Preparation of molecular imprinted polymer with quaternary ammonium groups as recognition sites for separation of pig cyclophilin 18 and bovine serum albumin

• Published in: Journal of separation science Vol. 33; no. 12; pp. 1856 - 1862
• Main Authors: Liu, Huijuan, Han, Ruifang, Feng, Miao, Gao, Junfei, Long, Yi, Zhao, Zhuo, Wang, Ying, Mi, Huaifeng
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 01.06.2010; WILEY-VCH Verlag; WILEY‐VCH Verlag; Wiley
• Subjects: Adsorption; Analytical chemistry; Animals; Cationic; Chains (polymeric); Chemistry; Chromatographic methods and physical methods associated with chromatography; Chromatography, Gel; Cyclophilins - isolation & purification; Cyclophilins - metabolism; Electrophoresis, Polyacrylamide Gel; Exact sciences and technology; Imprinted polymers; Magnetic Resonance Spectroscopy; Microspheres; Molecular Weight; Protein-imprinted polymer; Proteins; Quaternary ammonium cationic groups; Quaternary Ammonium Compounds - metabolism; Recognition; Recognition sites; Separation; Separation of natural protein; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - isolation & purification; Serum Albumin, Bovine - metabolism; Spectroscopy, Fourier Transform Infrared; Surface Properties; Swine; Vinyl ester copolymer; Quaternary ammonium copolymer; Chemical enrichment; Affinity adsorbent; Characterization; Separation method; Isomerases; Acrylate copolymer; cis-trans-Isomerases; Ungulata; Quaternary ammonium cationic groups; Recognition sites; Trace analysis; Peptidylprolyl isomerase; Bovine; Enzyme; Separation of natural protein; Serum albumin; Serum protein; Pig; Vertebrata; Protein-imprinted polymer; Mammalia; Adsorption; Animal; Preparation; Molecular recognition; Artiodactyla; Molecular imprinting
• ISSN: 1615-9306; 1615-9314
• DOI: 10.1002/jssc.201000038

We introduce a new type of molecular imprinted polymer (MIP) with immobilized assistant recognition polymer chains (ARPCs) to create effective recognition sites. In this work, cloned pig cyclophilin 18 (pCyP18) and BSA were used as templates, respectively. The template protein was selectively assembled with ARPCs from the library which consists of numerous limited length polymer chains with randomly distributed recognition sites of the quaternary ammonium cationic groups and immobilizing sites. The assemblies of protein and ARPCs were adsorbed by macroporous microspheres and immobilized by cross-linking polymerization. After removing the templates, the two kinds of synthesized MIPs were used to adsorb cloned pCyP18 and BSA from protein mixtures respectively and both showed high selectivity. It confirms that this new method is suitable to separate proteins of both low and high molecular weight. The extended experiment on adsorption of natural pCyP18 from cytosol shows that the obtained MIP using cloned protein as template can be used to enrich natural protein of low content.