In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge

doi:10.1021/acs.analchem.6b04394

	In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge
	Yan, Jingyu 1; Yu, Long 1; Guo, Zhimou 1; Zou, Hanfa 1; Ye, Mingliang 1; Liang, Xinmiao 1; Dong, Xuefang 1; Qin, Hongqiang 1; Mao, Jiawei 1,2; Yu, Dongping 1,2
刊名	ANALYTICAL CHEMISTRY
	2017-04-04
卷号	89 期号:7 页码:3966-3972
ISSN号	0003-2700
DOI	10.1021/acs.analchem.6b04394
文献子类	Article
英文摘要	Sialylation typically occurs at the terminal of glycans, and its aberration often correlates with diseases including neurological diseases and cancer. However, the analysis of glycoprotein sialylation in complex biological samples is still challenging due to their low abundance. Herein, a histidine-bonded silica (HBS) material with a hydrophilic interaction and switchable surface charge was fabricated to enrich sialylated glycopeptides (SGPs) from the digest of proteomics samples. High selectivity toward SGPs was obtained by combining the superior hydrophilicity and switchable-charge characteristics. During the enrichment of sialylated glycopeptides from bovine fetuin digest, seven glycopeptides were detected even at the ratio of 1:5000 with the nonsialylated glycopeptides, demonstrating the high specificity of SGP enrichment by using HBS material. Then, HBS material was further utilized to selectively enrich SGPs from the protein digest of human serum, and 487 glycosites were identified from only 2 mu L of human serum; 92.0% of the glycopeptides contained at least one sialic acid, indicating good performance for SGP enrichment by using HBS material. Furthermore, the prepared HBS material also has great potential applications in the analysis of glycoprotein sialylation from other complex biological samples.
WOS关键词	TITANIUM-DIOXIDE CHROMATOGRAPHY ; MASS-SPECTROMETRY ; GLYCOPEPTIDE ENRICHMENT ; SELECTIVE ENRICHMENT ; HYDRAZIDE CHEMISTRY ; STATIONARY PHASES ; N-GLYCOPEPTIDES ; FETUIN-A ; GLYCOSYLATION ; IDENTIFICATION
WOS研究方向	Chemistry
语种	英语
出版者	AMER CHEMICAL SOC
WOS记录号	WOS:000398645300025
内容类型	期刊论文
源URL	[http://cas-ir.dicp.ac.cn/handle/321008/169302]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
通讯作者	Guo, Zhimou; Ye, Mingliang; Liang, Xinmiao
作者单位	1.Chinese Acad Sci, Dalian Inst Chem Phys, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Yan, Jingyu,Yu, Long,Guo, Zhimou,et al. In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge[J]. ANALYTICAL CHEMISTRY,2017,89(7):3966-3972.
APA	Yan, Jingyu.,Yu, Long.,Guo, Zhimou.,Zou, Hanfa.,Ye, Mingliang.,...&Shen, Aijin.(2017).In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge.ANALYTICAL CHEMISTRY,89(7),3966-3972.
MLA	Yan, Jingyu,et al."In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge".ANALYTICAL CHEMISTRY 89.7(2017):3966-3972.