ArticleMass spectrometry (Tokyo, Japan)2012
Correlation between Sweet Spots of Glycopeptides and Polymorphism of the Matrix Crystal in MALDI Samples.
Article in Mass spectrometry (Tokyo, Japan), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Quantitative mass spectrometry imaging: therapeutics & biomolecules.Chemical communications (Cambridge, England) · 2024Review
- Sensitive and Structure-InformativeMass spectrometry (Tokyo, Japan) · 2017Article
- N-Glycan profile analysis of transferrin using a microfluidic compact disc and MALDI-MS.Analytical and bioanalytical chemistry · 2016Article
- Solvent separating secondary metabolites directly from biosynthetic tissue for surface-assisted laser desorption ionisation mass spectrometry.Marine drugs · 2015Article
- Salt Tolerance Enhancement of Liquid Chromatography-Matrix-Assisted Laser Desorption/Ionization-Mass Spectrometry Using Matrix Additive Methylenediphosphonic Acid.Mass spectrometry (Tokyo, Japan) · 2014Article
- Correlation between Sweet Spots of Glycopeptides and Polymorphism of the Matrix Crystal in MALDI Samples.Mass spectrometry (Tokyo, Japan) · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A standard dried-droplet preparation using 2,5-dihydroxybenzoic acid (2,5-DHBA) as the matrix results in a large variation in signal intensity and poor shot-to-shot reproducibility in matrix-assisted laser desorption/ionization (MALDI). We expected that the differences can be attributed to the nature of the crystal structures in the region of the "sweet spot" within the MALDI samples. 2,5-DHBA crystals with and without analytes on a target plate obtained by means of a dried-droplet preparation contain two polymorphs, which can be distinguished by Raman spectra. In comparing the Raman image with the MS image, a clear correlation between the signal distribution of glycopeptides and hydrophilic peptides and the specific crystal form of 2,5-DHBA could be made. The ionization of hydrophobic peptides appears to proceed in both types of polymorphic crystals. In addition, the derivatization of glycopeptides with a pyrene group enabled us to detect glycopeptides regardless the crystal form. As the result, the number of sweet spots increased and MS spectra with a high signal intensity were obtained. The results suggest that the introduction of a hydrophobic/aromatic moiety to glycopeptides results in a more successful MALDI analysis due to the effective incorporation of the analyte into matrix crystals.
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