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学科主题: 临床医学
题名:
Exploring drug-protein interactions using the relationship between injection volume and capacity factor
作者: Zhao, Xinfeng1; Li, Qian1; Chen, Jiejun2; Xiao, Chaoni1; Bian, Liujiao1; Zheng, Jianbin3; Zheng, Xiaohui1; Li, Zijian4,5; Zhang, Youyi4,5
关键词: Drug protein interactions ; Affinity chromatography ; Mathematical model ; Human serum albumin ; Beta(2)-adrenoceptor
刊名: JOURNAL OF CHROMATOGRAPHY A
发表日期: 2014-04-25
DOI: 10.1016/j.chroma.2014.03.017
卷: 1339, 页:137-144
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemical Research Methods ; Chemistry, Analytical
研究领域[WOS]: Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]: PERFORMANCE AFFINITY-CHROMATOGRAPHY ; HUMAN SERUM-ALBUMIN ; STATIONARY PHASES ; FRONTAL ANALYSIS ; FLUORESCENCE SPECTROSCOPY ; CAPILLARY-ELECTROPHORESIS ; BINDING CONSTANTS ; COUPLED RECEPTOR ; RAPID ANALYSIS ; ZONAL ELUTION
英文摘要:

Affinity chromatography is the most widespread and widely accepted methodology for exploring drug-protein and protein-protein interactions. Despite the successful application of frontal analysis and zonal elution in affinity chromatography, research into the creation of new mathematical tools for data processing is encouraged due to these two methods′ drawbacks of long analysis times and high ligand consumption. In this work, we created a novel mathematical model using the relationship between the molar amount of an injected solute and its capacity factor. We validated the method by analyzing the binding of drugs to human serum albumin (HSA) and beta(2)-adrenoceptor (beta(2)-AR). The association constants of omeprazole, propranolol and promethazine binding to HSA were determined to be (4.10 +/- 0.24) x 10(4), (2.30 +/- 0.12) x 10(4) and (1.24 +/- 0.14) x 10(4) M-1, respectively. These constants agreed with previously reported literature results of 4.60 x 10(4), 2.30 x 10(4) and 1.40 x 10(4) M-1. Salbutamol, norepinephrine, isoprenaline, bamethane and methoxyphenamine were found to bind to beta(2)-AR with association constants of (1.11 +/- 0.06) x 10(3), (0.95 +/- 0.03) x 10(3), (1.66 +/- 0.12) x 10(3), (0.47 +/- 0.04) x 10(3) and (0.43 +/- 0.02) x 10(3) M-1, respectively, which positively correlated to the negative logarithm of the dissociation constants obtained via radio-ligand binding assays. The proposed model is relatively fast and conserves ligand, and it has the potential to serve as an alternative method for rapidly revealing drug-protein and protein-protein interactions. (C) 2014 Elsevier B.V. All rights reserved.

语种: 英语
所属项目编号: 21005060 ; IRT1174 ; 2013KCT-24
项目资助者: National Natural Sciences Foundation of China ; Changjiang Scholars and Innovative Research Team in University ; Innovative Research Team of Research and Technology of Shaanxi Province
WOS记录号: WOS:000335201100017
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/56868
Appears in Collections:北京大学第三临床医学院_心血管内科_期刊论文

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作者单位: 1.NW Univ Xian, Minist Educ, Coll Life Sci, Key Lab Resource Biol & Biotechnol Western China, Xian 710069, Shaanxi, Peoples R China
2.China Natl Ctr Biotechnol Dev, Beijing 100039, Peoples R China
3.Minist Educ, Key Lab Mol Cardiovasc Sci, Beijing 100083, Peoples R China
4.NW Univ Xian, Shaanxi Prov Key Lab Electroanalyt Chem, Inst Analyt Sci, Xian 710069, Shaanxi, Peoples R China
5.Peking Univ, Hosp 3, Inst Vasc Med, Beijing 100083, Peoples R China

Recommended Citation:
Zhao, Xinfeng,Li, Qian,Chen, Jiejun,et al. Exploring drug-protein interactions using the relationship between injection volume and capacity factor[J]. JOURNAL OF CHROMATOGRAPHY A,2014,1339:137-144.
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