Chem. J. Chinese Universities ›› 2016, Vol. 37 ›› Issue (11): 2092.doi: 10.7503/cjcu20160437

• Polymer Chemistry • Previous Articles     Next Articles

Utilizing Macromolecular Chain as Functional Monomer and Crosslinker to Imprint BSA with Preserving the Structural Integrity of Template

QIAN Liwei1,*(), LI Ji2, SONG Wenqi2, HU Xiaoling2, GUAN Ping2   

  1. 1. College of Bioresources Chemical and Materials Engineering,Shaanxi University of Science and Technology, Xi’an 710021, China
    2. School of Natural and Applied Science, Northwestern Polytechnical University, Xi’an 710072, China
  • Received:2016-06-17 Online:2016-11-10 Published:2016-09-20
  • Contact: QIAN Liwei E-mail:qianliwei@mail.nwpu.edu.cn
  • Supported by:
    † Supported by the National Natural Science Foundation of China(No;21174111) and the Key projects of National Natural Science Foundation of China(No;51433008)

Abstract:

Protein imprinted hydrogels were prepared via redox initiated polymerization by utilizing bovine serum albumin(BSA) as a template and poly(hydroxyethylacrylate-vinylimidazole-[1-(allylacetate)-3-vinyl-imidazolium]chloride) [P(HEA-co-VIM-co-[AVIM]Cl)] as the macromolecularly functional monomer and crosslinker. The analytical results of circular dichroism and synchronous fluorescence spectrum demonstrated that P(HEA-co-VIM-co-[AVIM]Cl) could effectively maintain the structural stability of BSA, while the equivalent HEA, VIM and [AVIM]Cl denatured the template protein. The selective and competitive adsorption experiments showed that the imprinted hydrogels made by P(HEA-co-VIM-co-[AVIM]Cl) obtained better selectivity and recognition ability compared with those made by HEA, VIM and [AVIM]Cl. Therefore, the above results suggested the significant advantage of maintaining the structural and conformational stability of template protein during the preparation of imprinted polymers. The strategy of using macromolecule monomer to imprint protein could effectively overcome the difficulty of mutability of protein, therefore would promote the development and application of protein imprinting technology.

Key words: Molecularly imprinting technology, Protein imprinting, Stability of protein, Circular dichroism, Synchronous fluorescence spectrum

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