• Mass Spectrometry Letters
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• v.7 no.4
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• pp.96-101
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• 2016

To determine the influence of the cationization agent on the collision activated dissociation (CAD) fragmentation behavior of oligosaccharides, the CAD spectra of the singly protonated, sodiated oligosaccharides and singly sodiated and dibenzo-18-crown-6 ether conjugated oligosaccharides were carefully compared. Each of these three different species showed quite different fragmentation spectra. The comparison of singly protonated and sodiated oligosaccharide CAD spectra revealed that different cationization agents affected the cationization agent adduction sites as well as the fragmentation sites within the oligosaccharides. When the mobility of $Na^+$ was limited by the dibenzo-18-crown-6 ether encapsulation agent, the examined linear oligosaccharides showed fragmentation patterns quite different from the unmodified ones. For the dibenzo-18-crown-6 ether conjugated oligosaccharides, the charge-remote fragmentation pathways were more likely to be activated than the chargedirected pathways. This work demonstrates that dibenzo-18-crown-6 ether conjugation can potentially provide a route to selectively activate the charge-remote fragmentation pathways, albeit to a limited extent, in tandem mass spectrometry studies.

• Mass Spectrometry Letters
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• v.12 no.4
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• pp.131-136
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• 2021

Collision-induced dissociation of peptides involves a series of proton-transfer reactions in the activated peptide. To describe the kinetics of energy-variable dissociation, we considered the heat capacity of the peptide and the Marcus-theory-type proton-transfer rate. The peptide ion was activated to the high internal energy states by collision with a target gas in the collision cell. The mobile proton in the activated peptide then migrated from the most stable site to the amide oxygen and subsequently to the amide nitrogen (N-protonated) of the peptide bond to be broken. The N-protonated intermediate proceeded to the product-like complex that dissociated to products. Previous studies have suggested that the proton-transfer equilibria in the activated peptide affect the dissociation kinetics. To take the extent of collisional activation into account, we assumed a soft-sphere collision model, where the relative collision energy was fully available to the internal excitation of a collision complex. In addition, we employed a Marcus-theory-type rate equation to account for the proton-transfer equilibria. Herein, we present results from the integrated thermochemical approach using a tryptic peptide of ubiquitin.

• Bulletin of the Korean Chemical Society
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• v.26 no.5
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• pp.740-746
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• 2005

In this article, we report the tandem mass spectrometry investigations for the electron capture efficiencies of the protons belonging to the different locations (generations) in a poly(propylene imine) dendrimer with three layers of a repeat unit (named as the third generation dendrimer). The employed tandem mass spectrometry methods include SORI-CAD (sustained off-resonance irradiation collisional activation dissociation) and ECD(electron capture dissociation) mass spectrometry. We obtained SORI-CAD spectra for the dendrimer ions in the different charge states, ranging from 2+ to 4+. The analysis of fragmentation sites provides the information as to where the protons are distributed among various generations of the dendrimer. Based upon this, a new strategy to study the electron capture efficiencies of the protons is utilized to examine a new type of triplycharged ions by SORI-CAD, i.e., the 3+ ions generated from the charge reduction of the native 4+ ions by ECD: (M+4H)$^{4+}\;+\;e^-\;{\rightarrow}$ (M+4H)$^{3+\bullet}$ ${\rightarrow}\;({H^{\bullet}}_{ejected}$) + (M+3H)$^{3+}\;\rightarrow$ CAD. Interestingly, comparison of these four SORICAD spectra indicates that the proton distribution in the charge-reduced 3+ ions is very close to that in the native 4+ ions. It further suggests that in this synthetic polymer ($\sim$1.7 kDa) with an artificial architecture, the electron capture efficiencies of the protons are actually insensitive to where they are located in the molecule. This is somewhat contradictory to common expectations that the protons in the inner generations may not be well exposed to the incoming electron irradiation as much as the outer ones are, thus may be less efficient for electron capture. This finding may carry some implications for the case of medium sized peptide ions with similar masses, which are known to show no obvious site-specific fragmentations in ECD MS.