4.6 Article

Graphene oxide-based boronate polymer brushes via surface initiated atom transfer radical polymerization for the selective enrichment of glycoproteins

Journal

JOURNAL OF MATERIALS CHEMISTRY B
Volume 4, Issue 36, Pages 6125-6133

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c6tb01489e

Keywords

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Funding

  1. National Basic Research Program of China [2012CB910601]
  2. National Natural Science Foundation of China [21275080, 21475067]
  3. Natural Science Foundation of Tianjin [15JCYBJC20600]

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Biomedical sciences, and in particular biomarker research, demand efficient glycoprotein enrichment platforms. In this work, a facile and efficient method was developed to synthesize boronic acid polymer brushes immobilized on magnetic graphene oxide via surface initiated atom transfer radical polymerization (SI-ATRP) for the selective enrichment of glycoproteins from complex biological samples. The magnetic graphene oxide (GO@Fe3O4) nanocomposites were prepared by a solvothermal reaction, providing an ultrahigh surface area and allowing fast separation. Through the self-assembly procedure, the pyrene-based initiators (GO@Br) of SI-ATRP were easily functionalized on the GO sheet via noncovalent pi-pi interaction between pyrene and GO. Finally, the well-defined and high density poly(4-vinylphenylboronic acid) brushes (GO@PVPBA) via SI-ATRP were successfully fabricated. The morphology and structure of GO@Fe(3)O4, GO@Br, and GO@PVPBA nanocomposites were characterized by transmission electron microscopy (TEM), X-ray diffraction (XRD), vibrating sample magnetometry (VSM), Fourier transform-infrared spectroscopy (FTIR), and X-ray photoelectron spectroscopy (XPS). The selective recognition capability of GO@PVPBA nanocomposites was demonstrated by the selective enrichment of glycoproteins from a complex system consisting of standard proteins ovalbumin (OVA), transferrin (Trf), bovine serum albumin (BSA), and lysozyme (Lyz). Furthermore, the GO@PVPBA nanocomposite also exhibited a high binding capacity up to 514.8 and 445.9 mg g(-1) for OVA and Trf, respectively, and was applied to capture directly glycoproteins from the egg white samples.

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