دورية أكاديمية
Binding interactions between prazosin and alpha(1A)-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography
| العنوان: | Binding interactions between prazosin and alpha(1A)-adrenoceptor: investigation on the thermodynamic behaviors and the binding mechanism by high performance affinity chromatography |
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| المؤلفون: | Wang, Jing, Li, Qian, Yang, Lingjian, Zhang, Yajun, Yu, Jie, Zhao, Xinfeng, Zheng, Jianbin, Zhang, Youyi, Zheng, Xiaohui |
| المساهمون: | Zhang, YJ (reprint author), NW Univ Xian, Coll Life Sci, Minist Educ, Key Lab Resource Biol & Biotechnol Western China, Xian 710069, Peoples R China., NW Univ Xian, Coll Life Sci, Minist Educ, Key Lab Resource Biol & Biotechnol Western China, Xian 710069, Peoples R China., NW Univ Xian, Inst Analyt Sci, Xian 710069, Peoples R China., Peking Univ, Hosp 3, Inst Vasc Med, Beijing 100083, Peoples R China., Minist Educ, Key Lab Mol Cardiovasc Sci, Beijing 100083, Peoples R China. |
| المصدر: | SCI |
| بيانات النشر: | ANALYTICAL METHODS |
| سنة النشر: | 2015 |
| المجموعة: | Peking University Institutional Repository (PKU IR) / 北京大学机构知识库 |
| مصطلحات موضوعية: | HUMAN SERUM-ALBUMIN, PROTEIN-COUPLED RECEPTORS, FRONTAL ANALYSIS, IMMOBILIZED BETA(2)-ADRENOCEPTOR, LIQUID-CHROMATOGRAPHY, STATIONARY-PHASE, CONSTANTS, RESONANCE, DRUGS |
| الوصف: | 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. ; National Nature Science Foundation of China [21475103]; program for Innovative Research Team of Shaanxi Province [2013KCT-24]; Ministry of Science and Technology of the People's Republic of China [2013YQ170525, 2013YQ17052509] ; SCI(E) ; ARTICLE ; zhaoxf@nwu.edu.cn ; 8 ; 3340-3346 ; 7 |
| نوع الوثيقة: | journal/newspaper |
| اللغة: | English |
| تدمد: | 1759-9660 1759-9679 |
| العلاقة: | ANALYTICAL METHODS.2015,7,(8),3340-3346.; 1315450; http://hdl.handle.net/20.500.11897/421253Test; WOS:000352897500005 |
| DOI: | 10.1039/c4ay03046j |
| الإتاحة: | https://doi.org/20.500.11897/421253Test https://doi.org/10.1039/c4ay03046jTest https://hdl.handle.net/20.500.11897/421253Test |
| رقم الانضمام: | edsbas.C9F7057F |
| قاعدة البيانات: | BASE |
| تدمد: | 17599660 17599679 |
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| DOI: | 10.1039/c4ay03046j |