Free Radical-Initiated Peptide Sequencing Mass Spectrometry for Phosphopeptide Post-translational Modification Analysis.
Free radical–initiated peptide sequencing (FRIPS)
Phosphopeptides
Phosphorylation
Post-translational modifications (PTMs)
Radical-driven tandem mass spectrometry
Journal
Journal of the American Society for Mass Spectrometry
ISSN: 1879-1123
Titre abrégé: J Am Soc Mass Spectrom
Pays: United States
ID NLM: 9010412
Informations de publication
Date de publication:
Mar 2019
Mar 2019
Historique:
received:
18
07
2018
accepted:
23
10
2018
revised:
23
10
2018
pubmed:
11
11
2018
medline:
25
6
2019
entrez:
11
11
2018
Statut:
ppublish
Résumé
Free radical-initiated peptide sequencing mass spectrometry (FRIPS MS) was employed to analyze a number of representative singly or doubly protonated phosphopeptides (phosphoserine and phosphotyrosine peptides) in positive ion mode. In contrast to collision-activated dissociation (CAD) results, a loss of a phosphate group occurred to a limited degree for both phosphoserine and phosphotyrosine peptides, and thus, localization of a phosphorylated site was readily achieved. Considering that FRIPS MS supplies a substantial amount of collisional energy to peptides, this result was quite unexpected because a labile phosphate group was conserved. Analysis of the resulting peptide fragments revealed the extensive production of a-, c-, x-, and z-type fragments (with some minor b- and y-type fragments), suggesting that radical-driven peptide fragmentation was the primary mechanism involved in the FRIPS MS of phosphopeptides. Results of this study clearly indicate that FRIPS MS is a promising tool for the characterization of post-translational modifications such as phosphorylation. Graphical Abstract.
Identifiants
pubmed: 30414067
doi: 10.1007/s13361-018-2100-1
pii: 10.1007/s13361-018-2100-1
doi:
Substances chimiques
Cyclic N-Oxides
0
Free Radicals
0
Peptide Fragments
0
Phosphopeptides
0
Protons
0
Phosphoserine
17885-08-4
Phosphotyrosine
21820-51-9
TEMPO
VQN7359ICQ
Types de publication
Comparative Study
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
538-547Subventions
Organisme : National Research Foundation of Korea
ID : NRF-2015R1D1A1A01056782 and 2018R1A6A1A03024940
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