Design and performance of an ESI interface for selective external ion accumulation coupled to a Fourier transform ion cyclotron mass spectrometer.
Design and performance of an ESI interface for selective external ion accumulation coupled to a Fourier transform ion cyclotron mass spectrometer.
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DOI：
10.1021/ac000633w
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发表时间：
2001-01
影响因子：
7.4
通讯作者：
M. Belov;E. N. Nikolaev;G. Anderson;H. Udseth;T. Conrads;T. Veenstra;C. Masselon;M. Gorshkov;R. D. Smith
中科院分区：
文献类型：
--
作者：
M. Belov;E. N. Nikolaev;G. Anderson;H. Udseth;T. Conrads;T. Veenstra;C. Masselon;M. Gorshkov;R. D. Smith
傅里叶变换离子回旋共振质谱（FTICR MS）与电喷雾电离的耦合促进了对大型生物聚合物的分析，并为高通量蛋白质表征（例如快速“蛋白质组”分析）提供了基础。在这项工作中，高效毛细管液相色谱与FTICR质谱和外部离子积累的结合已被证明可以提高灵敏度和分析占空比。仪器的通用性进一步提高了离子预选后的离子积累在一个外部线性四极离子阱。用3.5 t FTICR质谱仪对界面进行了测试，并用分子量在500 ~ 66000之间的多肽和蛋白质进行了评价。与之前使用的累积捕获相比，灵敏度、占空比和动态范围显著增加，对较小的蛋白质（如细胞色素c）的检测限约为10 zmol（约6000分子）。毛细管LC外部积累界面与FTICR成功应用于全蛋白质组小鼠胰蛋白酶消化的研究。
The coupling of Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) with electrospray ionization has advanced the analysis of large biopolymers and provided the basis for high-throughput protein characterization (e.g., for rapid "proteome" analyses). In this work, the combination of high-performance capillary liquid chromatography with FTICR mass spectrometry and external ion accumulation has been shown to increase both sensitivity and analysis duty cycle. Instrument versatility is further improved by ion preselection followed by ion accumulation in an external linear quadrupole ion trap. The interface was tested with a 3.5-T FTICR mass spectrometer and evaluated with a number of peptides and proteins whose molecular weights ranged from 500 to 66000. A significant increase in the sensitivity, duty cycle, and dynamic range over that of the previously used accumulated trapping was achieved, exhibiting a detection limit of approximately 10 zmol (approximately 6000 molecules) for smaller proteins such as cytochrome c. Capillary LC external accumulation interface with FTICR was successfully applied for the study of whole-proteome mouse tryptic digests.