Zwitter-ion modified hydrophilic carbon spheres and preparation thereof, and applications in glycopeptide enrichment

Abstract

The invention particularly relates to preparation of amphoteric ion modified hydrophilic carbon spheres, and applications of the amphoteric ion modified hydrophilic carbon spheres in glycopeptide enrichment. According to the invention, glucose is used as a carbon source, a choline phosphate type monomer is used as a functional reagent to provide zwitterions, and carbon spheres with a particle sizeof 200-400 nm and hydrophilic surfaces are prepared through a hydrothermal method, wherein the preparation process of the hydrophilic carbon spheres is simple, the reaction conditions are mild, and the used raw materials are environmentally friendly; and the enrichment performance of the zwitterionic hydrophilic carbon spheres on glycopeptides is inspected by using a standard glycoprotein IgG enzymatic hydrolysate, and the zwitterionic hydrophilic carbon spheres are further applied to glycoproteomics analysis in serum.

Description

technical field [0001] The invention specifically relates to the preparation of zwitterion-modified hydrophilic carbon spheres, which can be used for glycopeptide enrichment in the field of life and health. Background technique [0002] Protein glycosylation is one of the most important post-translational modifications, which occurs in more than half of human proteins according to the records and predictions of the Swiss-Prot database (literature 1.A.Bairoch et.al "The Swiss-ProtProtein Sequence Data Bank and Its Supplement Trembl", 1999). Glycoproteins have been shown to be involved in many important cellular activities and disease processes, such as cell communication, signaling and cell adhesion. More importantly, many glycoproteins have been considered as biomarkers and therapeutic targets in clinical research (literature 2.Y.Tian et.al "Solid-phase extraction of N-linked glycopeptides", "Nature Protocols", 2007, 2, 334). Therefore, the study of protein glycosylation ...

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Problems solved by technology

However, due to: (1) the complexity of biological samples is high, there are many high-abundance proteins, and the percentage of glycopeptides only accounts for 2% to 5% (document 3.G.Alvarez-Manilla et.al "Tools for Glycoproteomic Analysis: Size Exclusion Chromatography Facilitates Identification of Tryptic Glycopeptides with N-linked Glycosylation Sites", "Journal of Proteome Research", 2006, 5: 701-708)

(2) Compared with non-glycopeptides, the presence of sugar chains greatly reduces the ionization efficiency of glycopeptides. These two reasons cause extremely low glycopeptide signals, making direct analysis of glycopeptides in protein hydrolysates a huge challenge. challenge

Among them, most of the zwitterionic hydrophilic materials are based on silica, and the preparation process is complicated, time-consuming and involves toxic organic reagents

For example, the most widely used ZIC-HILIC-SPE synthesis steps are very complex and require more than 50 hours in total

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