2 research outputs found

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

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    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 Fe<sub>3</sub>O<sub>4</sub> 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 Fe<sub>3</sub>O<sub>4</sub> nanoparticles by sonication. Second, the hydrophilic maltose-functionalized Fe<sub>3</sub>O<sub>4</sub> (Fe<sub>3</sub>O<sub>4</sub>-DA-Maltose) NPs were obtained via copper­(I)-catalyzed azide–alkyne cycloaddition (click chemistry). The morphology, structure, and composition of Fe<sub>3</sub>O<sub>4</sub>-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 Fe<sub>3</sub>O<sub>4</sub>-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 μL<sup>–1</sup>, a large binding capacity up to 43 mg g<sup>–1</sup>, and good recovery for glycopeptides enrichment (85–110%). Moreover, the Fe<sub>3</sub>O<sub>4</sub>-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

    Maltose-Functionalized Hydrophilic Magnetic Nanoparticles with Polymer Brushes for Highly Selective Enrichment of N‑Linked Glycopeptides

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    Efficient enrichment glycoproteins/glycopeptides from complex biological solutions are very important in the biomedical sciences, in particular biomarker research. In this work, the high hydrophilic polyethylenimine conjugated polymaltose polymer brushes functionalized magnetic Fe<sub>3</sub>O<sub>4</sub> nanoparticles (NPs) denoted as Fe<sub>3</sub>O<sub>4</sub>–PEI–pMaltose were designed and synthesized via a simple two-step modification. The obtained superhydrophilic Fe<sub>3</sub>O<sub>4</sub>–PEI–pMaltose NPs displayed outstanding advantages in the enrichment of N-linked glycopeptides, including high selectivity (1:100, mass ratios of HRP and bovine serum albumin (BSA) digest), low detection limit (10 fmol), large binding capacity (200 mg/g), and high enrichment recovery (above 85%). The above-mentioned excellent performance of novel Fe<sub>3</sub>O<sub>4</sub>–PEI–pMaltose NPs was attributed to graft of maltose polymer brushes and efficient assembly strategy. Moreover, Fe<sub>3</sub>O<sub>4</sub>–PEI–pMaltose NPs were further utilized to selectively enrich glycopeptides from human renal mesangial cell (HRMC, 200 μg) tryptic digest, and 449 N-linked glycopeptides, representing 323 different glycoproteins and 476 glycosylation sites, were identified. It was expected that the as-synthesized Fe<sub>3</sub>O<sub>4</sub>–PEI–pMaltose NPs, possessing excellent performance (high binding capacity, good selectivity, low detection limit, high enrichment recovery, and easy magnetic separation) coupled to a facile preparation procedure, have a huge potential in N-glycosylation proteome analysis of complex biological samples
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