DICP OpenIR
Cleavable hydrophobic derivatization strategy for enrichment and identification of phosphorylated lysine peptides
Hu, Yechen1,2; Li, Yang1,2; Gao, Hang1,2; Jiang, Bo1; Zhang, Xiaodan1; Li, Xiao1; Wu, Qiong1,2; Liang, Zhen1; Zhang, Lihua1; Zhang, Yukui1
Corresponding AuthorZhang, Lihua(lihuazhang@dicp.ac.cn)
KeywordPhosphorylated lysine peptides Cleavable hydrophobic derivatization N-Phosphorylation Proteomics Liquid chromatography-tandem mass spectrometry
Source PublicationANALYTICAL AND BIOANALYTICAL CHEMISTRY
2019-07-01
ISSN1618-2642
DOI10.1007/s00216-019-01770-w
Volume411Issue:18Pages:4159-4166
Funding ProjectNational Key Research and Development Program of China[2017YFA0505003] ; National Natural Science Foundation[91543201] ; National Natural Science Foundation[21505133] ; National Natural Science Foundation[21725506] ; Chinese Academy of Sciences Key Project in Frontier Science[QYZDY-SSW-SLH017] ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key[DICP TMSR201601]
Funding OrganizationNational Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS KeywordBOVINE LIVER ; 1-32P-PHOSPHOHISTIDINE 3-32P-PHOSPHOHISTIDINE ; PROTEIN ; 3-PHOSPHOHISTIDINE ; 6-PHOSPHOLYSINE
AbstractBecause of structural flexibility and acid lability, the identification of phosphorylated lysine (pLys) peptides is a great challenge. We report here a cleavable hydrophobic derivatization (CHD) strategy for the enrichment and identification of pLys peptides. First, 2,5-dioxopyrrolidin-1-yl-3-(decyldisulfanyl)propanoate was synthesized to react with dephosphorylated lysine peptides, and then the derived peptides were captured by a C-18 column, followed by cleavage of the hydrophobic chain, with the specific label left on the target peptides for further identification. By CHD, the enrichment of pLys peptides from interfering peptides (1:1000 mass ratio) was achieved. Furthermore, CHD was applied to screen the pLys targets from Escherichia coli lysates, and 39 pLys sites from 35 proteins were identified. Gene Ontology (GO) analysis showed that these proteins played vital roles in catabolism, metabolism, biogenesis, and biosynthetic processes. All these results demonstrate that CHD might pave the way for comprehensive profiling of the pLys proteome.
Language英语
Funding OrganizationNational Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; National Natural Science Foundation ; National Natural Science Foundation ; Chinese Academy of Sciences Key Project in Frontier Science ; Chinese Academy of Sciences Key Project in Frontier Science ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key ; Innovation Program of Dalian Institute of Chemical Physics, Chinese Academy of Sciences Key
WOS IDWOS:000474266400020
PublisherSPRINGER HEIDELBERG
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/175435
Collection中国科学院大连化学物理研究所
Corresponding AuthorZhang, Lihua
Affiliation1.Chinese Acad Sci, CAS Key Lab Separat Sci Analyt Chem, Natl Chromatog R&D Ctr, Dalian Inst Chem Phys, 457 Zhongshan Rd, Dalian 116023, Liaoning, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Hu, Yechen,Li, Yang,Gao, Hang,et al. Cleavable hydrophobic derivatization strategy for enrichment and identification of phosphorylated lysine peptides[J]. ANALYTICAL AND BIOANALYTICAL CHEMISTRY,2019,411(18):4159-4166.
APA Hu, Yechen.,Li, Yang.,Gao, Hang.,Jiang, Bo.,Zhang, Xiaodan.,...&Zhang, Yukui.(2019).Cleavable hydrophobic derivatization strategy for enrichment and identification of phosphorylated lysine peptides.ANALYTICAL AND BIOANALYTICAL CHEMISTRY,411(18),4159-4166.
MLA Hu, Yechen,et al."Cleavable hydrophobic derivatization strategy for enrichment and identification of phosphorylated lysine peptides".ANALYTICAL AND BIOANALYTICAL CHEMISTRY 411.18(2019):4159-4166.
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