On the Preservation of Non-covalent Peptide Assemblies in a Tandem-Trapped Ion Mobility Spectrometer-Mass Spectrometer (TIMS-TIMS-MS)
On the Preservation of Non-covalent Peptide Assemblies in a Tandem-Trapped Ion Mobility Spectrometer-Mass Spectrometer (TIMS-TIMS-MS)
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DOI：
10.1007/s13361-019-02200-y
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发表时间：
2019-07-01
影响因子：
3.2
通讯作者：
Bleiholder, Christian
中科院分区：
文献类型：
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作者：
Kirk, Samuel R.;Liu, Fanny C.;Bleiholder, Christian
离子迁移谱-质谱 (IMS-MS) 已证明能够表征弱结合肽组装体的结构。然而，如果这些组件经历高能离子-中性碰撞，它们可能会在 IMS-MS 测量过程中解离。在这里，我们研究了串联捕获离子迁移谱-质谱 (TIMS-TIMS-MS) 保留弱结合肽组装体的能力。我们使用缓激肽及其组件作为参考系统评估串联 TIMS 仪器中的离子加热和解离。我们的数据表明，在精心选择的操作条件下，非共价缓激肽组装体大部分保留在 TIMS-TIMS 中。重要的是，我们观察到四电荷缓激肽四聚体，这证明了我们仪器的柔软性。
Ion mobility spectrometry-mass spectrometry (IMS-MS) has demonstrated the ability to characterize structures of weakly-bound peptide assemblies. However, these assemblies can potentially dissociate during the IMS-MS measurement if they undergo energetic ion-neutral collisions. Here, we investigate the ability of tandem-trapped ion mobility spectrometry-mass spectrometry (TIMS-TIMS-MS) to retain weakly-bound peptide assemblies. We assess ion heating and dissociaton in the tandem-TIMS instrument using bradykinin and its assemblies as reference systems. Our data indicate that non-covalent bradykinin assemblies are largely preserved in TIMS-TIMS under carefully selected operating conditions. Importantly, we observe quadruply-charged bradykinin tetramers, which attests to the softness of our instrument.