2024/04/15 by Richard J. Bell, David S. Hage, Eric D. Dodds · 1 voice
Chemistry · #Mass Spectrometry Techniques and Applications #Advanced Proteomics Techniques and Applications #Analytical Chemistry and Chromatography
paper · doi:10.1021/acs.analchem.3c05601
openalex publication_date 2024/04/15 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/15
Two-dimensional Fourier transform ion cyclotron resonance (2D FTICR) mass spectrometry is a developing form of data-independent acquisition that allows for the simultaneous fragmentation and correlation of fragment ions to their precursors across a range of m / z values. The modern usage of 2D FTICR is performed using electrospray ionization (ESI) as the dried droplet preparation for matrix-assisted laser desorption ionization (MALDI) does not produce a consistent packet of ions over a number of scans. This work uses pneumatic spray techniques from mass spectrometry imaging to create a homogeneous surface for use with MALDI as an ionization source for 2D FTICR. A mixture of peptides and matrix was deposited onto a glass slide using an HTX pneumatic sprayer. MALDI was then used to ionize the peptide mixture for use with a standard 2D FTICR pulse sequence. The generated 2D spectrum reveals comparable structural information to spectra collected in a 1D experiment. Artifacts observed in the collected 2D MALDI spectra do not significantly differ from those expected from 2D ESI spectra.