Letter: Electron-Capture Dissociation and Collision-Induced Dissociation Fragmentation of the Supermetallized Complexes of Substance P with Potassium, Cesium and Silver

2016 ◽  
Vol 22 (2) ◽  
pp. 91-95 ◽  
Author(s):  
Yury Kostyukevich ◽  
Alexander Zherebker ◽  
Alexey Kononikhin ◽  
Maria Indeykina ◽  
Igor Popov ◽  
...  
Keyword(s):  
Substance P ◽  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Collision Induced Dissociation

scholarly journals The effect of radical trap moieties on electron capture dissociation spectra of substance P

2006 ◽  
Vol 17 (10) ◽  
pp. 1429-1436 ◽  
Author(s):  
Marina A. Belyayev ◽  
Jason J. Cournoyer ◽  
Cheng Lin ◽  
Peter B. O’Connor
Keyword(s):  
Substance P ◽  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Radical Trap

scholarly journals Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

2010 ◽  
Vol 30 (6) ◽  
pp. 433-443 ◽  
Author(s):  
Karolina Kowalewska ◽  
Piotr Stefanowicz ◽  
Tomasz Ruman ◽  
Tomasz Frączyk ◽  
Wojciech Rode ◽  
...  
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
31P Nmr ◽  
Basic Amino Acid ◽  
Collision Induced Dissociation ◽  
Spectrometric Analysis ◽  
Phosphorylation Sites ◽  
Nmr Studies ◽  
Phosphorylated Peptides ◽  
Phosphorylation Reaction

Phosphorylation of proteins is an essential signalling mechanism in eukaryotic and prokaryotic cells. Although N-phosphorylation of basic amino acid is known for its importance in biological systems, it is still poorly explored in terms of products and mechanisms. In the present study, two MS fragmentation methods, ECD (electron-capture dissociation) and CID (collision-induced dissociation), were tested as tools for analysis of N-phosphorylation of three model peptides, RKRSRAE, RKRARKE and PLSRTLSVAAKK. The peptides were phosphorylated by reaction with monopotassium phosphoramidate. The results were confirmed by 1H NMR and 31P NMR studies. The ECD method was found useful for the localization of phosphorylation sites in unstable lysine-phosphorylated peptides. Its main advantage is a significant reduction of the neutral losses related to the phosphoramidate moiety. Moreover, the results indicate that the ECD–MS may be useful for analysis of regioselectivity of the N-phosphorylation reaction. Stabilities of the obtained lysine-phosphorylated peptides under various conditions were also tested.

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