Subject Area物理化学
Sample Preparation in Phosphoproteome Analysis
Zou HF(邹汉法); Ye ML(叶明亮)
Conference NameThe 13rd Asia Chemical Congress
Conference Date2009-9-14
Conference Place中国
Funding OrganizationThe Federation of Asian Chemical Societies
AbstractThe elucidation of protein post-translational modifications, such as phosphorylation, remains a challenging analytical task of proteomic studies. Since many of the proteins targeted for phosphorylation are low in abundance and phosphorylation is typically sub-stochiometric, a prerequisite for their identification is the specific enrichment of phosphopeptide prior to mass spectrometric analysis. A new type of the immobilized metal ion affinity chromatography (IMAC) through the chelating interaction between phosphate groups on the polymer and Zr4+ and Ti4+ (Zr4+-and Ti4+-IMAC) has been developed for enriching phosphopeptides1,2. We also compared Zr4+- and Ti4+-IMAC to other enrichment methods including Fe3+-IMAC, TiO2 and ZrO2, and demonstrate superior selectivity and efficiency of Zr4+- and Ti4+-IMAC for the isolation and enrichment of phosphopeptides. Highly ordered mesoporous silica particles were modified with titanium phosphonate to selectively capture the phosphopeptides from complex peptide and protein mixtures3,4. The modified mesoporous silica particles were further used to enrich phosphopeptides from serum of hepatocellular carcinoma patients and healthy individuals and then analyzed with MALDI-TOFMS. The profiling of the serum phosphopeptides between the cancer patients and healthy persons was distinguishingly different, which indicated the potential ability of this technique for cancer diagnosis and biomarker discovery.
Document Type会议论文
Corresponding AuthorZou HF(邹汉法)
Recommended Citation
GB/T 7714
Zou HF,Ye ML. Sample Preparation in Phosphoproteome Analysis[C],2009:26/1.
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