Attomole biomolecule mass analysis by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance.
Attomole biomolecule mass analysis by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance.
复制标题
通过基质辅助激光解吸/电离傅立叶变换离子回旋共振进行阿托莫尔生物分子质量分析。
DOI：
10.1021/ac00118a017
复制
发表时间：
1995
影响因子：
7.4
通讯作者：
Marshall,AG
中科院分区：
文献类型：
--
作者：
Solouki,T;Marto,JA;White,FM;Guan,S;Marshall,AG
通过以下方式显着提高了 MALDI FT-ICR 质谱法分析生物分子的灵敏度：(i) 将显微镜监测的样品沉积到探针尖端上的小压痕上，以及 (ii) 通过单次激光发射对离子进行多次重新测量。对固体探针尖端进行简单修改，即可将几摩尔分析物微沉积到先前与激光束对齐的小压痕点上。同一离子包的离子多次重新测量增强了信噪比，从而扩展了可实现的 FT-ICR MS 检测限 我们证明 FT-ICR 可用于检测低摩尔量的肽和磷脂的母体和结构上重要的碎片离子。约 90 amol 血管紧张素 II 和缓克明混合物、约 40 amol 二棕榈酰甘油磷脂酰胆碱和约 8 amol P 物质的正离子质谱构成了迄今为止 MALDI 生成离子的 FT-ICR 质量分析报告的最低检测限。基质辅助激光解吸/电离 (MALDI)* 1 和电喷雾电离 (ESI) 2 34567891011技术彻底改变了生物分子的质量分析。 MALDI 生成的离子通常通过飞行时间仪器以相对较低的质量分辨率（m/Aw< 1000，其中 m 是离子质量，Aw 是峰最大高度的指定分数处的质谱峰宽度）以及磁扇区仪器和四极离子阱进行质量分析。 3 4
Significantly improved sensitivity for analysis of biomol-ecules by MALDI FT-ICR mass spectrometry is achieved by (i) microscope-monitored sample deposition onto a small indentation on the probe tip and (ii) multiple remeasurement of ions from a single laser shot A simple modification to the solids probe tip allows for microdepo-sition of a few amols of analyte onto small indentation spots previously aligned with the laser beam. Ion multiple remeasurement of the same ion packet enhances the signal-to-noise ratio and thus extends the achievable FT-ICR MS detection limit We demonstrate that FT-ICR can be used to detectparent and structurally significant fragment ions of peptides and phospholipids at low amol amounts. Positive ion mass spectra for~ 90 amol of a mixture of angiotensin II and bradykmin,~ 40 amol of dipalmitoylglycerophosphatidylcholine, and~ 8 amol of substance P constitute the lowest reported detection limits to date for FT-ICR mass analysis of MALDI-generated ions.Matrix-assisted laser desorption/ionization (MALDI)* 1 and electrospray ionization (ESI) 2 34567891011techniques have revolutionized mass analysis of biomolecules. MALDI-generated ions have been mass-analyzed by time-of-flight instruments typically at relatively low mass resolving power (m/Aw< 1000, in which m is the ion mass and Aw is the mass spectral peak width at a specified fraction of peak maximum height), as well as with magneticsector instruments and quadrupole ion traps. 3 4