2 research outputs found

    Dual-Functionalized Magnetic Metalā€“Organic Framework for Highly Specific Enrichment of Phosphopeptides

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    The highly specific enrichment of phosphoproteins and phosphopeptides from intricate biological systems is the precondition of in-depth phosphoproteome research. Herein, a novel dual-functionalized magnetic zirconium-based metalā€“organic framework (MOF) denoted as DFMMOF, with the purpose of combining the affinity of immobilized metal ion affinity chromatography (IMAC) and metal oxide affinity chromatography (MOAC) has been successfully synthesized. The inherent Zrā€“O cluster of DFMMOF particles acted as MOAC and the immobilized titaniumĀ­(IV) ions served for IMAC. The obtained DFMMOF exhibited rapid magnetic separation (within 5 s), large surface area (237.9 m<sup>2</sup> g<sup>ā€“1</sup>), high binding capacity (100 mg g<sup>ā€“1</sup>), and good postenrichment recovery (84.8%). Thanks to the strong affinity, low detection sensitivity (5 fmol) and high selectivity (Ī²-casein/BSA with a molar ratio of 1:1000) for phosphopeptide enrichment were obtained using DFMMOF as absorbent. Moreover, the effective identification of phosphopeptides from real samples (human serum and nonfat milk) further confirmed the immense potential of DFMMOF as a promising candidate for the detection and extraction of trace amounts of phosphorylated peptides in complex biosamples

    Maltose-Functionalized Hydrophilic Magnetic Nanoparticles with Polymer Brushes for Highly Selective Enrichment of Nā€‘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>ā€“PEIā€“pMaltose were designed and synthesized via a simple two-step modification. The obtained superhydrophilic Fe<sub>3</sub>O<sub>4</sub>ā€“PEIā€“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>ā€“PEIā€“pMaltose NPs was attributed to graft of maltose polymer brushes and efficient assembly strategy. Moreover, Fe<sub>3</sub>O<sub>4</sub>ā€“PEIā€“pMaltose NPs were further utilized to selectively enrich glycopeptides from human renal mesangial cell (HRMC, 200 Ī¼g) 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>ā€“PEIā€“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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