, Xiaohui Yang, Lingjian Zhang, Yajun Yu, Jie Wang, Jing Zheng, Jianbin
Copyright Year	2015
Abstract	Although the association constant and the number of binding sites of prazosin to α1A-adrenoceptor were determined by high performance affinity chromatography (HPAC) in our previous work, the thermodynamic behaviors and the binding mechanism of the drug to immobilized α1A-adrenoceptor remained unclear. This work intended to address the issue by HPAC and molecular docking. The investigations involved the determination of association constants by frontal analysis at different temperatures, the calculation of enthalpy, entropy and free energy changes, the examination of mobile phase composition on the binding parameters and the site-directed molecular docking. The changes of enthalpy, entropy and free energy during the interaction were −20.79 kJ mol−1, −59.28 J mol−1 K−1 and −2.4 kJ mol−1, respectively. The binding of prazosin to α1A-adrenoceptor was an endothermic process with an increase in entropy. This reaction was mainly driven by hydrogen bonds. The ionic strength of the mobile phase provided a positive response to the values of association constants, while the power of hydrogen and the concentration of isopropyl in the mobile phase showed a negative trend. Ser203 and Ser192 in the fifth transmembrane segment of the receptor were the positions for the formation of hydrogen bonds. It is possible to utilize the immobilized receptor to determine the mechanism of drug–receptor interactions.
Starting Page	3340
Ending Page	3346
Page Count	7
File Format	HTM / HTML PDF
ISSN	17599660
Volume Number	7
Issue Number	8
Journal	Analytical Methods
DOI	10.1039/c4ay03046j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Gibbs free energy Enthalpy Binding constant Docking (molecular) Entropy HPAC Endothermic process Prazosin Affinity chromatography Ionic strength Site-directed mutagenesis Propyl group Negative Trend Hydrogen bond
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Engineering Chemical Engineering

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