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PreprintCC BY-NC-NDChemRxiv

Vibrational Excitation of Water Drives Proton Reactivity with Native Proteins During Mid-Infrared Laser Desorption Coupled to Mass Spectrometry.

  • Khaled Madhoun1,2
  • Semah Keissieh3,4
  • Alexander Wainwright1,2
  • R.J. Dwayne Miller1,2,5
  • Pei Su3,4,6
6 affiliations
  1. 1Physics
  2. 2University of Toronto
  3. 3Biochemistry
  4. 4University of California Riverside
  5. 5Chemistry
  6. 6Bioengineering
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Abstract

We discovered a vibrational-excitation-driven proton reactivity between proteins and their surrounding aqueous environment during mid-infrared laser Desorption by Impulsive Vibrational Excitation (DIVE). We show that this process, when coupled directly to high resolution mass spectrometry (MS) without secondary ionization sources, produces intact gas-phase ions of proteins retaining their compact conformations. The unexpected multiple protonation states of protein ions are generated through a series of concerted proton transfer processes to protein surface residues. We propose that laser-induced ionization via DIVE is facilitated by sub-nanosecond transient superheating and Grotthuss proton hopping processes. By coupling to high-resolution MS, protein ionization via DIVE opens up an avenue for chemical and structural characterization of proteins and their complexes directly from aqueous and physiological buffer environments.

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Cite

BibTeXRIS
BibTeX
@misc{madhoun2026vibrational,
  title = {{Vibrational Excitation of Water Drives Proton Reactivity with Native Proteins During Mid-Infrared Laser Desorption Coupled to Mass Spectrometry.}},
  author = {Khaled Madhoun and Semah Keissieh and Alexander Wainwright and R.J. Dwayne Miller and Pei Su},
  howpublished = {ChemRxiv},
  year = {2026},
  month = oct,
  doi = {10.26434/chemrxiv-2025-gj685/v2},
  url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv-2025-gj685/v2},
  note = {CC BY-NC-ND},
}
RIS
TY  - UNPB
TI  - Vibrational Excitation of Water Drives Proton Reactivity with Native Proteins During Mid-Infrared Laser Desorption Coupled to Mass Spectrometry.
AU  - Khaled Madhoun
AU  - Semah Keissieh
AU  - Alexander Wainwright
AU  - R.J. Dwayne Miller
AU  - Pei Su
PY  - 2026
DA  - 2026/10/21
PB  - ChemRxiv
DO  - 10.26434/chemrxiv-2025-gj685/v2
UR  - https://chemrxiv.org/doi/full/10.26434/chemrxiv-2025-gj685/v2
AB  - We discovered a vibrational-excitation-driven proton reactivity between proteins and their surrounding aqueous environment during mid-infrared laser Desorption by Impulsive Vibrational Excitation (DIVE). We show that this process, when coupled directly to high resolution mass spectrometry (MS) without secondary ionization sources, produces intact gas-phase ions of proteins retaining their compact conformations. The unexpected multiple protonation states of protein ions are generated through a series of concerted proton transfer processes to protein surface residues. We propose that laser-induced ionization via DIVE is facilitated by sub-nanosecond transient superheating and Grotthuss proton hopping processes. By coupling to high-resolution MS, protein ionization via DIVE opens up an avenue for chemical and structural characterization of proteins and their complexes directly from aqueous and physiological buffer environments.
ER  -