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Peer-reviewedCC BY-NC-NDJournal of the American Society for Mass Spectrometry

Deep Ultraviolet Laser Ablation Surface Sampling for Native Mass Spectrometry.

  • Neda Feizi1
  • Kadeem O Hayes2
  • Kelcey B Hines2
  • Raul A Villacob3
  • Kermit K Murray2
  • Touradj Solouki1
  1. 1Department of Chemistry and Biochemistry, Baylor University, Waco, Texas76798, United States.
  2. 2Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana70803, United States.
  3. 3Department of Surgery, Baylor College of Medicine, Houston, Texas77030, United States.
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Abstract

A pulsed 193 nm deep ultraviolet (DUV) laser was used to ablate proteins and a noncovalently bound protein assembly deposited on surfaces. DUV laser ablation has been used for ablation of proteins from surfaces without fragmentation; however, DUV ablation of native proteins from surfaces without the loss of higher-order structure of proteins has not been demonstrated. Here, protein charge state distribution (CSD) and collision-induced unfolding (CIU) were used to probe the structure of DUV laser-ablated native proteins. Standard solutions containing native bovine serum albumin (BSA), jack-bean concanavalin A (ConA), and bovine carbonic anhydrase (CA) were deposited on a quartz microscope slide, laser-ablated, and captured for ion mobility-mass spectrometry (IM-MS) analysis. Observed CSD from native MS of conventionally extracted and DUV laser-ablated proteins were comparable. CIU plots for all charge states of laser-ablated proteins exhibited the same ion mobility features and comparable transition voltages (CIU50) as the extracted samples. These results suggest that DUV laser ablation can yield intact proteins with conserved higher-order structures.

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Cite

BibTeXRIS
BibTeX
@article{feizi2026deep,
  title = {{Deep Ultraviolet Laser Ablation Surface Sampling for Native Mass Spectrometry.}},
  author = {Neda Feizi and Kadeem O Hayes and Kelcey B Hines and Raul A Villacob and Kermit K Murray and Touradj Solouki},
  journal = {Journal of the American Society for Mass Spectrometry},
  year = {2026},
  month = oct,
  doi = {10.1021/jasms.6c00185},
  url = {https://europepmc.org/article/MED/42916771},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - Deep Ultraviolet Laser Ablation Surface Sampling for Native Mass Spectrometry.
AU  - Neda Feizi
AU  - Kadeem O Hayes
AU  - Kelcey B Hines
AU  - Raul A Villacob
AU  - Kermit K Murray
AU  - Touradj Solouki
PY  - 2026
DA  - 2026/10/01
JO  - Journal of the American Society for Mass Spectrometry
DO  - 10.1021/jasms.6c00185
UR  - https://europepmc.org/article/MED/42916771
AB  - A pulsed 193 nm deep ultraviolet (DUV) laser was used to ablate proteins and a noncovalently bound protein assembly deposited on surfaces. DUV laser ablation has been used for ablation of proteins from surfaces without fragmentation; however, DUV ablation of native proteins from surfaces without the loss of higher-order structure of proteins has not been demonstrated. Here, protein charge state distribution (CSD) and collision-induced unfolding (CIU) were used to probe the structure of DUV laser-ablated native proteins. Standard solutions containing native bovine serum albumin (BSA), jack-bean concanavalin A (ConA), and bovine carbonic anhydrase (CA) were deposited on a quartz microscope slide, laser-ablated, and captured for ion mobility-mass spectrometry (IM-MS) analysis. Observed CSD from native MS of conventionally extracted and DUV laser-ablated proteins were comparable. CIU plots for all charge states of laser-ablated proteins exhibited the same ion mobility features and comparable transition voltages (CIU50) as the extracted samples. These results suggest that DUV laser ablation can yield intact proteins with conserved higher-order structures.
SN  - 1044-0305
SN  - 1879-1123
ER  -