journal article·2020-03-01

Soft cluster-induced desorption/ionization mass spectrometry: How soft is soft?

André Portz, Karolin Bomhardt, Marcus Rohnke, Pascal Schneider, Arndt Asperger, Christoph R. Gebhardt, Michael Dürr

Biointerphases· Volume 15· Issue 2
Publisher page

Abstract

Desorption/ionization induced by neutral clusters (DINeC) is used as an ultrasoft desorption/ionization method for the analysis of fragile biomolecules by means of mass spectrometry (MS). As a test molecule, the glycopeptide vancomycin was measured with DINeC-MS, and resulting mass spectra were compared to the results obtained with electrospray ionization (ESI), matrix assisted laser desorption ionization, and time-of-flight secondary ion MS. Of the desorption-based techniques, DINeC spectra show the lowest abundance of fragments comparable to ESI spectra. The soft desorption nature of DINeC was further demonstrated when applied to MS analysis of teicoplanin.
Source: crossref · Quality: baseline

Research context

OpenAlex topics: Mass Spectrometry Techniques and Applications · Ion-surface interactions and analysis · Advanced Proteomics Techniques and Applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Institut für Angewandte Physik and Zentrum für Materialforschung, Justus-Liebig-Universität Giessen 1 , Heinrich-Buff-Ring 16, D-35392 Giessen, Germany

Institut für Physikalische Chemie and Zentrum für Materialforschung, Justus-Liebig-Universität Giessen 2 , Heinrich-Buff-Ring 17, D-35392 Giessen, Germany

Bruker Daltonik GmbH 3 , Fahrenheitstr. 4, D-28359 Bremen, Germany

Funding

HICforFAIR · Helmholtz Graduate School for Hadron and Ion Research · Bundesministerium für Bildung und Forschung

References (22)

Show source-provided references
1. Science · 2006 · 312 · 21210.1126/science.1124619 ↗
2. Annu. Rev. Anal. Chem. · 2019 · 12 · 20110.1146/annurev-anchem-061318-115516 ↗
3. Appl. Surf. Sci. · 2008 · 255 · 114810.1016/j.apsusc.2008.05.032 ↗
4. Rapid Commun. Mass Spectrom. · 2009 · 23 · 64810.1002/rcm.3922 ↗
5. Anal. Chem. · 2016 · 88 · 359210.1021/acs.analchem.5b04133 ↗
6. Fresenius J. Anal. Chem. · 1994 · 348 · 78310.1007/BF01780979 ↗
7. Science · 1998 · 281 · 26010.1126/science.281.5374.260 ↗
8. Angew. Chem. Int. Ed. · 2009 · 48 · 416210.1002/anie.200804431 ↗
9. Rapid Commun. Mass Spectrom. · 2014 · 28 · 29010.1002/rcm.6781 ↗
10. J. Chem. Phys. · 2017 · 146 · 13470510.1063/1.4979488 ↗
11. J. Chem. Phys. · 2019 · 150 · 21430110.1063/1.5095512 ↗
12. Appl. Phys. Lett. · 2011 · 99 · 23410310.1063/1.3664348 ↗
13. Biointerphases · 2016 · 11 · 02A31610.1116/1.4940705 ↗
14. Anal. Chem. · 2018 · 90 · 332810.1021/acs.analchem.7b04876 ↗
15. Biointerphases · 2018 · 13 · 03B40510.1116/1.5013151 ↗
16. ACS Omega · 2019 · 4 · 2242610.1021/acsomega.9b03060 ↗
17. Anal. Chem. · 2003 · 75 · 512410.1021/ac0345143 ↗
18. Surf. Interface Anal. · 2013 · 45 · 17110.1002/sia.5122 ↗
19. Rapid Commun. Mass Spectrom. · 2013 · 27 · 109010.1002/rcm.6550 ↗
20. Rapid Commun. Mass Spectrom. · 2013 · 27 · 263110.1002/rcm.6728 ↗
21. Biointerphases · 2018 · 13 · 03B40110.1116/1.5016186 ↗
22. J. Am. Soc. Mass. Spectrom. · 1996 · 7 · 122710.1016/S1044-0305(96)00104-3 ↗