Negative Electron Transfer Dissociation Fourier Transform Mass Spectrometry of Glycosaminoglycan Carbohydrates

Abstract

Electron transfer through gas-phase ion–ion reactions has led to the widespread application of electron-based techniques once only capable in ion trapping mass spectrometers. Although any mass analyzer can, in theory, be coupled to an ion–ion reaction device (typically a 3-D ion trap), some systems of interest exceed the capabilities of most mass spectrometers. This case is particularly true in the structural characterization of glycosaminoglycan (GAG) oligosaccharides. To adequately characterize highly sulfated GAGs or oligosac charides above the tetrasaccharide level, a high-resolution mass analyzer is required. To extend previous efforts on an ion trap mass spectrometer, negative electron transfer dissociation coupled with a Fourier transform ion cyclotron resonance mass spectrometer has been applied to increasingly sulfated heparan sulfate and heparin tetrasaccharides as well as a dermatan sulfate octasaccharide. Results similar to those obtained by electron detachment dissociation are observed.

The Negative Mode Proteome with Activated Ion Negative Electron Transfer Dissociation (AI-NETD)

“…Negative mode approaches for the characterization of peptide anions offer a valuable dimension to proteomic analyses (21,24,25,66), especially as biologically relevant posttranslational modifications and other analytes that pose challenges to canonical positive mode techniques continue to emerge (7,53,(67)(68)(69)(70)(71)(72). Platforms for shotgun analysis of complex mixtures of peptide anions have been introduced, most notably using UVPD and NETD; however, these approaches have yet to provide considerable proteomic depth (fewer than ϳ800 total proteins identified in a given experiment), restricting the degree to which peptide anion characterization can benefit the proteomic community.…”

New Spectral Applications of the Fourier Transforms in Medicine, Biological and Biomedical Fields

“…When applying ECD fragmentation technique, co-and post-translational modiications within the peptide and protein sequence are maintained, as opposed to the using of those two methods, namely CID and IRMPD, which may provoke dissociation of post-translational modiications [55]. This fact is important for the application of ECD to glycosylation [56,57], sulfation [56,57], and phosphorylation analysis [56,58].…”

Electron transfer dissociation of sodium cationized polyesters: Reaction time effects and combination with collisional activation and ion mobility separation

“…Meanwhile, the extent of consecutive fragmentations, which may compromise end group determination, was negligible in ETD, but significant in CAD [4]. These features indicate that ETD could develop into a promising MS 2 method, complementary to CAD, for the determination of polyester structures [4,13], as is true for many types of biopolymers [14][15][16][17][18].…”