Electron transfer dissociation mass spectrometry in proteomics

Abstract

Mass spectrometry has rapidly evolved to become the platform of choice for proteomic analysis. While CID remains the major fragmentation method for peptide sequencing, electron transfer dissociation (ETD) is emerging as a complementary method for characterization of peptides and post-translational modifications (PTMs). Here, we review the evolution of ETD and some of its newer applications including characterization of PTMs, non-tryptic peptides and intact proteins. We will also discuss some of the unique features of ETD such as its complementarity with CID and the use of alternating CID/ETD along with issues pertaining to analysis of ETD data. The potential of ETD for applications such as multiple reaction monitoring and proteogenomics in the future will also be discussed.

Exploring the peptide fragmentation mechanisms under atmospheric pressure photoionization using tunable VUV synchrotron radiation

“…Nevertheless this technique is not always efficient for the localization of labile post-translational modifications (PTMs) on the peptide sequence. For that purpose electron-capture dissociation (ECD) [4] and electron-transfer dissociation (ETD) [5] have proven to be helpful, even if the fragmentation yields remain low. A good compromise between CID and ETD/ECD would exhibit high fragmentation yields and the capability to retain information on labile chemical modification.…”

A Short Overview of the Components in Mass Spectrometry Instrumentation for Proteomics Analyses

“…It involves transferring an electron from a radical anion to a protonated peptide [72,73], resulting in cleavages at the N-Cα bond of the peptide backbone and preserving most of the posttranslational modifications [66]. Differently from CID, but similar to ECD, ETD creates the complementary c-and z-type ions.…”

“…The electron-transfer dissociation (ETD) is based on ion/ion chemistry [66,72,73]. It involves transferring an electron from a radical anion to a protonated peptide [72,73], resulting in cleavages at the N-Cα bond of the peptide backbone and preserving most of the posttranslational modifications [66].…”

GPU Assisted Simulation Study of Ion–Ion Reactions within Quadrupole Ion Traps

“…Furthermore, the use of DC potential to control ion-ion reaction rate in ion traps was also reported [27,28]. Although ETD has the advantage of providing complementary structure information to collision induced dissociation (CID) [29][30][31], ETD still suffers from relatively low product ion intensity and slow reaction rate [32]. To address these issues, experiments were also performed to accelerate the reaction process by optimizing ion trap operation parameters and the selection of reactant partners [32].…”