KapScience LLC, Tewksbury, Massachusetts 01876, United States.
Anal Chem. 2020 Aug 18;92(16):11195-11203. doi: 10.1021/acs.analchem.0c01657. Epub 2020 Aug 7.
We describe a set of simple devices for surface-induced dissociation of proteins and protein complexes on three instrument platforms. All of the devices use a novel yet simple split lens geometry that is minimally invasive (requiring a few millimeters along the ion path axis) and is easier to operate than prior generations of devices. The split lens is designed to be small enough to replace the entrance lens of a Bruker FT-ICR collision cell, the dynamic range enhancement (DRE) lens of a Waters Q-IM-TOF, or the exit lens of a transfer multipole of a Thermo Scientific Extended Mass Range (EMR) Orbitrap. Despite the decrease in size and reduction in number of electrodes to 3 (from 10 to 12 in Gen 1 and ∼6 in Gen 2), we show sensitivity improvement in a variety of cases across all platforms while also maintaining SID capabilities across a wide mass and energy range. The coupling of SID, high resolution, and ion mobility is demonstrated for a variety of protein complexes of varying topologies.
我们描述了一组用于在三个仪器平台上进行蛋白质和蛋白质复合物的表面诱导解离的简单装置。所有这些装置都采用了一种新颖而简单的分裂透镜几何形状,这种形状的侵入性最小(沿离子路径轴需要几毫米),而且比前几代装置更容易操作。分裂透镜设计得足够小,可以取代布鲁克 FT-ICR 碰撞池的入口透镜、沃特世 Q-IM-TOF 的动态范围增强(DRE)透镜或热电扩展质量范围(EMR)轨道阱的转移多极的出口透镜。尽管尺寸减小,电极数量减少到 3 个(第一代有 10 到 12 个,第二代有 ∼6 个),但我们在所有平台上的各种情况下都显示出了灵敏度的提高,同时在很宽的质量和能量范围内保持了 SID 能力。各种拓扑结构的蛋白质复合物的 SID、高分辨率和离子迁移率的耦合得到了证明。