Comparison between collision induced dissociation of electrosprayed protonated peptides in the up-front source region and in a low-energy collision cell

Abstract

A systematic comparison between the up-front Collision induced dissociation (CID) mass spectra and low-energy CID tandem mass spectra from twenty-one singly and/or doubly charged peptides has been made. CID spectra of the peptides were recorded at different electrode voltages in the up-front source region of a single quadrupole instrument and different collision energies in the collision cell of a tandem quadrupole instrument. It was observed that up-front CID and low-energy CID yielded comparable product ion spectra from protonated peptides, and that the instrumental settings necessary for obtaining comparable CID mass spectra from the two methods are correlated.

Amide bond cleavage in deprotonated tripeptides: a newly discovered pathway to ″b2 ions

“…It is well known 19,20 that CID can be achieved in this region, so-called cone-voltage CID, and it has been clearly established [21][22][23] that the average energy imparted to the decomposing ions increases as the field in the interface region increases. Indeed, recent work [24][25][26][27] has shown that, by varying this field in steps, energy-resolved mass spectra [28][29][30] comparable to those obtained in variable low-energy CID in quadrupole cells can be obtained. The results of these cone-voltage CID experiments are presented in the following either as CID mass spectra at a set cone voltage or as breakdown graphs expressing the percent of total ion abundance as a function of the cone voltage, a measure of the field in the interface region.…”

In‐source collision‐induced dissociation (IS‐CID): Applications, issues and structure elucidation with single‐stage mass analyzers

“…Early work with this ionization process occurred in the 1990s. [12][13][14][15][16][17][18] With the commercialization of modern MS instrumentation, work was carried out using IS-CID for diverse types of projects. 4,19,20 DART MS with IS-CID has been used 21 for species-level identification of Datura plant seeds without complete identification of the components.…”

Use of an integrated MS – multiplexed MS/MS data acquisition strategy for high‐coverage peptide mapping studies

“…20,21 One systematic study has shown that both in-source and low-energy collision cell CID processes can generate comparable product ion spectra if proper instrumental parameters are utilized. 22 Williams and colleagues 20 showed proof of principle that a peptide map could be acquired while alternating the source region between high-and low-voltage potentials and that resulting peptide fragmentation data were of sufficient quality for peptide identification. Purvine and colleagues 21 analyzed yeast lysate using two independent LC/ion-trap MS runs, at differing source potentials, and demonstrated that precursor and product ion data could be manually aligned between the two data sets to produce SEQUES-T-based peptide identifications.…”