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Abstract: N-(p-Vinylbenzyl)-N,N-bis[2-(3-carboxypropionyloxy)ethyl] amine has been designed and synthesized as a novel functional monomer for molecular imprinting, the structure of which was established with elemental analysis, FT-IR and 1H NMR spectroscopy. The binding mechanism between this functional monomer and bovine serum albumin was studied by a fluorescence quenching method and measurement of synchronous fluorescence intensity. These research results indicated that at ionic strength 0.5 mol L-1 and pH 7.4, the monomer had strong interaction with tryptophan residues of bovine serum albumin. The composition ratio of the complex formed between the monomer and bovine serum albumin is 2:1, and the apparent binding constant between them is KA=2.239×10 11 L2 mol-2. Based on this study, a molecularly imprinted composite polymeric membrane was prepared over a poly(vinylidene fluoride) film support in aqueous solution using the novel monomer as a functional one, bovine serum albumin as template molecules and N,N'-methylenebisacrylamide as a crosslinker. Permselectivity of the imprinted composite membrane to bovine serum albumin was tested by diffusion experiments. These results showed that the imprinted composite membrane exhibited higher transport selectivity to the template molecule bovine serum albumin than human serum albumin and ovum protein. The diffusion experiments for the imprinted and non-imprinted membranes indicated that the imprinted one also took on high permselectivity for the template molecule bovine serum albumin in comparison with the non-imprinted one.
Template and target information: protein, bovine serum albumin, BSA
Author keywords: N-(p-vinylbenzyl)-N,N-bis[2-(3-carboxypropionyloxy)ethyl] amine, template molecule, Bovine serum albumin, Molecularly imprinted composite membrane