Laboratory of Mass Spectrometry, University of Liege, Quartier Agora, Allée du six Aout 11, B-4000, Liege, Belgium.
Commissariat à l'Energie Atomique, DRF/iBiTec-S/SIMOPRO, CE Saclay, 91191, Gif-sur-Yvette, France.
J Am Soc Mass Spectrom. 2016 Oct;27(10):1637-46. doi: 10.1007/s13361-016-1443-8. Epub 2016 Aug 3.
Disulfide bonds are post-translationnal modifications that can be crucial for the stability and the biological activities of natural peptides. Considering the importance of these disulfide bond-containing peptides, the development of new techniques in order to characterize these modifications is of great interest. For this purpose, collision cross cections (CCS) of a large data set of 118 peptides (displaying various sequences) bearing zero, one, two, or three disulfide bond(s) have been measured in this study at different charge states using ion mobility-mass spectrometry. From an experimental point of view, CCS differences (ΔCCS) between peptides bearing various numbers of disulfide bonds and peptides having no disulfide bonds have been calculated. The ΔCCS calculations have also been applied to peptides bearing two disulfide bonds but different cysteine connectivities (Cys1-Cys2/Cys3-Cys4; Cys1-Cys3/Cys2-Cys4; Cys1-Cys4/Cys2-Cys3). The effect of the replacement of a proton by a potassium adduct on a peptidic structure has also been investigated. Graphical Abstract ᅟ.
二硫键是翻译后修饰，对天然肽的稳定性和生物活性至关重要。考虑到这些含二硫键肽的重要性，开发新的技术来表征这些修饰具有重要意义。为此，本研究使用离子淌度-质谱法，在不同的电荷状态下，测量了 118 种肽（具有不同序列）的大数据集的碰撞截面（CCS），这些肽分别含有零、一、二或三个二硫键。从实验的角度来看，计算了具有不同数量二硫键的肽与不含二硫键的肽之间的 CCS 差异（ΔCCS）。还将 ΔCCS 计算应用于具有两个二硫键但不同半胱氨酸连接性（Cys1-Cys2/Cys3-Cys4；Cys1-Cys3/Cys2-Cys4；Cys1-Cys4/Cys2-Cys3）的肽。还研究了用钾加合物取代质子对肽结构的影响。图摘要。
