DICP OpenIR
学科主题物理化学
CD bonded stationary phase in phosphopeptide fractionation and enrichment
Zhao YY(赵艳艳); Li XL(李秀玲); Yan JY(闫竟宇); Liang XM(梁鑫淼); Zhang YK(张玉奎)
会议名称24th International Symposium on Microscale Bioseparations
会议日期2009-10-18
2009-10-18
会议地点中国
其他题名环糊精键合固定相在磷酸化肽分段和富集的应用
页码277/1
部门归属十八室
主办者中国科学院大连化物所
英文摘要eversible protein phosphorylation regulates many significant cellular processes. Identification of the phosphorylation sites is vital to elucidate their biofunctions. To aid in phosphoproteome characterization, selective enrichent method, such as IMAC and TiO2, have been developed. However,high pH elution step is always used, which may degrade phosphopeptides. Furthermore, multiphosphopeptides bind strongly on TiO2 and are difficult to elute. More selective enrichment methods should be developed for phosphopeptide separation. Click CD stationary phase was synthesized and used to fractionate and enrich phosphopeptides in HILIC mode. Both fractionation and solid phase extraction (SPE) were carried out for separating phopshopeptides from tryptic α-casein. In fractionation, phosphopeptides are separated according to polarity, which is different from that with SCX or SAX. Phosphopeptides with same charge could be well resolved with the method. In SPE, CD stationary phase has similar selectivity to that with commercial TiO2. Furthermore, multiphosphopeptides could be well enriched and easily eluted from CD stationary phase, which are often unable to detect with TiO2. It is worthy of note that the whole enrichment process was carried out under low PH, which could avoid degradation of phosphopeptides. We demonstrate that the CD stationary phase be complementary to conventional method in phosphopeptide fractionation and enrichment.
语种中文
文献类型会议论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/113886
专题中国科学院大连化学物理研究所
通讯作者Li XL(李秀玲); Liang XM(梁鑫淼)
推荐引用方式
GB/T 7714
Zhao YY,Li XL,Yan JY,et al. CD bonded stationary phase in phosphopeptide fractionation and enrichment[C],2009:277/1.
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