Journal
NANOSCALE
Volume 11, Issue 22, Pages 10952-10960Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9nr01441a
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Funding
- Zhejiang Public Welfare Technology Research Plan/Rural Agriculture [LGN18B010001]
- Open Project of the Key Laboratory of Modern Toxicology of Ministry of Education, Nanjing Medical University [NMUAMT201807]
- Scientific Research Project of Zhejiang Provincial Education Department [Y201839892]
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High-performance affinity materials are highly required in the sample preparation process in mass spectrometry- based glycoproteomics studies. In this research, a novel magnetic nanofiber-based zwitterionic hydrophilic material is prepared for glycopeptide enrichment and identification. The one-dimensional hydroxyapatite nanofiber (HN) acted as the supporting substance for immobilizing both Fe3O4 nanoparticles and Au nanoparticles, following the surface modification with a zwitterionic tripeptide L-glutathione (GSH) via the affinity interactions between the thiol group in GSH and both Au and Fe3O4 to form the magHN/Au-GSH nanofiber. Owing to the unique structural features, excellent hydrophilicity, abundant zwitterionic molecules, and strong magnetic responsiveness, the as-prepared magHN/Au-GSH nanofiber possesses satisfactory specificity for glycopeptide enrichment. As a result, the magHN/Au-GSH nanofiber demonstrated great detection sensitivity (2 fmol), satisfying enrichment recovery (89.65%), large binding capacity (100 mg g-1), and high enrichment selectivity (1 : 100) toward glycopeptides. Furthermore, 246 N-glycosylated peptides corresponding to 104 N-glycosylated proteins were identified from only 1 mu L human serum, revealing the great potential of this affinity nanofiber for glycopeptide enrichment and glycoproteomics research.
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