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Ultrasensitive Detection of Biomarkers by Using a Molecular Imprinting Based Capacitive Biosensor
Published on: February 16, 2018
Preparation of surface molecularly imprinted polymeric microspheres and their recognition property for basic protein
Baojiao Gao1, Hongyan Fu, Yanbin Li
1Department of Chemical Engineering, North University of China, Taiyuan 030051, People' s Republic of China. gaobaojiao@126.com
Abstract:
The surface imprinting of basic protein lysozyme (Lys) was carried out by designing a new route. The copolymerization of N-vinylpyrrolidone (NVP) and 2-hydroxyethyl methacrylate (HEMA) was first conducted in an inverse suspension polymerization system, and the crosslinked copolymeric microspheres HEMA/NVP were prepared. Subsequently, the esterification reaction of methacryloyl (MAO) chloride with the hydroxyl groups on the surfaces of HEMA/NVP microspheres was performed, and the modified microspheres MAO-HEMA/NVP, on which a mass of polymerisable double bonds were introduced, were obtained. In the presence of lysozyme, by initiating of K(2)S(2)O(8)-NaHSO(3), the monomer methacrylic acid (MAA) in the solution was crosslink-polymerized on the surfaces of MAO-HEMA/NVP microspheres, resulting in the surface imprinting of lysozyme. After removing the template molecules, the lysozyme molecule-surface-imprinted material MIP-HEMA/NVP was obtained. Because there were strong interactions between lysozyme and monomer MAA, electrostatic interaction and hydrogen bonding, the lysozyme molecule-surface imprinting was successfully realized. The MIP-HEMA/NVP microspheres have very high binding affinity for lysozyme, and the binding capacity gets up to 216 mg/g. It is more important that MIP-HEMA/NVP microspheres have specific recognition selectivity for lysozyme, and the selectivity coefficient for lysozyme with respect to bovine hemoglobin (BHb), which was used as a contrast protein in the experiments, actually reaches 31.07. In the respect of protein imprinting, the imprinting material with such high performance is unwonted.

