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学科主题临床医学
Binding interactions between prazosin and alpha(1A)-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography
Wang, Jing1; Li, Qian1; Yang, Lingjian1; Zhang, Yajun1; Yu, Jie1; Zhao, Xinfeng1; Zheng, Jianbin2; Zhang, Youyi3,4; Zheng, Xiaohui1
刊名ANALYTICAL METHODS
2015
DOI10.1039/c4ay03046j
7期:8页:3340-3346
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Chemistry, Analytical ; Food Science & Technology ; Spectroscopy
研究领域[WOS]Chemistry ; Food Science & Technology ; Spectroscopy
关键词[WOS]HUMAN SERUM-ALBUMIN ; PROTEIN-COUPLED RECEPTORS ; FRONTAL ANALYSIS ; IMMOBILIZED BETA(2)-ADRENOCEPTOR ; LIQUID-CHROMATOGRAPHY ; STATIONARY-PHASE ; CONSTANTS ; RESONANCE ; DRUGS
英文摘要

Although the association constant and the number of binding sites of prazosin to alpha(1A)-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 alpha(1A)-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 alpha(1A)-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. Ser(203) and Ser(192) 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.

语种英语
WOS记录号WOS:000352897500005
引用统计
被引频次:3[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/66311
专题北京大学第三临床医学院_心血管内科
作者单位1.NW Univ Xian, Coll Life Sci, Minist Educ, Key Lab Resource Biol & Biotechnol Western China, Xian 710069, Peoples R China
2.NW Univ Xian, Inst Analyt Sci, Xian 710069, Peoples R China
3.Peking Univ, Hosp 3, Inst Vasc Med, Beijing 100083, Peoples R China
4.Minist Educ, Key Lab Mol Cardiovasc Sci, Beijing 100083, Peoples R China
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GB/T 7714
Wang, Jing,Li, Qian,Yang, Lingjian,et al. Binding interactions between prazosin and alpha(1A)-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography[J]. ANALYTICAL METHODS,2015,7(8):3340-3346.
APA Wang, Jing.,Li, Qian.,Yang, Lingjian.,Zhang, Yajun.,Yu, Jie.,...&Zheng, Xiaohui.(2015).Binding interactions between prazosin and alpha(1A)-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography.ANALYTICAL METHODS,7(8),3340-3346.
MLA Wang, Jing,et al."Binding interactions between prazosin and alpha(1A)-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography".ANALYTICAL METHODS 7.8(2015):3340-3346.
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