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Updated: Sep 18, 2025

Detection and Enrichment of Rare Antigen-specific B Cells for Analysis of Phenotype and Function
Published on: February 16, 2017
A simple and highly efficient method for enriching and separating glycoproteins in complex biological samples using
Hang Gong1,2, Ruirui Hu3, Feng Chen3
1Yunnan Key Laboratory of Modern Separation Analysis and Substance Transformation, College of Chemistry and Chemical Engineering, Yunnan Normal University, Kunming, 650500, China. hgong@xtu.edu.cn.
Abstract:
Alterations in glycosylation patterns have been observed in many diseases, including inflammatory, auto-immune, and infectious diseases as well as cancer. However, the low concentrations of glycoproteins in biological samples make it difficult to enrich and separate glycoproteins efficiently before determination. In this study, a composite material was prepared in which Fe3O4-based magnetic nanospheres were modified with polyethyleneimine (PEI)- and boric acid-grafted metal-organic frameworks (MOFs) to enable the selective enrichment and separation of glycoproteins from complex biological samples. With the coordination between amino and boric acid, a teamed boronate affinity (TBA) molecular group is formed, which enables the cyclization of boric acid and the cis-diol groups in glycoproteins to be achieved at physiological pH. In addition, the abundant hydrogen bonds between amino and glycoprotein also increase the affinity of the synthesized Fe3O4@MOF@PEI@BBA nanoparticles for glycoprotein. The adsorption capacities for ovalbumin, transferrin, and horseradish peroxidase were 489.3, 522.0, and 578.2 mg/g, respectively. Meanwhile, adsorption equilibrium was achieved within 30 min under mild physiological conditions (pH = 7.4, T = 25 °C).
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