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Atmospheric pressure MALDI/ion trap mass spectrometry.
V V Laiko1, S C Moyer, R J Cotter
1Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Analytical Chemistry
|November 18, 2000
Summary
A novel atmospheric pressure matrix-assisted laser desorption/ionization (AP MALDI) technique coupled with an ion trap mass spectrometer offers versatile ionization source selection. This method achieves sensitive peptide detection and enables structural analysis for AP MALDI-generated ions.
Area of Science:
- Analytical Chemistry
- Mass Spectrometry
- Biochemistry
Background:
- Coupling atmospheric pressure ionization sources with mass spectrometers enhances analytical capabilities.
- Matrix-assisted laser desorption/ionization (MALDI) is a widely used ionization technique.
- Ion trap mass spectrometers offer high sensitivity and structural elucidation capabilities.
Purpose of the Study:
- To develop and evaluate a novel atmospheric pressure matrix-assisted laser desorption/ionization (AP MALDI) technique.
- To integrate AP MALDI with a commercial ion trap mass spectrometer for versatile analysis.
- To demonstrate the feasibility of peptide structural analysis using AP MALDI-generated ions.
Main Methods:
- A new AP MALDI source was developed and coupled with a commercial ion trap mass spectrometer.
- The system allowed for rapid interchangeability with a commercial electrospray/APCI source.
- Detection limits were assessed using a four-component peptide mixture (800-1700 molecular weight).
Main Results:
- The AP MALDI/ion trap system achieved a detection limit of 10-50 fmol for deposited analyte.
- Peptide structural analysis was successfully performed using MS/MS and MS3 experiments on AP MALDI-generated ions.
- The system demonstrated flexibility with interchangeable atmospheric ionization sources.
Conclusions:
- The novel AP MALDI/ion trap configuration provides a sensitive and versatile platform for peptide analysis.
- This technique enables structural characterization of peptides ionized via AP MALDI.
- The ability to switch ionization sources enhances the applicability of the ion trap mass spectrometer.