Zitieren Sie bitte immer diesen URN: urn:nbn:de:kobv:b43-647565
Radiation damage to amino acids, peptides and DNA-binding proteins: the influence of water directly monitored by X-ray photoelectron spectroscopy
- Ionizing radiation damage to biomolecules plays a crucial role in radiotherapy as a cancer treatment. Among these, DNA-binding proteins are of particular interest due to their pivotal roles in shielding DNA and facilitating its repair. Hence, in this study, we present first-ever recorded data of radiation damage to a protein monitored directly with near-ambient pressure (NAP) X-ray photoelectron spectroscopy (XPS) under a water atmosphere. This surface sensitive technique was used to in situ damage and probe gene-V protein (G5P, a model DNA-binding protein) under wet NAP conditions and dry vacuum (UHV) conditions to determine the effect of water on the radiation response. In addition, the X-ray radiation damage to selected pure amino acids and short homopeptides was determined to better understand the variety of damage mechanisms within the complex protein. In dry samples, drastic chemical changes were detected in all biomolecules dominated by fragmentation processes. Here, theIonizing radiation damage to biomolecules plays a crucial role in radiotherapy as a cancer treatment. Among these, DNA-binding proteins are of particular interest due to their pivotal roles in shielding DNA and facilitating its repair. Hence, in this study, we present first-ever recorded data of radiation damage to a protein monitored directly with near-ambient pressure (NAP) X-ray photoelectron spectroscopy (XPS) under a water atmosphere. This surface sensitive technique was used to in situ damage and probe gene-V protein (G5P, a model DNA-binding protein) under wet NAP conditions and dry vacuum (UHV) conditions to determine the effect of water on the radiation response. In addition, the X-ray radiation damage to selected pure amino acids and short homopeptides was determined to better understand the variety of damage mechanisms within the complex protein. In dry samples, drastic chemical changes were detected in all biomolecules dominated by fragmentation processes. Here, the breakage of peptide
bonds in the peptides and the protein are dominant. Surprisingly, hydration – despite introducing additional indirect damage pathways via water radiolysis – led to a reduction in overall radiation damage. This behaviour was attributed to hydration-dependent changes in reaction rates and respective deexcitation and damaging channels within the molecules and secondary species such as low-energy (LEE), (pre)-hydrated/(pre)-solvated electrons and radical species such as hydroxyl radicals.…


| Autor*innen: | Dorothea C. Hallier, Jörg RadnikORCiD, Paul M. Dietrich, Harald Seitz, Marc Benjamin Hahn |
|---|---|
| Dokumenttyp: | Zeitschriftenartikel |
| Veröffentlichungsform: | Verlagsliteratur |
| Sprache: | Englisch |
| Titel des übergeordneten Werkes (Englisch): | Phyisical Chemistry Chemical Physics |
| Jahr der Erstveröffentlichung: | 2025 |
| Organisationseinheit der BAM: | 6 Materialchemie |
| 6 Materialchemie / 6.1 Oberflächen- und Dünnschichtanalyse | |
| Veröffentlichende Institution: | Bundesanstalt für Materialforschung und -prüfung (BAM) |
| Verlag: | Royal Society of Chemistry |
| Jahrgang/Band: | 27 |
| Ausgabe/Heft: | 48 |
| Erste Seite: | 1 |
| Letzte Seite: | 22 |
| DDC-Klassifikation: | Technik, Medizin, angewandte Wissenschaften / Ingenieurwissenschaften / Ingenieurwissenschaften und zugeordnete Tätigkeiten |
| Freie Schlagwörter: | (Near-ambient pressure) X-ray photoelectron spectroscopy; Radiation damage; Ultra-high vacuum |
| Themenfelder/Aktivitätsfelder der BAM: | Material |
| Material / Advanced Materials | |
| DOI: | 10.1039/d5cp01887k |
| URN: | urn:nbn:de:kobv:b43-647565 |
| Verfügbarkeit des Dokuments: | Datei für die Öffentlichkeit verfügbar ("Open Access") |
| Lizenz (Deutsch): | Creative Commons - CC BY - Namensnennung 4.0 International |
| Datum der Freischaltung: | 19.11.2025 |
| Referierte Publikation: | Ja |
| Datum der Eintragung als referierte Publikation: | 22.12.2025 |
| Schriftenreihen ohne Nummerierung: | Wissenschaftliche Artikel der BAM |


