Facile synthesis of hydrophilic magnetic graphene nanocomposites via dopamine self-polymerization and Michael addition for selective enrichment of N-linked glycopeptides

• Published in: Scientific reports 2020-01, Vol.10 (1), p.71, Article 71
• Main Authors: Bi, Changfen, Yuan, Ye, Tu, Yuran, Wu, Jiahui, Liang, Yulu, Li, Yiliang, He, Xiwen, Chen, Langxing, Zhang, Yukui
• Format: Article
• Language: English
• Subjects: 631/92; 639/301; 639/638; 692/53; Antibiotics; Biological samples; Bovine serum albumin; Cell Line; Chitosan; Chitosan - chemistry; Chromatography, High Pressure Liquid; Dopamine; Dopamine - chemistry; Dopamine - metabolism; Ferrosoferric Oxide - chemistry; Glycopeptides; Glycopeptides - analysis; Glycoproteins; Glycosylation; Graphene; Graphite - chemistry; Horseradish peroxidase; Humanities and Social Sciences; Humans; Hydrophobic and Hydrophilic Interactions; Iron oxides; Limit of Detection; Magnetite Nanoparticles - chemistry; multidisciplinary; Nanocomposites; Nanocomposites - chemistry; Polymerization; Science; Science (multidisciplinary); Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-019-56944-4

The development of methods to effectively capture N-glycopeptides from the complex biological samples is crucial to N-glycoproteome profiling. Herein, the hydrophilic chitosan–functionalized magnetic graphene nanocomposites (denoted as Fe 3 O 4 -GO@PDA-Chitosan) were designed and synthesized via a simple two-step modification (dopamine self-polymerization and Michael addition). The Fe 3 O 4 -GO@PDA-Chitosan nanocomposites exhibited good performances with low detection limit (0.4 fmol·μL −1 ), good selectivity (mixture of bovine serum albumin and horseradish peroxidase tryptic digests at a molar ration of 10:1), good repeatability (4 times), high binding capacity (75 mg·g −1 ). Moreover, Fe 3 O 4 -GO@PDA-Chitosan nanocomposites were further utilized to selectively enrich glycopeptides from human renal mesangial cell (HRMC, 200 μg) tryptic digest, and 393 N-linked glycopeptides, representing 195 different glycoproteins and 458 glycosylation sites were identified. This study provides a feasible strategy for the surface functionalized novel materials for isolation and enrichment of N-glycopeptides.