文献类型：期刊文献

英文题名：Hydrophilic graphene oxide-dopamine-cationic cellulose composites and their applications in N-Glycopeptides enrichment

作者：Sheng, Qianying[1];Li, Junyan[2];Chen, Yingxin[1];Liang, Xinmiao[2];Lan, Minbo[1]

机构：[1]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Engn Res Ctr Pharmaceut Proc Chem, Sch Pharm, Minist Educ, Shanghai 200237, Peoples R China

年份：2021

卷号：226

外文期刊名：TALANTA

收录：;EI(收录号：20210709911380);WOS:【SCI-EXPANDED(收录号:WOS:000656959000072)】；

基金：This work was supported by the National Natural Science Foundation of China (21804041), and the Fundamental Research Funds for the Central Universities (No. 50321102017022).

语种：英文

外文关键词：Hydrophilic composites; Cationic cellulose; Glycopeptides; Selective enrichment; Mass spectrometry

摘要：Glycosylation is one of the most important post-translational modifications of proteins, and plays an important role in the structure and function of proteins. However, due to the diversity of glycopeptide forms and their low abundance, it is extraordinarily challenging to capture and separate glycopeptides with high selectivity from complex biological samples with mass spectrometric analysis. Here, we synthesized a new type of hydrophilic composite based on electrostatic interactions, which has been proven to be effective in immobilizing cationic cellulose on graphene oxide-dopamine carriers (expressed as GO-DA-JR), for highly specific enrichment of N-glycopeptides. The introduction of cationic cellulose provides not only a perfect surface charge for the composite but also a greater ability to enrich glycosylated peptides. Thirty-two glycopeptides from human serum immunoglobulin G (IgG) tryptic digests were observed with a greatly improved signal-to-noise ratio (S/N) and also presented high performance in anti-interfering enrichment of glycopeptides from complex samples containing 100-fold bovine serum albumin tryptic digests. In addition, GO-DA-JR has higher sensitivity (1 fmol/mu L IgG) and better enrichment capacity (up to 150 mg/g). Moreover, the results of glycopeptide enrichment and glycosylation analysis from human serum also show egood enrichment selectivity from real biological samples. This work exhibits high selectivity, high sensitivity, good stability and operability, indicating its potential for applications of glycopeptides enrichment in post-translational modification proteomics.