Narrowband Modulation Two-dimensional Mass Spectrometry and Label-free Relative Quantification of Histone Peptides.
Fiche publication
Date publication
septembre 2020
Journal
Analytical chemistry
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DELSUC Marc-André
Tous les auteurs :
Halper M, Delsuc MA, Breuker K, van Agthoven MA
Lien Pubmed
Résumé
Two-dimensional mass spectrometry (2D MS) on an FT-ICR mass analyzer allows for tandem mass spectrometry without requiring ion isolation. In the ICR cell, precursor ion radii are modulated before fragmentation, which results in modulation of the abundance of their fragments. The resulting 2D mass spectrum enables correlation between precursor and fragment ions. In standard broadband 2D MS, the range of precursor ion cyclotron frequencies is determined by the lowest mass-to-charge (m/z) ratio to be fragmented in the 2D MS experiment, which leads to precursor ion m/z ranges that are much wider than necessary, thereby limiting the resolving power for precursor ions and the accuracy of the correlation between precursor and fragment ions. We present narrowband modulation 2D MS, which increases the precursor ion resolving power by reduc-ing the precursor ion m/z range, with the aim of resolving the fragment ion patterns of overlapping isotopic distributions. In this proof-of-concept study, we compare broadband and narrowband modulation 2D mass spectra of an equimolar mixture of histone peptide isoforms. In narrowband modulation 2D MS, we were able to separate the fragment ion patterns of all 13C isotopes of the different histone peptide forms. We further demonstrate the potential of narrowband 2D MS for label-free quantification of peptides.
Référence
Anal. Chem.. 2020 Sep 22;: