Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS

被引:62
作者
Chang, Sarah Y. [1 ]
Zheng, Nan-Yan
Chen, Chee-Shan
Chen, Cheng-Dah
Chen, Ying-Yi
Wang, C. R. Cris
机构
[1] Tunghai Univ, Dept Chem, Taichung 407, Taiwan
[2] Chaoyang Univ Technol, Dept Appl Chem, Taichung, Taiwan
[3] Natl Chung Cheng Univ, Dept Chem & Biochem, Chiayi, Taiwan
关键词
D O I
10.1016/j.jasms.2007.01.011
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Iron oxide nanoparticles modified with oleate have been employed for the extraction of peptides and proteins from aqueous solution before matrix-assisted laser desorption/ionization (MALDI) mass spectrometric (MS) analysis. Adsorption of peptides and proteins onto the nanoparticles were mainly through electrostatic attraction and hydrophobic interaction. The analyte-adsorbed iron oxide nanoparticles could be efficiently collected from solution using a magnet. No elution step was needed. With this preconcentration strategy, the lowest detectable concentration of angiotensin I, insulin, and myoglobin in 500 mu l, of aqueous solution were 0.1 nM, 0.1 nM, and 10.0 nM, respectively. In addition, the nanoparticles could extract the analytes from solution with a high content of salt and surfactant, thus eliminating suppression effect during MALDI MS analysis. This method was successfully applied to concentrate the tryptic digest products of cytochrome c. In addition, the tryptic digestion of cytochrome c can be directly conducted on the iron oxide nanoparticles.
引用
收藏
页码:910 / 918
页数:9
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