Specific Isolation of Glycoproteins with Mesoporous Zirconia‐Polyoxometalate Hybrid

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EarlyView Article

  • Published: Mar 7, 2018
  • Author: Dandan Zhang, Mengmeng Wang, Zhiyong Guo, Pengfei Guo, Xuwei Chen, Jianhua Wang
  • Journal: PROTEOMICS


A novel mesoporous zirconia‐polyoxometalate ZrO2‐P8W48 hybrid was prepared using a surfactant‐assisted solvent evaporation technique. The acid–base reaction between the Zr‐OH groups of zirconium oxides and P8W48 was followed by self‐assembly with an amphiphilic triblock copolymer as template to obtain a polyoxometalate‐based hybrid. The ZrO2‐P8W48 hybrid was characterized by Fourier‐transform infrared spectroscopy (FT‐IR), thermal gravimetric assay (TGA), scanning electron microscopy (SEM), high‐resolution transmission electron microscopy (HR‐TEM), energy‐dispersive X‐ray spectroscopy (EDXS), X‐ray diffraction (XRD), and nitrogen sorption/desorption. Owing to the multiple hydrogen‐bonding interactions between the P8W48 moiety and the hydroxyl groups of glycoproteins, the ZrO2‐P8W48 hybrid exhibited highly selective isolation of glycoproteins from complex matrices that included various non‐glycoproteins. The retained glycoproteins could be readily recovered using a 0.01 mol L−1 cetane trimethyl ammonium bromide (CTAB) solution as stripping reagent, with recovery rates of 92, 100, 100, 100, and 74% for the five target glycoproteins, Ovalbumin (Ova), conalbumin (ConA), immunoglobulin G from human serum (IgG), γ‐globulin from bovine milk (γ‐Glo), and horseradish peroxidase (HRP), respectively. The ZrO2‐P8W48 hybrid was successfully applied to the isolation of glycoproteins from egg white and human serum samples, as confirmed by SDS‐PAGE and LC‐MS/MS assays.

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