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Automated Sample Multiplexing by using Combined Precursor Isotopic Labeling and Isobaric Tagging (cPILOT)
Published on: December 18, 2020
Non-specific, on-probe cleanup methods for MALDI-MS samples
Yingda Xu1, Merlin L Bruening, J Throck Watson
1Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA.
Abstract:
High concentrations of contaminants such as salts and surfactants are often present in biological samples to solubilize or stabilize analytes such as proteins. Unfortunately, the presence of those contaminants often precludes direct analysis by MALDI-MS. Selective adsorption of analytes directly on modified MALDI probes, followed by rinsing to remove contaminants, overcomes this problem. This review focuses on various modifications of MALDI probes to allow the adsorption of proteins and DNA, even in a large excess of salt or surfactant. Interfaces deposited on the MALDI probes to adsorb analytes include films of commercial polymers, thin layers of matrix crystals, self-assembled monolayers, and ultrathin polymer films. Hydrophobic and ionic interactions both effect analyte adsorption on those interfaces, and patterned interfaces allow the concentration and purification of analyte molecules.
Insights
Modified MALDI probes selectively adsorb proteins and DNA from biological samples, removing salts and surfactants for direct analysis. This purification method enhances mass spectrometry accuracy.
Area of Science:
- Analytical Chemistry
- Biochemistry
- Materials Science
Background:
- Biological samples often contain high salt and surfactant concentrations that interfere with direct analysis by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry (MALDI-MS).
- These contaminants can inhibit or prevent the ionization and detection of target analytes like proteins and DNA.
Purpose of the Study:
- To review modifications of MALDI probes for selective analyte adsorption.
- To enable direct analysis of proteins and DNA from complex biological matrices by overcoming contaminant interference.
Main Methods:
- Utilizing MALDI probes modified with various interfaces, including polymer films, matrix crystal layers, self-assembled monolayers, and ultrathin polymer films.
- Investigating the adsorption of proteins and DNA onto these modified interfaces.
- Employing rinsing steps to remove interfering salts and surfactants.
Main Results:
- Modified MALDI probes effectively adsorb proteins and DNA, even in the presence of high salt or surfactant concentrations.
- Hydrophobic and ionic interactions play crucial roles in analyte adsorption onto the modified interfaces.
- Patterned interfaces demonstrate potential for concentrating and purifying analyte molecules.
Conclusions:
- Selective adsorption onto modified MALDI probes is a viable strategy to overcome contaminant interference in MALDI-MS analysis of biological samples.
- Tailored interfaces on MALDI probes can facilitate the purification and concentration of biomolecules like proteins and DNA.
- This approach broadens the applicability of MALDI-MS for complex biological sample analysis.
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