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In-Depth Analysis of Glycoprotein Sialylation in Serum Using a Dual-Functional Material with Superior Hydrophilicity and Switchable Surface Charge
Dong, Xuefang1; Qin, Hongqiang1; Mao, Jiawei1,2; Yu, Dongping1,2; Li, Xiuling1; Shen, Aijin1; Yan, Jingyu1; Yu, Long1; Guo, Zhimou1; Ye, Mingliang1; Zou, Hanfa1; Liang, Xinmiao1
Source PublicationANALYTICAL CHEMISTRY
2017-04-04
ISSN0003-2700
DOI10.1021/acs.analchem.6b04394
Volume89Issue:7Pages:3966-3972
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Analytical
WOS Research AreaChemistry
WOS KeywordTITANIUM-DIOXIDE CHROMATOGRAPHY ; MASS-SPECTROMETRY ; GLYCOPEPTIDE ENRICHMENT ; SELECTIVE ENRICHMENT ; HYDRAZIDE CHEMISTRY ; STATIONARY PHASES ; N-GLYCOPEPTIDES ; FETUIN-A ; GLYCOSYLATION ; IDENTIFICATION
AbstractSialylation 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.
Language英语
WOS IDWOS:000398645300025
PublisherAMER CHEMICAL SOC
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/169303
Collection中国科学院大连化学物理研究所
Corresponding AuthorGuo, Zhimou; Ye, Mingliang; Liang, Xinmiao
Affiliation1.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
Recommended Citation
GB/T 7714
Dong, Xuefang,Qin, Hongqiang,Mao, Jiawei,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 Dong, Xuefang.,Qin, Hongqiang.,Mao, Jiawei.,Yu, Dongping.,Li, Xiuling.,...&Liang, Xinmiao.(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 Dong, Xuefang,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.
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