Selective recognition in molecularly imprinted polymer and its chromatographic characterization for cinchonine
Selective recognition in molecularly imprinted polymer and its chromatographic characterization for cinchonine作者机构：School of Chemistry and Chemical Engineering Central South University Changsha 410083 China School of Chemistry and Chemical Engineering Central South University Changsha 410083 China School of Chemistry and Chemical Engineering Central South University Changsha 410083 China School of Chemistry and Chemical Engineering Central South University Changsha 410083 China
出 版 物：《Journal of Central South University of Technology》 (中南工业大学学报（英文版）)
年 卷 期：2005年第12卷第Z1期
页 面：102-107页
核心收录：
学科分类：081704[工学-应用化学] 07[理学] 0806[工学-冶金工程] 08[工学] 0817[工学-化学工程与技术] 070302[理学-分析化学] 0703[理学-化学]
基 金：Project(2004035085) supported by the Postdoctoral Science Foundation of China project(04JJ3080) supported by theNatural Science Foundation of Hunan Province
主 题：molecular imprinting cinchonine chiral separation HPLC
摘 要：A molecularly imprinting polymer (MIP) was synthesized via bulk polymerization under different conditions using anti-ague drug cinchonine (CN) as template. Infrared spectra (IR) results show that the template CNand functional monomer α-methyl acrylic acid (MAA) formed complexes before polymerization and the structure of complexes was simulated by Hyperchem. The results indicate that there are hydrogen bond or ionic bond between functional monomer and template molecule in acetonitrile solution. The MIP made in cold-initiated photo-polymerization has higher separation performance than that in the therm-initiated polymerization. The separation of the isomers CN and cinchonidine (CD) can be successfully obtained when its separate factor α reaches 1.82. Scatchard analysis suggests that the MIP recognizing CN with two classes of binding sites. The partition coefficient Kd, 1 and apparent maximum number nmax, 1 of binding sites with high affinity are 131.43 μmol/L and 58. 90 μmol/g, respectively,while Kd, 2 and nmax, 2 of binding sites with low affinity are 2.32 mmol/L and 169.08 mmol/g, respectively.
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