期刊
INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH
卷 52, 期 23, 页码 7729-7736出版社
AMER CHEMICAL SOC
DOI: 10.1021/ie4003377
关键词
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资金
- Natural Science Foundation of Zhejiang Province, China [LY12B06003]
- Science and Technology Program of Shaoxing [2011A21056]
Immobilized metal affinity chromatography (IMAC) is a widely employed method for the enrichment of phosphopeptides from complex proteolytic digests prior to mass spectrometric analysis. In this work, a novel IMAC material, zirconium-phosphate (Zr4+-PO3)-modified magnetic Fe3O4/GMA-co-EDMA (core/shell) (Zr4+-Fe3O4@polymer) microspheres, has been synthesized in a facile manner and used for the selective capture of phosphopeptides from protein tryptic digests for mass spectrometry analysis. The enrichment conditions were optimized using a protein digest solution of beta-casein. By virtue of a thick and biocompatible poly(GMA-co-EDMA) shell, high tolerance of contaminants (salt, nonphosphopeptide) was demonstrated for the use of Zr4+-Fe3O4@polymer microspheres for the highly selective enrichment of phosphopeptides from a protein tryptic solution that contained a high concentration of NaCl (6.2 M) or urea (8,M) and a high ratio of nonphosphoprotein (BSA) to phosphoprotein (alpha-casein) (1:500). The performance of the Zr4+-Fe3O4@polymer microspheres was further successfully examined by the phosphoproteome analysis of mouse liver lysate.
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