Click Synthesis of Hydrophilic Maltose-Functionalized Iron Oxide Magnetic Nanoparticles Based on Dopamine Anchors for Highly Selective Enrichment of Glycopeptides

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• 作者：Changfen Bi ; Yingran Zhao ; Lijin Shen ; Kai Zhang ; Xiwen He ; Langxing Chen ; Yukui Zhang
• 刊名：ACS Applied Materials & Interfaces
• 出版年：2015
• 出版时间：November 11, 2015
• 年：2015
• 卷：7
• 期：44
• 页码：24670-24678
• 全文大小：531K
• ISSN：1944-8252

文摘

The development of methods to isolate and enrich low-abundance glycopeptides from biological samples is crucial to glycoproteomics. Herein, we present an easy and one-step surface modification strategy to prepare hydrophilic maltose functionalized Fe₃O₄ nanoparticles (NPs). First, based on the chelation of the catechol ligand with iron atoms, azido-terminated dopamine (DA) derivative was assembled on the surface of magnetic Fe₃O₄ nanoparticles by sonication. Second, the hydrophilic maltose-functionalized Fe₃O₄ (Fe₃O₄-DA-Maltose) NPs were obtained via copper(I)-catalyzed azide鈥揳lkyne cycloaddition (click chemistry). The morphology, structure, and composition of Fe₃O₄-DA-Maltose NPs were investigated by Fourier transform infrared spectroscopy (FT-IR), transmission electron microscopy (TEM), X-ray powder diffraction (XRD), X-ray photoelectron spectrometer (XPS), and vibrating sample magnetometer (VSM). Meanwhile, hydrophilicity of the obtained NPs was evaluated by water contact angle measurement. The hydrophilic Fe₃O₄-DA-Maltose NPs were applied in isolation and enrichment of glycopeptides from horseradish peroxidase (HRP), immunoglobulin (IgG) digests. The MALDI-TOF mass spectrometric analysis indicated that the novel NPs exhibited high detection sensitivity in enrichment from HRP digests at concentration as low as 0.05 ng 渭L^鈥?, a large binding capacity up to 43 mg g^鈥?, and good recovery for glycopeptides enrichment (85鈥?10%). Moreover, the Fe₃O₄-DA-Maltose NPs were applied to enrich glycopeptides from human renal mesangial cells (HRMC) for identification of N-glycosylation sites. Finally, we identified 115 different N-linked glycopeptides, representing 93 gene products and 124 glycosylation sites in HRMC.