文献类型：期刊文献

英文题名：Oriented Assembly of Hydrophilic Nanochains Modified by Porous Zirconium-Based Coordination Polymers for Glycopeptides Analysis

作者：Gu, Qinying[1]; Zhao, Hongli[1]; Zhu, Tianyi[1]; Lu, Yichen[1]; Lin, Yunfan[1]; Yuan, Huihui[1]; Lan, Minbo[1,2]

机构：[1] Shanghai Key Laboratory of Functional Materials Chemistry, School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai, 200237, China; [2] Research Center of Analysis and Test, East China University of Science and Technology, Shanghai, 200237, China

年份：2023

外文期刊名：SSRN

收录：EI(收录号：20230141417)

语种：英文

外文关键词：Glycoproteins - Magnetite - Mass spectrometry - Molar ratio - Peptides - Reusability - Zirconium

摘要：Mass spectrometry (MS)-based glycoproteomics research requires additional sample pretreatment to improve the effective identification of low-abundance glycopeptides without interference from non-glycoproteins. Herein, an attractive strategy was established to prepare one-dimensional porous coordination polymer composites (Fe3O4@RF@Zr-BCP) for glycopeptide enrichment before MS analysis. The obtained Fe3O4@RF@Zr-BCP nanochains feature excellent magnetic response (42.26 emu/g), high hydrophilicity (16.0 °), and large specific surface area (140.84 m2/g), which provides abundant affinity sites for specific capture of glycopeptides. The materials exhibit outstanding performance in the enrichment of glycopeptides in terms of sensitivity (15 fmol/μL IgG), selectivity (1:200, molar ratio of IgG/BSA), loading capacity (200 mg/g) and recovery (106.4 ± 3.5%). In addition, the developed method based on Fe3O4@RF@Zr-BCP has been successfully applied to capture glycopeptides in tryptic digest of mouse teratoma cell extracts. It is worth emphasizing that compared with dispersed nanoparticles, the one-dimensional chain structure brings extraordinary reusability to Fe3O4@RF@Zr-BCP nanochains, which is conducive to the rapid cyclic enrichment of glycopeptides. This present work provides a potential enrichment platform for comprehensive glycoprotein analysis, and opens a new avenue for the application of oriented-assembly nanochains. ? 2023, The Authors. All rights reserved.