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题名: Enrichment of phosphopeptides by Fe3+-immobilized mesoporous nanoparticles of MCM-41 for MALDI and nano-LC-MS/MS analysis
作者: Pan, Chensong;  Ye, Mingliang;  Liu, Yuge;  Feng, Shun;  Jiang, Xiaogang;  Han, Guanghui;  Zhu, Junjie;  Zou, Hanfa
通讯作者: 邹汉法
关键词: phosphopeptides ;  MALDI ;  Fe3+-immobilized MCM-41 ;  nano-LC-MS/MS ;  enrichment
刊名: JOURNAL OF PROTEOME RESEARCH
发表日期: 2006-11-03
DOI: 10.1021/pr0600125
卷: 5, 期:11, 页:3114-3124
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1809
产权排名: 1;1
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biochemical Research Methods
研究领域[WOS]: Biochemistry & Molecular Biology
英文摘要: Fe3+-immobilized mesoporous molecular sieves MCM-41 with particle size of ca. 600 nm and pore size of ca. 3 nm is synthesized and applied to selectively trap and separate phosphopeptides from tryptic digest of proteins. For the capture of phosphopeptides, typically 10 mu L of tryptic digest solution was first diluted to 1 mL by solution of ACN/0.1% TFA (50:50, v/v) and incubated with 10 mu L of 0.1% acetic acid dispersed Fe3+-immobilized MCM-41 for 1 h under vibration. Fe3+-immobilized MCM-41 with trapped phosphopeptides was separated by centrifugation. The deposition was first washed with a volume of 300 mu L of solution containing 100 mM NaCl in ACN/0.1% TFA (50:50, v/v) and followed by a volume of 300 mu L of solution of 0.1% acetic acid to remove nonspecifically bound peptides. The nanoparticles with trapped phosphopeptides are mixed with 2,5-dihydroxybenzoic acid (2,5-DHB) and deposited onto the target for analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). It was found that phosphopeptides from tryptic digest of alpha-casein and beta-casein are effectively and specifically trapped on Fe3+-immobilized MCM-41 with few peptides nonspecifically adsorbed. After the extraction by Fe3+-immobilized MCM-41, the suppression to the detection of phosphopeptides caused by abundant nonphosphopeptides from tryptic digest is effectively eliminated, and the detection of phosphopeptides by MALDI is greatly enhanced with the value of signal-to-noise (S/N) increased by more than an order of magnitude. It is demonstrated that the mechanism of the adsorption of phosphopeptides on Fe3+-immobilized MCM-41 is based on the interaction between the Fe3+ and the phosphate group. Finally, Fe3+-immobilized MCM-41 is applied to extract phosphopeptides from tryptic digest of the lysate of mouse liver for phosphoproteome analysis by nano-LC-MS/MS.
关键词[WOS]: FLIGHT-MASS-SPECTROMETRY ;  ION AFFINITY-CHROMATOGRAPHY ;  PROTEIN-PHOSPHORYLATION ;  MOLECULAR-SIEVES ;  PHOSPHOPROTEOME ANALYSIS ;  MS ANALYSIS ;  ADSORPTION ;  SITES ;  TIME ;  IDENTIFICATION
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000241755400025
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/97477
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Dalian 116023, Peoples R China
2.Nanjing Univ, Dept Chem, Nanjing 210093, Peoples R China

Recommended Citation:
Pan, Chensong,Ye, Mingliang,Liu, Yuge,et al. Enrichment of phosphopeptides by Fe3+-immobilized mesoporous nanoparticles of MCM-41 for MALDI and nano-LC-MS/MS analysis[J]. JOURNAL OF PROTEOME RESEARCH,2006,5(11):3114-3124.
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