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Whole-body Mass Spectrometry Imaging by Infrared Matrix-assisted Laser Desorption Electrospray Ionization IR-MALDESI
Published on: March 24, 2016
Infrared matrix-assisted laser desorption and ionization by using a tunable mid-infrared free-electron laser
R Cramer1, F Hillenkamp, R F Haglund
1Institut für Medizinische Physik und Biophysik, Westfälische/Wilhelms Universität, Münster, Germany.
Infrared matrix-assisted laser desorption/ionization mass spectrometry (IR-MALDI) now uses tunable lasers for protein analysis. This advancement enables IR-MALDI at new wavelengths, expanding its capabilities.
Area of Science:
- Analytical Chemistry
- Mass Spectrometry
- Spectroscopy
Background:
- Infrared matrix-assisted laser desorption/ionization (IR-MALDI) is a mass spectrometry technique.
- Conventional IR-MALDI utilizes fixed-frequency infrared lasers.
- Selective vibrational excitation is key to IR-MALDI's mechanism.
Purpose of the Study:
- To report initial results of IR-MALDI using a free-electron laser.
- To demonstrate IR-MALDI's capability with selective vibrational excitation.
- To explore IR-MALDI at wavelengths beyond conventional fixed-frequency lasers.
Main Methods:
- Utilized the Vanderbilt free-electron laser for selective vibrational excitation.
- Performed IR-MALDI mass spectrometry in the 2.8–4 µm and 5.5–6.5 µm wavelength ranges.
- Analyzed organic compounds like succinic acid, fumaric acid, and nicotinic acid as matrices.
Main Results:
- Demonstrated successful IR-MALDI of proteins using a tunable free-electron laser.
- Showed feasibility and comparable performance of IR-MALDI at new wavelengths.
- Obtained IR-MALDI mass spectra covering O-H and C=O stretch vibration absorption bands.
Conclusions:
- IR-MALDI is feasible and effective using tunable laser sources beyond conventional fixed frequencies.
- The study highlights the potential of IR-MALDI near C=O stretch vibrations.
- Tunable sources offer new avenues for studying IR-MALDI mechanisms.
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