High-energy electron transfer dissociation (HE-ETD) using alkali metal targets for sequence analysis of post-translational peptides |
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Authors: | Shigeo Hayakawa Shinya Matsumoto Mami Hashimoto Kenichi Iwamoto Hirofumi Nagao Michisato Toyoda Yasushi Shigeri Michiko Tajiri Yoshinao Wada |
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Institution: | 1.Department of Chemistry, Graduate School of Science,Osaka Prefecture University,Osaka,Japan;2.Department of Physics, Graduate School of Science,Osaka University,Osaka,Japan;3.National Institute of Advanced Industrial Science and Technology,Osaka,Japan;4.Osaka Medical Center and Research Institute for Maternal and Child Health,Osaka,Japan |
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Abstract: | Post-translational modifications (PTMs) of proteins are important in the activation, localization, and regulation of protein
function in vivo. The usefulness of electron capture dissociation (ECD) and electron-transfer dissociation (ETD) in tandem
mass spectrometry (MS/MS) using low-energy (LE) trap type mass spectrometer is associated with no loss of a labile PTM group
regarding peptide and protein sequencing. The experimental results of high-energy (HE) collision induced dissociation (CID)
using the Xe and Cs targets and LE-ETD were compared for doubly-phosphorylated peptides TGFLT(p)EY(p)VATR (1). Although HE-CID using the Xe target did not provide information on the amino acid sequence, HE-CID using the Cs target
provided all the z-type ions without loss of the phosphate groups as a result of HE-ETD process, while LE-ETD using fluoranthene
anion gave only z-type ions from z5 to z11. The difference in the results of HE-CID between the Xe and Cs targets demonstrated that HE-ETD process with the Cs target
took place much more dominantly than collisional activation. The difference between HE-ETD using Cs targets and LE-ETD using
the anion demonstrated that mass discrimination was much weaker in the high-energy process. HE-ETD was also applied to three
other phosphopeptides YGGMHRQEX(p)VDC (2: X = S, 3: X = T, 4: X = Y). The HE-CID spectra of the doubly-protonated phosphopeptides
(= M + 2H]2+) of 2, 3, and 4 using the Cs target showed a very similar feature that the c-type ions from c7 to c11 and the z-type ions from z7 to z11 were formed via N-Cα bond cleavage without a loss of the phosphate group. |
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