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Updated: Jan 22, 2026

Whole-body Mass Spectrometry Imaging by Infrared Matrix-assisted Laser Desorption Electrospray Ionization IR-MALDESI
Published on: March 24, 2016
Deep Ultraviolet Laser Ablation Electrospray Ion Mobility Mass Spectrometry.
Kelcey B Hines1, Neda Feizi2, Touradj Solouki2
1Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803, United States.
Laser ablation electrospray postionization (LA-ESI) coupled with ion mobility mass spectrometry (IM-MS) successfully ionized peptides and proteins from solid samples. This method produced intact multiply charged ions comparable to direct electrospray ionization (ESI).
Area of Science:
- Analytical Chemistry
- Biochemistry
- Spectrometry
Background:
- Direct electrospray ionization (ESI) is a common technique for analyzing biomolecules.
- Solid-state sample presentation offers potential advantages for certain analyses.
- Developing novel ionization methods is crucial for advancing mass spectrometry.
Purpose of the Study:
- To investigate laser ablation electrospray postionization (LA-ESI) for peptide and protein analysis using ion mobility mass spectrometry (IM-MS).
- To assess the efficiency and stability of LA-ESI for biomolecules.
- To compare LA-ESI results with direct ESI.
Main Methods:
- Solid-state deep ultraviolet (DUV) optical parametric oscillator (OPO) at 206 nm was used for laser ablation.
- Peptide and protein standards were deposited as dry films on quartz slides.
- Ablated material was merged with an electrospray plume for ionization before IM-MS analysis.
Main Results:
- Laser ablation electrospray postionization yielded intact multiply charged peptide and protein ions, similar to direct ESI.
- No significant fragmentation of biomolecules was observed during LA-ESI.
- Ion mobility drift times for proteins analyzed via LA-ESI were indistinguishable from those obtained by direct ESI.
- Ionization efficiency was estimated at ~1%, with observed signal instability.
Conclusions:
- LA-ESI is a viable method for ionizing peptides and proteins from solid samples without fragmentation.
- The technique produces comparable mass spectra and ion mobility data to direct ESI.
- Further optimization is needed to improve signal stability for routine applications.
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