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学科主题: 药学
题名:
Immobilizing CC chemokine receptor 4′s N-terminal extracellular tail on a capillary to study its potential ligands by capillary electrophoresis
作者: Chen, Wenjing1,2; Li, Meina1,2; Yakufu, Pazilaiti1,2; Ling, Xiaomei1,2; Qi, Hui3,4; Xiao, Junhai5; Wang, Ying3,4
关键词: Tertiary amine compounds chiral separation ; ML40 ; Nonlinear chromatography ; Interaction ; Capillary electrophoresis
刊名: ANALYTICAL BIOCHEMISTRY
发表日期: 2012-04-01
DOI: 10.1016/j.ab.2011.12.033
卷: 423, 期:1, 页:1-6
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemical Research Methods ; Biochemistry & Molecular Biology ; Chemistry, Analytical
研究领域[WOS]: Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]: ZONE ELECTROPHORESIS ; STATIONARY-PHASE ; ELECTROOSMOTIC FLOW ; SEPARATION ; SYSTEM ; ELECTROCHROMATOGRAPHY ; MICROREACTOR ; BINDING ; COLUMN
英文摘要:

ML40 is the equivalent peptide derived from the N terminal of CCC4 (CC chemokine receptor 4), which plays a pivotal role in allergic inflammation. A new capillary electrophoresis method was developed to study the interactions between ML40 and its potential ligands in which ML40 was immobilized on the inner wall of capillary as the stationary phase based on the covalent linking technique. The interaction between S009, a known CCR4 antagonist, and the immobilized ML40 was studied to validate the bioactivity of ML40. The electropherogram of S009 showed that the peak height was reduced and the peak width was broadened in the ML40 immobilized capillary. Otherwise, 25 computer-aided design and drafting compounds were screened out using this method. Four compounds′ peak widths were broadened and their peak heights were reduced, as with S009. Meanwhile, nonlinear chromatography was used to calculate the constants for the ligand-receptor complex formation. Furthermore, the tertiary amine compounds belonging to the chiral tertiary amines of the type NRR′R ′′, which are optically inactive resulting from rapid pyramide inversion, were chiral separated by our protein immobilization method for the first time. In general, the methodology presented would be applicable to study compound-ML40 interactions as a reliable and robust screening method for CCR4 antagonist discovery. (C) 2012 Elsevier Inc. All rights reserved.

语种: 英语
所属项目编号: 30671907 ; 30472093 ; 81072612 ; 7102107 ; K20090207 ; 2009ZX09301-010
项目资助者: National Natural Science Foundation of China ; Natural Science Foundation of Beijing ; Open Foundation of State Key Laboratory of Natural and Biomimetic Drugs ; National New Drug Research and Development Project
WOS记录号: WOS:000301759200001
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/56012
Appears in Collections:北京大学药学院_化学生物学系_期刊论文

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作者单位: 1.Peking Univ, Sch Pharmaceut Sci, Dept Pharmaceut Anal, Beijing 100191, Peoples R China
2.Peking Univ, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
3.Peking Univ, Ctr Human Dis Genom, Beijing 100191, Peoples R China
4.Peking Univ, Sch Basic Med Sci, Dept Med Immunol, Beijing 100191, Peoples R China
5.Beijing Inst Pharmacol & Toxicol, Beijing 100850, Peoples R China

Recommended Citation:
Chen, Wenjing,Li, Meina,Yakufu, Pazilaiti,et al. Immobilizing CC chemokine receptor 4′s N-terminal extracellular tail on a capillary to study its potential ligands by capillary electrophoresis[J]. ANALYTICAL BIOCHEMISTRY,2012,423(1):1-6.
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