Issue 6, 2014

Synthesis of boronic acid-functionalized molecularly imprinted silica nanoparticles for glycoprotein recognition and enrichment

Abstract

A novel imprinting strategy using reversible covalent complexation of glycoprotein is described for creating glycoprotein-specific recognition cavities on 3-acrylamidophenylboronic acid-immobilized silica nanoparticles (SiO2@AAPBA). Two kinds of organic silanes (3-aminopropyltriethoxysilane (APTES) and n-octyltrimethoxysilane (OTMS)) were then polymerized on the surface of SiO2@AAPBA after the template (horseradish peroxidase (HRP)) was covalently immobilized by forming cyclic boronate complexes and their influence was examined. The results showed that not only the silane composition but also the relative proportions play an important role in glycoprotein imprinting. The template recognition properties were evaluated by single-protein or competitive batch rebinding experiments, and the results showed that the HRP-imprinted silica nanoparticles (HRP-MIP silica NPs) exhibited higher recognition ability and selectivity towards the template than the nonimprinted silica NPs and their corresponding imprinted factor (a) reached 2.71. The as-prepared HRP-MIP silica NPs could not only differentiate the template from another glycoprotein, but also enrich HRP from spiked human serum. The good results demonstrated their potential in glycoproteomic analysis.

Graphical abstract: Synthesis of boronic acid-functionalized molecularly imprinted silica nanoparticles for glycoprotein recognition and enrichment

Supplementary files

Article information

Article type
Paper
Submitted
29 Oct 2013
Accepted
22 Nov 2013
First published
25 Nov 2013

J. Mater. Chem. B, 2014,2, 637-643

Synthesis of boronic acid-functionalized molecularly imprinted silica nanoparticles for glycoprotein recognition and enrichment

Z. Lin, L. Sun, W. Liu, Z. Xia, H. Yang and G. Chen, J. Mater. Chem. B, 2014, 2, 637 DOI: 10.1039/C3TB21520B

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