Ion Mobility-Mass Spectrometry as a Tool for the Structural Characterization of Peptides Bearing Intramolecular Disulfide Bond(s)

Abstract

Abstract. 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.

Effective Temperature and Structural Rearrangement in Trapped Ion Mobility Spectrometry

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Comprehensive Ion Mobility Calibration: Poly(ethylene oxide) Polymer Calibrants and General Strategies

“…Ion mobility spectrometry (IM) provides a fast electrophoretic separation of ions in the gas phase. The interest of analytical sciences to couple IM separation, mass spectrometry (MS; IM-MS), and conventional separation techniques (such as liquid chromatography, LC-MS) has peaked during recent years. − IM-MS coupling improves the peak capacity and raises the confidence level in the identification of compounds and in their structural elucidations.…”

A novel rapid analysis using mass spectrometry to evaluate downstream refolding of recombinant human insulin-like growth factor-1 (mecasermin)

“…Moreover, ESI‐IMS‐MS can analyze and quantify a mixture of proteoforms by increasing and decreasing the abundance of each protoform during folding or unfolding . The recent studies show that the different proteoforms originating from different disulfide bond(s) can be separated by ESI‐IMS‐MS …”