High-energy Electron Transfer Dissociation (HE-ETD) Using Alkali Metal Targets for Sequence Analysis of Post-translational Peptides

Overview

Journal J Am Soc Mass Spectrom

Specialty Chemistry

Date 2010 Jul 6

PMID 20598903

Citations 3

Authors

Shigeo Hayakawa

Shinya Matsumoto

Mami Hashimoto

Kenichi Iwamoto

Hirofumi Nagao

Michisato Toyoda

Yasushi Shigeri

Michiko Tajiri

Yoshinao Wada

Affiliations

Soon will be listed here.

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 z(5) to z(11). 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 c(7) to c(11) and the z-type ions from z(7) to z(11) were formed via N-C alpha bond cleavage without a loss of the phosphate group.

Citing Articles

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