1. A novel hydrophilic hydrogel with a 3D network structure for the highly efficient enrichment of N-glycopeptides.
- Author
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Jin, Haozhou, Gao, Wenqing, Liu, Rong, Yang, Jiaqian, Zhang, Shun, Han, Renlu, Lin, Jing, Zhang, Sijia, Yu, Jiancheng, and Tang, Keqi
- Subjects
GLYCOPROTEIN analysis ,HYDROGELS ,GLYCOPEPTIDES ,BLOOD serum analysis ,GLYCOPROTEINS - 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. [ABSTRACT FROM AUTHOR]- Published
- 2022
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