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学科主题: 分析化学
题名: Effect of alkyl chain length on reversed phase stationary phase for separation of integral membrane protein digests
作者: Zhao Q(赵群) ;  Sun LL(孙良亮) ;  Wu Q(吴琪) ;  Liang Z(梁振) ;  Zhang LH(张丽华) ;  Zhang YK(张玉奎)
会议文集: 26th International Symposium on Microscale Bioseparations
会议名称: 26th International Symposium on Microscale Bioseparations
会议日期: 2011-5-1
出版日期: 2011
会议地点: 圣地亚哥
通讯作者: 张丽华
出版者: 待补充
出版地: 待补充
合作性质: 墙报
部门归属: 1810
主办者: CASSS
摘要: Integral membrane proteins (IMPs) play a critical role in regulating various cellular processes, including intercellular communication, vesicle trafficking, ion transport, protein translocation/integration, and the propagation of signaling cascades. However, the IMP analysis presents great challenge due to the hydrophobic nature. Recently, much attention has been paid to the solubilization of IMPs by chaotropes, detergents, organic solvents, and organic acid. Besides, the separation of hydrophobic peptide also has significant impact on the identification of IMPs. However, the in-depth study on this aspect has rarely been reported. In our recent work, membrane proteins from rat hippocampus were first solubilized by ionic liquids based protocol [1]. Then, to decrease the complexity of membrane protein digests, the prefractionation of peptides was performed during desalting. Finally, the effect of alkyl chain length of stationary phase on the separation of IMP digests was studied by μRPLC-ESI-MS/MS. In duplicate runs, in total, 536 and 703 peptides, corresponding to 301 and 398 proteins (FDR <5% at peptide level), were identified with protein digests separated by C18 and C8, respectively. For hydrophobic peptides and IMPs, the identified number obtained by C8 column was improved by 29.3% and 20.3%, respectively, compared with that obtained with C18 stationary phase. All these results indicate that C8 reverse-phase stationary phase is preferred for the large scale membrane proteome study
英文摘要: Integral membrane proteins (IMPs) play a critical role in regulating various cellular processes, including intercellular communication, vesicle trafficking, ion transport, protein translocation/integration, and the propagation of signaling cascades. However, the IMP analysis presents great challenge due to the hydrophobic nature. Recently, much attention has been paid to the solubilization of IMPs by chaotropes, detergents, organic solvents, and organic acid. Besides, the separation of hydrophobic peptide also has significant impact on the identification of IMPs. However, the in-depth study on this aspect has rarely been reported. In our recent work, membrane proteins from rat hippocampus were first solubilized by ionic liquids based protocol [1]. Then, to decrease the complexity of membrane protein digests, the prefractionation of peptides was performed during desalting. Finally, the effect of alkyl chain length of stationary phase on the separation of IMP digests was studied by μRPLC-ESI-MS/MS. In duplicate runs, in total, 536 and 703 peptides, corresponding to 301 and 398 proteins (FDR <5% at peptide level), were identified with protein digests separated by C18 and C8, respectively. For hydrophobic peptides and IMPs, the identified number obtained by C8 column was improved by 29.3% and 20.3%, respectively, compared with that obtained with C18 stationary phase. All these results indicate that C8 reverse-phase stationary phase is preferred for the large scale membrane proteome study
语种: 英语
内容类型: 会议论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/116024
Appears in Collections:中国科学院大连化学物理研究所_会议论文

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Recommended Citation:
Zhao Q,Sun LL,Wu Q,et al. Effect of alkyl chain length on reversed phase stationary phase for separation of integral membrane protein digests[C]. 见:26th International Symposium on Microscale Bioseparations. 圣地亚哥. 2011-5-1.
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