ArticleJournal of the American Society for Mass Spectrometry2013
Analysis of biomolecules by atmospheric pressure visible-wavelength MALDI-ion trap-MS in transmission geometry.
Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Commercially Available Blue Diode Laser Engraver Operating at 455 nm as an Affordable LD-REIMS Ionization Source.Analytical chemistry · 2025Article
- Direct sub-atmospheric pressure ionization mass spectrometry: Evaporation/sublimation-driven ionization is amazing, fundamentally, and practically.Journal of mass spectrometry : JMS · 2024Review
- Nanoparticle-based applications by atmospheric pressure matrix assisted desorption/ionization mass spectrometry.Nanoscale advances · 2023Review
- "Magic" Ionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Tip-enhanced laser ablation sample transfer for biomolecule mass spectrometry.Journal of the American Society for Mass Spectrometry · 2015Article
- Analysis of biomolecules by atmospheric pressure visible-wavelength MALDI-ion trap-MS in transmission geometry.Journal of the American Society for Mass Spectrometry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the development of a new AP visible-wavelength MALDI-ion trap-MS instrument with significantly improved performance over our previously reported system (Int. J. Mass Spectrom. 315, 66-73 (2012)). A Nd:YAG pulsed laser emitting light at 532 nm was used to desorb and ionize oligosaccharides and peptides in transmission geometry through a glass slide. Limits of detection (LODs) achieved in MS mode correspond to picomole quantities of oligosaccharides and femtomole quantities of peptides. Tandem MS (MS/MS) experiments enabled identification of enzymatically digested proteins and oligosaccharides by comparison of MS/MS spectra with data found in protein and glycan databases. Moreover, the softness of ionization, LODs, and fragmentation spectra of biomolecules by AP visible-wavelength MALDI-MS were compared to those obtained by AP UV MALDI-MS using a Nd:YAG laser emitting light at 355 nm. AP visible-wavelength MALDI appears to be a softer ionization technique then AP UV MALDI for the analysis of sulfated peptides, while visible-wavelength MALDI-MS, MS/MS, and MS/MS/MS spectra of other biomolecules analyzed were mostly similar to those obtained by AP UV MALDI-MS. Therefore, the methodology presented will be useful for MS and MS(n) analyses of biomolecules at atmospheric pressure. Additionally, the AP visible-wavelength MALDI developed can be readily used for soft ionization of analytes on various mass spectrometers.
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