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A novel hydrophilic hydrogel with a 3D network structure for the highly efficient enrichment of N-glycopeptides.
- Source :
- Analyst; 6/7/2022, Vol. 147 Issue 11, p2425-2432, 8p
- Publication Year :
- 2022
-
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<superscript>−1</superscript>), large binding capacity (300 mg g<superscript>−1</superscript>) 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]
- Subjects :
- GLYCOPROTEIN analysis
HYDROGELS
GLYCOPEPTIDES
BLOOD serum analysis
GLYCOPROTEINS
Subjects
Details
- Language :
- English
- ISSN :
- 00032654
- Volume :
- 147
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- Analyst
- Publication Type :
- Academic Journal
- Accession number :
- 157152850
- Full Text :
- https://doi.org/10.1039/d2an00516f