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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.
Template and target information: protein, bovine serum albumin, BSA
Author keywords: molecularly imprinting technology, protein imprinting, Stability of protein, circular dichroism, Synchronous fluorescence spectrum