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Imaging of Biological Tissues by Desorption Electrospray Ionization Mass Spectrometry
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Desorption Electrospray Ionization (DESI) Analysis of Tryptic Digests/Peptides
CSH Protocols
|March 2, 2011
Summary
Desorption electrospray ionization (DESI) offers a high-throughput method for qualitative proteomics, analyzing tryptic peptides similarly to MALDI and ESI. This technique shows promise for broad applications in mass spectrometry.
Area of Science:
- Analytical Chemistry
- Mass Spectrometry
- Proteomics
Background:
- Desorption electrospray ionization (DESI) is a surface analysis technique with potential for proteomics.
- Existing work on DESI for proteomics is limited, necessitating further investigation into its applications.
Purpose of the Study:
- To present general procedures for DESI-mass spectrometry (DESI-MS) analysis of tryptic digests/peptides.
- To highlight the potential of DESI as a high-throughput qualitative proteomics tool.
Main Methods:
- Analysis of tryptic peptides using DESI-mass spectrometry.
- Direct spotting of peptide mixtures onto an insulating surface followed by analysis without matrix compounds.
- Comparison of spectral characteristics with traditional electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) methods.
Main Results:
- DESI can be automated for high-throughput applications, including analysis of chromatographic fractions.
- Spectral characteristics of DESI are similar to ESI, detecting both singly and multiply charged ions.
- Spectra show a high prevalence of multiply charged peptide ions, characteristic of tryptic digests.
Conclusions:
- DESI-mass spectrometry is a promising emerging technique for qualitative proteomics.
- The presented protocol provides a foundation for current DESI-MS applications in peptide analysis.
- Optimal parameters for DESI-MS may vary depending on specific research applications.
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