Hydrophilic Mesoporous Silica Materials for Highly Specific Enrichment of N‑Linked Glycopeptide

• Published in: Analytical chemistry (Washington) Vol. 89; no. 3; pp. 1764 - 1771
• Main Authors: Sun, Nianrong, Wang, Jiawen, Yao, Jizong, Deng, Chunhui
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 07.02.2017
• Subjects: Affinity; Chromatography; Chromatography, Liquid; Enrichment; Ferrosoferric Oxide - chemistry; Glycopeptides; Glycopeptides - analysis; Glycopeptides - blood; Glycopeptides - isolation & purification; Horseradish Peroxidase - chemistry; Horseradish Peroxidase - metabolism; Humans; Hydrophobic and Hydrophilic Interactions; Imino Acids - chemistry; Immunoglobulin G - chemistry; Immunoglobulin G - metabolism; Magnetite Nanoparticles - chemistry; Nanomaterials; Nanostructures - chemistry; Peptides; Platforms; Porosity; Porous materials; Proteomics; Silica; Silicon dioxide; Silicon Dioxide - chemistry; Strategy; Surface area
• ISSN: 0003-2700; 1520-6882
• DOI: 10.1021/acs.analchem.6b04054

Hydrophilic interaction liquid chromatography (HILIC) is a significant enrichment strategy in glycoproteomics profiling. In this report, hydrophilic magnetic mesoporous silica materials (denoted as Fe3O4@mSiO2-IDA) were designed and synthesized as an outstanding enrichment platform for glycopeptide analysis. By taking advantage of their merits, such as large surface area, excellent hydrophilicity and unbiased affinity toward all types of glycopeptides, the Fe3O4@mSiO2-IDA nanomaterials were successfully applied to capture glycopeptides from complex samples. A total of 25 glycopeptides from horseradish peroxidase (HRP) digests and 33 glycopeptides from IgG were identified, respectively. Especially, as a result, 424 glycopeptides assigned to 140 glycoproteins were identified from only 2 μL human serum.