Can Two-Dimensional IR-ECD Mass Spectrometry Improve Peptide de Novo Sequencing?
Fiche publication
Date publication
mars 2018
Journal
Analytical chemistry
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DELSUC Marc-André
Tous les auteurs :
van Agthoven MA, Lynch AM, Morgan TE, Wootton CA, Lam YPY, Chiron L, Barrow MP, Delsuc MA, O'Connor PB
Lien Pubmed
Résumé
Two-dimensional mass spectrometry (2D MS) correlates precursor and fragment ions without ion isolation in a Fourier transform ion cyclotron resonance mass spectrometer (FTICR MS) for tandem mass spectrometry. Infrared activated electron capture dissociation (IR-ECD), using a hollow cathode configuration, generally yields more information for peptide sequencing in tandem mass spectrometry than ECD (electron capture dissociation) alone. The effects of the fragmentation zone on the 2D mass spectrum are investigated as well as the structural information that can be derived from it. The enhanced structural information gathered from the 2D mass spectrum is discussed in terms of how de novo peptide sequencing can be performed with increased confidence. 2D IR-ECD MS is shown to sequence peptides, to distinguish between leucine and isoleucine residues through the production of w ions as well as between C-terminal ( b/ c) and N-terminal ( y/ z) fragments through the use of higher harmonics, and to assign and locate peptide modifications.
Référence
Anal. Chem.. 2018 Mar 6;90(5):3496-3504