S-Persulfidation Analysis – LC-MS/MS Mapping of Protein Persulfide Modifications

Protein S-persulfidation is a reversible process that alters the thiol groups (-SH) of cysteine residues into persulfides (-SSH). This modification helps in boosting antioxidant defenses, controlling redox signaling, and maintaining protein function during oxidative stress. Creative Proteomics offers precise research services aimed at identifying and measuring protein S-persulfidation.

Comprehensive Detection: Identify and measure S-persulfidated proteins and specific amino acid modifications.
Advanced Technology: Utilize biotin labeling and enrichment techniques combined with LC-MS/MS for accuracy and depth.
Functional Insights: Apply bioinformatics tools to analyze motifs, pathways, and network interactions.
Research Impact: Clarify the regulatory roles of S-persulfidation in signaling pathways and offer new perspectives for understanding mechanisms and identifying therapeutic targets in metabolic and cardiovascular diseases.

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What is S-persulfidation?

Protein S-persulfidation, also known as S-sulfhydration, is a reversible redox modification where the thiol group of cysteine residues is transformed into a persulfide. This process is critical for hydrogen sulfide (H₂S) to perform its biological functions. It mainly occurs when H₂S reacts with oxidized cysteine intermediates or transfers sulfur through small molecule persulfides and sulfur transferases. This modification enhances antioxidant capacity by protecting proteins from damage due to irreversible oxidation, regulates enzyme activity and redox signaling, and helps in maintaining cellular balance. Persulfidation plays a significant role in metabolism, mitochondrial function, cardiovascular and neuroprotection, and its reduction is linked to aging and various diseases. Being a dynamic and reversible post-translational modification, S-persulfidation is a key element connecting H₂S signaling to protein regulation^[1].

S-persulfidation Service at Creative Proteomics

Understanding S-persulfidation is essential for exploring redox-based regulatory processes and discovering new biomarkers or therapeutic targets related to oxidative stress diseases. Therefore, identifying S-persulfidated proteins and their specific amino acid sites in biological tissues or cells is crucial. We provide complete proteomics services for analyzing S-persulfidated proteins, including high-resolution mass spectrometry, site-specific identification, quantitative profiling, and advanced bioinformatics analysis. Our services assist researchers in systematically studying S-persulfidated proteins, exploring their pathway connections, and uncovering their clinical and therapeutic significance.

S-persulfidation Research Platforms

Thermo Fisher Easy-nLC 1000 and Thermo Fisher LTQ Obitrap ETD
(Figure from Thermo Scientific)

Workflow of S-persulfidation Analysis

Advantages of Our S-persulfidation Service

Professional Detection and Analysis: Experienced research team with reliable and established techniques.
Broad Applicability: We can handle protein samples from a wide range of sources such as cells, animal and plant tissues, microorganisms, etc.
High Specificity and Accuracy: Use of skilled quantification proteomics techniques and PTMs enrichment methods.
Consistent and Reproducible Results: Obtain stable and repeatable inter- and intra-assay results for data analysis.
Advanced Analytical Platforms: Utilization of high-sensitivity mass spectrometry and state-of-the-art technologies to ensure precise and repeatable results.
End-to-End Support: Provide full-service from design to data interpretation with continuous technical support throughout the research process.

Applications of S-persulfidation

Neurodegenerative disease

In neurodegenerative conditions such as Alzheimer's and Parkinson's diseases, lower levels of protein S-persulfidation lead to reduced activity, abnormal phosphorylation, and increased aggregation of proteins such as Parkin and GSK3β, thereby promoting neuronal damage and the progression of disease^[2][3].

Macrophages and inflammation

In activated macrophages involved in inflammation, protein S-persulfidation helps by suppressing NLRP3 inflammasome activity, reducing inflammatory cell death^[4].

Senescence and Sarcopenia

During aging, the production of hydrogen sulfide (H₂S) decreases due to reduced expression of H₂S-producing enzymes, such as cystathionine γ-lyase (CSE), leading to lower levels of protein S-persulfidation. This reduction weakens antioxidant defenses, impairs mitochondrial function, and interferes with proteostasis, accelerating aging and contributing to the loss of muscle mass and function (sarcopenia)^[3].

Cardiometabolic health

In the cardiovascular system, S-persulfidation helps maintain vasodilation, mitochondrial balance, and antioxidant capacity by modifying key enzymes and signaling proteins. A deficiency or decrease in this modification worsens inflammation, increases oxidative damage accumulation, and raises the risk of myocardial structural changes and heart failure^[2].

COVID-19

During a COVID-19 infection, the body's reduced production of H₂S and lower levels of S-persulfidation disrupt redox balance, impair mitochondrial function, and amplify inflammatory responses, which facilitate viral replication, lung injury, and vascular or coagulation issues^[2].

Demo Result of S-persulfidation Service

PCA plot

Heat map

GO analysis

Heatmap

The plot represents the pathway enrichment analysis of S-persulfidated proteins.

KEGG analysis

The protein-protein interaction network highlights the interactions between all differentially S-persulfidated proteins.

PPI

FAQs of S-persulfidation Service

Which sample types are accepted by the service？

We accept a variety of sample types including cells, tissues, plant tissue and more. If you have other special sample types, please consult in advance.

Whether the sample needs pretreatment?

We recommend that customers provide fresh or frozen samples, which should avoid repeated freezing and thawing, and we will be responsible for subsequent protein extraction and pretreatment. If you have already extracted the protein, please communicate with us in advance about the sample handling method.

Learn about other Q&A.

Case Study

Article

Publications

Here are some publications in Proteomics research from our clients:

The yeast protein Mam33 functions in the assembly of the mitochondrial ribosome. 2019. https://doi.org/10.1074/jbc.RA119.008476
Microglia-mediated synaptic pruning in the nucleus accumbens during adolescence: A preliminary study of the proteomic consequences and putative female-specific pruning target. 2023. https://doi.org/10.1101/2023.05.03.539317
In Vitro Identification of Phosphorylation Sites on TcPolβ by Protein Kinases TcCK1, TcCK2, TcAUK1, and TcPKC1 and Effect of Phorbol Ester on Activation by TcPKC of TcPolβ in Trypanosoma cruzi Epimastigotes. 2024. https://doi.org/10.3390/microorganisms12050907
Extracellular vesicles regulate metastable phenotypes of lymphangioleiomyomatosis cells via shuttling ATP synthesis to pseudopodia and activation of integrin adhesion complexes. 2024. https://doi.org/10.1101/2024.09.09.611297
Assessment of Fasciola hepatica glutathione S-transferase as an antigen for serodiagnosis of human chronic fascioliasis. 2018. https://doi.org/10.1016/j.actatropica.2018.07.002

More Publications

S-persulfidation Service Sample Requirements

Sample	Sample Quantity
Tissue	animal tissue	200-500mg
Tissue	fresh plant	200-500mg
Cell	suspension cell	> 3x10⁸
	adherent cell	> 3x10⁸
	microorganism	> 50 mg or 3 × 10⁸ cells
Protein	Total protein > 5mg and concentration >1 μg/μL

References

Andrés, C. M. C., Lobo, F., Lastra, J. M. P., Munguira, E. B., Juan, C. A., & Pérez Lebeña, E. (2025). Reactive Sulfur Species and Protein Persulfidation: An Emerging Redox Axis in Human Health and Disease. Current issues in molecular biology, 47(9), 765. https://doi.org/10.3390/cimb47090765
Petrovic, D., Kouroussis, E., Vignane, T., & Filipovic, M. R. (2021). The Role of Protein Persulfidation in Brain Aging and Neurodegeneration. Frontiers in aging neuroscience, 13, 674135. https://doi.org/10.3389/fnagi.2021.674135
Salti, T., Braunstein, I., Haimovich, Y., Ziv, T., & Benhar, M. (2024). Widespread S-persulfidation in activated macrophages as a protective mechanism against oxidative-inflammatory stress. Redox biology, 72, 103125. https://doi.org/10.1016/j.redox.2024.103125

Proteomics Sample Submission Guidelines

Ensure your samples are prepared and submitted correctly by downloading our comprehensive Proteomics Sample Submission Guidelines. This document provides detailed instructions and essential information to facilitate a smooth submission process. Click the link below to access the PDF and ensure your submission meets all necessary criteria.

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From Our Clients

"I recently used their proteomics service for a project analyzing protein interactions in yeast models. The team was very responsive and helped clarify the methodology they employed, which made me feel confident in the results. The data quality was solid, with clear identification of several key proteins involved in our study. Their thorough analysis enabled me to pinpoint specific interactions that I hadn't considered before, which significantly improved the direction of my research. I appreciate their professionalism and support throughout the process."

Sarah Thompson, University of California, Berkeley

"Our lab collaborated with them on a project studying cancer biomarkers. The proteomics analysis provided was detailed and focused, specifically highlighting the differential expression of proteins between healthy and tumor samples. Their clear explanations of the data helped my team understand the biological implications. I also appreciated their willingness to revise the reports based on our feedback, ensuring that we had everything we needed for our publication. This collaborative spirit was invaluable."

Emily Rodriguez, Stanford University

"Our lab worked with them on a project studying the effects of diet on gut microbiota using proteomics. They used a label-free quantification method to analyze proteins in fecal samples before and after dietary intervention. The results showed significant changes in protein expression linked to microbial activity. This was pivotal for our hypothesis about diet-microbiota interactions. The clarity of their data presentation made it easy for our team to integrate these findings into our ongoing research."

Dr. Lisa Wong, University of Toronto

"My experience with Creative Proteomics during the mass spectrometry analysis was excellent. We sent in human saliva and mouse brain tissue samples, which they expertly analyzed using both LC-MS and GC-MS techniques. The results were invaluable, revealing key metabolites in the saliva and identifying biomarkers linked to brain function in the brain tissue."

Dr. Emily Carter, Senior Research Scientist

"The overall service from Creative Proteomics was outstanding. They made the entire process seamless and efficient, allowing us to focus on our research. We worked with leaf and root samples from various Arabidopsis genotypes for targeted metabolomics analysis. Their thorough profiling of primary and secondary metabolites gave us important insights into how the plants respond metabolically to environmental stress."

Dr. Laura Henderson, Plant Physiologist

"We had a pleasant collaboration with Creative Proteomics on mass spectrometry analysis of lipids. They conducted a detailed analysis of lipid species, providing us with important insights into lipid metabolism and its relationship with metabolic syndrome disease states."

Dr. Sarah Mitchell, Research Scientist

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