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Abstract: High specific selectivity is the continuous goal of exploit glycoprotein-imprinted materials. Boronate-affinity-oriented surface imprinting can limit the heterogeneity of imprinted cavities, and PEGylation can reduce the nonspecific adsorption of imprinted materials towards non-target molecules. However, there are no reports on the integration of the above two advantages. Herein, we first integrated the boronate-affinity-oriented surface imprinting and PEGylation, and fabricated PEGylated boronate-affinity-oriented surface imprinting magnetic nanoparticles (PBSIMN) with horseradish peroxidase (HRP) as a model glycoprotein template. The successful synthesis of PBSIMN was demonstrated in detail by various characterization. Compared with non-PEGylated control, the PBSIMN showed greater adsorption capacity for HRP, and faster adsorption rate. To evaluate the improved performance, the PBSIMN was linked with hydrophilic boronic acid-modified/fluorescein isothiocyanate-loaded graphene oxide (BFGO), and used for the detection of HRP in real samples. Because PEGylation led to decrease of non-specific binding on PBSIMN, the proposed strategy provided ultrahigh sensitivity with limit of detection of 6.0 fg mL-1 for HRP, which were an order of magnitude lower than the non-PEGylated counterparts. When spiked with 0.05, 0.5 and 5.0 mg mL-1, recoveries of HRP were in the range of 97.4%-101.8% with relative standard deviation (RSD) no more than 5.4% for mouse serum, and between 98.2% and 103.2% with RSD no more than 5.0% human serum. This work indicates that the boronate-affinity-oriented surface imprinting and PEGylation can improve the performance of imprinted materials
Template and target information: protein, glycoprotein, horseradish peroxidase, HRP
Author keywords: PEGylation, oriented surface imprinting, glycoprotein, fluorescence, Dual boronate-affinity synergy