Highly Efficient Separation of Glycoprotein by Dual-Functional Magnetic Metal-Organic Framework with Hydrophilicity and Boronic Acid Affinity

Protein glycosylation plays a critical role in post translational modifications of proteins in the organism and is involved in many diseases. However, the huge challenge for glycoproteins to be highly specific isolated and adsorbed from complicated biological samples results from their low abundance and interference. In this work, a novel dual-functionalized magnetic metal-organic frameworks nanoparticle for selective enrichment of glycoproteins was synthesized for the first time. Due to the abundant amino groups and grafted phenylboronic acid, the proposed nanoparticles have the dual properties of hydrophilicity and boronic acid affinity. The obtained nanoparticles show high binding capacities toward glycoproteins under physiological state (pH 7.4) such as ovalbumin (327.28 mg/g), transferrin (241.17 mg/g), horseradish peroxidase (530.79 mg/g). Furthermore, the nanoparticles still have excellent enrichment performance after being used six times repeatedly. More importantly, the prepared nanoparticles also have great potential applications in the adsorption of glycoproteins from complex biological specimens.