Thesis
Tracing hydrogen sulfide mediated protein persulfidation in plants with ³⁴S labeled dithiophosphate probe
University of Iowa
Master of Science (MS), University of Iowa
Autumn 2025
Abstract
Hydrogen sulfide (H2S) is an important cellular signaling chemical that regulates redox balance through the persulfidation of cysteine residues on proteins. This research focuses on developing isotopically labeled H2S donors and model disulfides to study these processes in biological systems. The key goal of this study was the synthesis of P2S5 from P and S to develop this method to ultimately enable the synthesis of 34S labeled P234S5 as a source of labelled H2S. Additionally, chemicals that can be used to investigate the degradation of protected persulfides to determine which one of two sulfurs was retained was investigated. P2S5 was successfully synthesized from red phosphorus and elemental sulfur under inert conditions, producing a yellow solid confirmed by 31P NMR spectroscopy and offering a safer, more reliable alternative to traditional methods. This intermediate was then used to prepare dibutyldithiophosphate (DBDTP) with 1H and 31P NMR spectroscopy confirming its purity and structure. To investigate the incorporation of 34S into persulfides, N-acetylcysteine (NAC) was first oxidized to its disulfide and then converted into an N-propylamide peptide model, while thiol-functionalized iodoacetamide derivatives were also prepared to allow controlled 34S incorporation into the models. NMR analyses verified the successful synthesis of these compounds, providing well-characterized intermediates for studying isotopically labeled persulfides and H2S mediated processes. This study reports a practical route to synthesize isotopically labeled H2S donors and peptide models, providing useful tools to study persulfidation and H2S driven redox processes. Future work will refine thiol protection and labeling strategies while applying these compounds in plant and cell-based research. Overall, this work establishes a versatile platform for exploring sulfur biology with promising applications in agriculture and therapeutics.
Details
- Title: Subtitle
- Tracing hydrogen sulfide mediated protein persulfidation in plants with ³⁴S labeled dithiophosphate probe
- Creators
- Heenatigala Pathiranage Kavindi Vishuka Tiroshini Pathirana
- Contributors
- Ned B Bowden (Advisor)Gregory K Friestad (Committee Member)F Christopher Pigge (Committee Member)
- Resource Type
- Thesis
- Degree Awarded
- Master of Science (MS), University of Iowa
- Degree in
- Chemistry
- Date degree season
- Autumn 2025
- Publisher
- University of Iowa
- Number of pages
- vi, 43 pages
- Copyright
- Copyright 2025 Heenatigala Pathiranage Kavindi Vishuka Tiroshini Pathirana
- Language
- English
- Date submitted
- 12/08/2025
- Description illustrations
- illustrations (some color)
- Description bibliographic
- Includes bibliographical references (page 25-27).
- Public Abstract (ETD)
Hydrogen sulfide might be best known for its rotten egg smell, but in our bodies and plants, it is an important messenger that helps protect cells and regulate key chemical processes. This research focuses on making special, traceable forms of hydrogen sulfide and related chemicals to better understand how it interacts with proteins and controls cellular functions. We developed a safer way to synthesize a sulfur-based chemical that can release hydrogen sulfide in a controlled manner, including versions labeled with a detectable sulfur isotope. These labeled compounds can be used to build small protein models that mimic how hydrogen sulfide modifies proteins in living systems. Careful analysis confirmed that these molecules were well-prepared and ready for use in studying these processes. This work provides scientists with practical tools to explore how hydrogen sulfide acts within cells. In the future, these methods can be applied to plants and other biological systems to trace how sulfur moves and affects proteins, offering exciting possibilities for agriculture and medicine.
- Academic Unit
- Chemistry
- Record Identifier
- 9985135149102771
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