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Boronate Affinity Monolith with a Gold Nanoparticle‐Modified Hydrophilic Polymer as a Matrix for the Highly Specific Capture of Glycoproteins
Author(s) -
Wu Ci,
Liang Yu,
Zhao Qun,
Qu Yanyan,
Zhang Shen,
Wu Qi,
Liang Zhen,
Zhang Lihua,
Zhang Yukui
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201402787
Subject(s) - monolith , chemistry , ethylene glycol , selectivity , methacrylate , chromatography , horseradish peroxidase , glycidyl methacrylate , affinity chromatography , bovine serum albumin , polymer , combinatorial chemistry , polymer chemistry , organic chemistry , polymerization , enzyme , catalysis
As low abundance is the great obstacle for glycoprotein analysis, the development of materials with high efficiency and selectivity for glycoprotein enrichment is a prerequisite in glycoproteome research. Herein, we report a new kind of hydrophilic boronate affinity monolith by attaching 4‐mercaptophenylboronic acid (MPBA) with 2‐mercaptoethylamine (MPA) on the gold nanoparticle‐modified poly(glycidyl methacrylate‐co‐poly(ethylene glycol) diacrylate)) monolith for glycoprotein enrichment. With poly(ethylene glycol) diacrylate as the cross‐linker and the further modification of gold nanoparticles, the matrix has advantages of good hydrophilicity and enhanced surface area, which are beneficial to improve the enrichment selectivity and efficiency for glycoproteins. The attachment of MPBA and MPA provide intramolecular BN coordination, which could further enhance the specificity of glycoprotein capture. Such a boronate affinity monolith was applied to enrich horseradish peroxidase (HRP) from the mixture of HRP and bovine serum albumin (BSA), and high selectivity was obtained even at a mass ratio of 1:1000. In addition, the binding capacity of ovalbumin on such monolith reached 390 μg g −1 . Furthermore, the average recovery of HRP on the prepared affinity monoliths was (84.8±1.9) %, obtained in three times enrichment with the same column. Finally, the boronate affinity monolith was successfully applied for the human‐plasma glycoproteome analysis. As a result, 160 glycoproteins were credibly identified from 9 μg of human plasma, demonstrating the great potential of such a monolith for large‐scale glycoproteome research.