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Immobilizing CC chemokine receptor 4's N-terminal extracellular tail on a capillary to study its potential ligands by capillary electrophoresis
Chen W.1; Li M.1; Yakufu P.1; Ling X.1; Qi H.1; Xiao J.2; Wang Y.1
2012-04-01
Source PublicationAnalytical Biochemistry
ISSN00032697 10960309
Volume423Issue:1Pages:1-6
AbstractML40 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. © 2012 Elsevier Inc. All rights reserved.
KeywordCapillary electrophoresis Interaction ML40 Nonlinear chromatography Tertiary amine compounds chiral separation
DOI10.1016/j.ab.2011.12.033
URLView the original
Language英語
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Cited Times [WOS]:2   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionInstitute of Chinese Medical Sciences
Affiliation1.Peking University
2.Beijing Institute of Pharmacology and Toxicology
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GB/T 7714
Chen W.,Li M.,Yakufu P.,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.
APA Chen W..,Li M..,Yakufu P..,Ling X..,Qi H..,...&Wang Y..(2012).Immobilizing CC chemokine receptor 4's N-terminal extracellular tail on a capillary to study its potential ligands by capillary electrophoresis.Analytical Biochemistry,423(1),1-6.
MLA Chen W.,et al."Immobilizing CC chemokine receptor 4's N-terminal extracellular tail on a capillary to study its potential ligands by capillary electrophoresis".Analytical Biochemistry 423.1(2012):1-6.
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