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Sequential enrichment of singly- and multiply-phosphorylated peptides with zwitterionic hydrophilic interaction chromatography material
Sheng, Qianying1; Yang, Kaiya1; Xue, Xingya3; Li, Xiuling3,4; Guo, Zhimou3; Shen, Aijin3; Ke, Yanxiong5; Lan, Minbo1,2; Liang, Xinmiao
KeywordZwitterionic Material Mixed-mode Retention Mechanisms Sequential Enrichment Multiply-phosphorylated Peptides Mass Spectrometry
Source PublicationJOURNAL OF CHROMATOGRAPHY A
2015-09-25
DOI10.1016/j.chroma.2015.08.018
Volume1413Pages:47-59
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS KeywordSOLID-PHASE EXTRACTION ; INTERACTION LIQUID-CHROMATOGRAPHY ; PHOSPHOPROTEOME ANALYSIS ; MASS-SPECTROMETRY ; EXCHANGE CHROMATOGRAPHY ; ION-EXCHANGE ; IN-VIVO ; SEPARATION ; PHOSPHOPEPTIDES ; COMBINATION
AbstractAn interesting and novel method for the selective and sequential enrichment of singly- and multiply-phosphorylated peptides with a zwitterionic material "Click TE-Cys" is presented. Retention mechanisms between phosphopeptides and Click TE-Cys are systematically investigated by checking the influence of acetonitrile content, pH value, and buffer concentration on the retention of phosphopeptides. Both hydrophilic interaction and electrostatic interaction are involved in retention between phosphopeptides and Click TE-Cys. Based on these results, an optimized method is established for selective enrichment of phosphopeptides using Click TE-Cys. This method not only exhibits high selectivity for phosphopeptides, but also fractionates singly- and multiply-phosphorylated peptides into two fractions. This method was evaluated using relatively complex samples, including peptide mixtures of alpha-casein and bovine serum albumin (BSA) at a molar ratio of 1:10 and skim milk. This efficient and optimized protocol has great potential for enriching multiply-phosphorylated peptides and could be a valuable tool for specific enrichment of phosphopeptides in phosphoproteome analysis. (C) 2015 Elsevier B.V. All rights reserved.
Language英语
WOS IDWOS:000361577600005
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/146558
Collection中国科学院大连化学物理研究所
Affiliation1.E China Univ Sci & Technol, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China
2.E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China
3.Chinese Acad Sci, Dalian Inst Chem Phys, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
4.Nantong Univ, Coinnovat Ctr Neuroregenerat, Nantong 226019, Peoples R China
5.E China Univ Sci & Technol, Engn Res Ctr Pharmaceut Proc Chem, Shanghai 200237, Peoples R China
Recommended Citation
GB/T 7714
Sheng, Qianying,Yang, Kaiya,Xue, Xingya,et al. Sequential enrichment of singly- and multiply-phosphorylated peptides with zwitterionic hydrophilic interaction chromatography material[J]. JOURNAL OF CHROMATOGRAPHY A,2015,1413:47-59.
APA Sheng, Qianying.,Yang, Kaiya.,Xue, Xingya.,Li, Xiuling.,Guo, Zhimou.,...&Liang, Xinmiao.(2015).Sequential enrichment of singly- and multiply-phosphorylated peptides with zwitterionic hydrophilic interaction chromatography material.JOURNAL OF CHROMATOGRAPHY A,1413,47-59.
MLA Sheng, Qianying,et al."Sequential enrichment of singly- and multiply-phosphorylated peptides with zwitterionic hydrophilic interaction chromatography material".JOURNAL OF CHROMATOGRAPHY A 1413(2015):47-59.
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