Issue 11, 2022

A novel hydrophilic hydrogel with a 3D network structure for the highly efficient enrichment of N-glycopeptides

Abstract

Protein glycosylation is of great significance in various physiological processes. Nevertheless, it remains a huge challenge to identify glycopeptides in complex biosamples by the direct mass spectrometry analysis due to the low ion efficiency and low abundance of glycopeptides. In this study, a novel hydrogel (denoted as ZIF-8/SAP) with a stable three-dimensional (3D) network structure and excellent hydrophilicity was successfully fabricated to capture glycopeptides with high efficiency. Owing to the unique characteristics, ZIF-8/SAP exhibited great selectivity (1 : 1000), great sensitivity (1 fmol μL−1), large binding capacity (300 mg g−1) and satisfactory reusability (seven cycles). Inspired by the great enrichment performance of the as-prepared material toward glycopeptides, ZIF-8/SAP was further applied to capture glycopeptides from a real human serum sample. The experimental results demonstrated that 217 N-glycosylation sites were identified in 283 N-glycopeptides, corresponding to 95 glycoproteins identified from 10 μL human serum by the nano-LC-MS/MS analysis, revealing the great potential of the novel ZIF-8/SAP hydrogel for glycopeptide enrichment and glycoproteomic research.

Graphical abstract: A novel hydrophilic hydrogel with a 3D network structure for the highly efficient enrichment of N-glycopeptides

Supplementary files

Article information

Article type
Paper
Submitted
24 Mar 2022
Accepted
07 Apr 2022
First published
21 Apr 2022

Analyst, 2022,147, 2425-2432

A novel hydrophilic hydrogel with a 3D network structure for the highly efficient enrichment of N-glycopeptides

H. Jin, W. Gao, R. Liu, J. Yang, S. Zhang, R. Han, J. Lin, S. Zhang, J. Yu and K. Tang, Analyst, 2022, 147, 2425 DOI: 10.1039/D2AN00516F

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