Habeck, Tanja ; Maciel, Edvaldo Vasconcelos Soares ; Kretschmer, Kevin ; Lermyte, Frederik (2024)
Charge site manipulation to enhance top‐down fragmentation efficiency.
In: Proteomics : Proteomics and Systems Biology, 2024, 24 (3-4)
doi: 10.26083/tuprints-00027109
Artikel, Zweitveröffentlichung, Verlagsversion
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Kurzbeschreibung (Abstract)
In recent years, top‐down mass spectrometry has become a widely used approach to study proteoforms; however, improving sequence coverage remains an important goal. Here, two different proteins, α‐synuclein and bovine carbonic anhydrase, were subjected to top‐down collision‐induced dissociation (CID) after electrospray ionisation. Two high‐boiling solvents, DMSO and propylene carbonate, were added to the protein solution in low concentration (2%) and the effects on the top‐down fragmentation patterns of the proteins were systematically investigated. Each sample was measured in triplicate, which revealed highly reproducible differences in the top‐down CID fragmentation patterns in the presence of a solution additive, even if the same precursor charge state was isolated in the quadrupole of the instrument. Further investigation supports the solution condition‐dependent selective formation of different protonation site isomers as the underlying cause of these differences. Higher sequence coverage was often observed in the presence of additives, and the benefits of this approach became even more evident when datasets from different solution conditions were combined, as increases up to 35% in cleavage coverage were obtained. Overall, this approach therefore represents a promising opportunity to increase top‐down fragmentation efficiency.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2024 |
| Autor(en): | Habeck, Tanja ; Maciel, Edvaldo Vasconcelos Soares ; Kretschmer, Kevin ; Lermyte, Frederik |
| Art des Eintrags: | Zweitveröffentlichung |
| Titel: | Charge site manipulation to enhance top‐down fragmentation efficiency |
| Sprache: | Englisch |
| Publikationsjahr: | 17 Juni 2024 |
| Ort: | Darmstadt |
| Publikationsdatum der Erstveröffentlichung: | Februar 2024 |
| Ort der Erstveröffentlichung: | Weinheim |
| Verlag: | Wiley-VCH |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Proteomics : Proteomics and Systems Biology |
| Jahrgang/Volume einer Zeitschrift: | 24 |
| (Heft-)Nummer: | 3-4 |
| Kollation: | 10 Seiten |
| DOI: | 10.26083/tuprints-00027109 |
| URL / URN: | https://tuprints.ulb.tu-darmstadt.de/27109 |
| Zugehörige Links: | |
| Herkunft: | Zweitveröffentlichung DeepGreen |
| Kurzbeschreibung (Abstract): | In recent years, top‐down mass spectrometry has become a widely used approach to study proteoforms; however, improving sequence coverage remains an important goal. Here, two different proteins, α‐synuclein and bovine carbonic anhydrase, were subjected to top‐down collision‐induced dissociation (CID) after electrospray ionisation. Two high‐boiling solvents, DMSO and propylene carbonate, were added to the protein solution in low concentration (2%) and the effects on the top‐down fragmentation patterns of the proteins were systematically investigated. Each sample was measured in triplicate, which revealed highly reproducible differences in the top‐down CID fragmentation patterns in the presence of a solution additive, even if the same precursor charge state was isolated in the quadrupole of the instrument. Further investigation supports the solution condition‐dependent selective formation of different protonation site isomers as the underlying cause of these differences. Higher sequence coverage was often observed in the presence of additives, and the benefits of this approach became even more evident when datasets from different solution conditions were combined, as increases up to 35% in cleavage coverage were obtained. Overall, this approach therefore represents a promising opportunity to increase top‐down fragmentation efficiency. |
| Freie Schlagworte: | electrospray ionization mass spectrometry (ESI‐MS), mass spectrometry, top‐down proteomics |
| ID-Nummer: | Artikel-ID: 2300082 |
| Status: | Verlagsversion |
| URN: | urn:nbn:de:tuda-tuprints-271094 |
| Zusätzliche Informationen: | Special Issue: Top‐down proteomics and proteoforms |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 540 Chemie 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie |
| Fachbereich(e)/-gebiet(e): | 07 Fachbereich Chemie 07 Fachbereich Chemie > Clemens-Schöpf-Institut > Fachgebiet Biochemie 07 Fachbereich Chemie > Clemens-Schöpf-Institut |
| Hinterlegungsdatum: | 17 Jun 2024 12:38 |
| Letzte Änderung: | 18 Jun 2024 05:42 |
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| Suche nach Titel in: | TUfind oder in Google |
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- Charge site manipulation to enhance top‐down fragmentation efficiency. (deposited 17 Jun 2024 12:38) [Gegenwärtig angezeigt]
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