Cysteine Modification Mass Spectrometry
Cysteine modification mass spectrometry is a highly sensitive analytical method based on mass spectrometry technology, used to study the modification status of cysteine residues in proteins and their functional roles in biological processes. Cysteine is a sulfur-containing amino acid, and due to the high reactivity of its side chain thiol group, it plays a role in intracellular redox balance, signal transmission, and enzyme-catalyzed reactions. Through specific chemical modification methods and mass spectrometry technology, cysteine modification mass spectrometry can precisely identify and quantify the types of modifications (such as thiolation, disulfide bonds, nitrosylation, glutathionylation, etc.) of cysteine in proteins, and reveal their key roles in biological processes. The application scope of cysteine modification mass spectrometry is very broad. In oxidative stress research, when cells are exposed to oxidative stimuli, cysteine residues are the primary reactive sites, and changes in their modification status can reflect the degree of redox imbalance within the cells. Using cysteine modification mass spectrometry, researchers can dynamically monitor modifications induced by oxidative stress and explore the cellular antioxidant mechanisms in depth. In disease research, cysteine modifications play roles in many pathological processes, such as cancer, diabetes, neurodegenerative diseases, and cardiovascular diseases. This method can reveal the modification patterns and regulatory mechanisms of disease-related proteins, providing scientific evidence for developing new diagnostic markers and therapeutic strategies. Additionally, this method is widely used in drug screening and target research, especially for precise analysis of active centers or regulatory sites of target proteins.
The technical process of cysteine modification mass spectrometry generally includes several main steps: sample preparation, chemical modification, mass spectrometry detection, and data analysis. In the sample preparation stage, researchers need to select appropriate protein extraction methods according to experimental needs and treat protein samples with reducing or oxidizing agents to control the modification status of cysteine. Subsequently, specific modifications of thiol groups are carried out using chemical labeling reagents (such as iodoacetamide or methylation reagents) to enhance the sensitivity and accuracy of mass spectrometry detection. In the mass spectrometry analysis stage, samples are separated by liquid chromatography before entering the mass spectrometer, where the characteristic peptides of cysteine modifications are analyzed using tandem mass spectrometry (MS/MS) technology. Finally, specialized bioinformatics tools are used to analyze and annotate the mass spectrometry data, generating high-confidence identification results of modification sites.
In recent years, with the enhancement of mass spectrometry instrument performance and advancements in chemical labeling technology, the sensitivity and resolution of cysteine modification mass spectrometry have significantly improved, allowing efficient detection of low-abundance modification sites in complex proteome samples. This advancement has expanded the applicability of the method, enabling not only the analysis of modification status of individual proteins but also the comprehensive revelation of the dynamic network of cysteine modifications at the proteome level. For example, in high-throughput redox proteomics, it can simultaneously analyze the modification status of thousands of proteins, providing researchers with systematic insights and revealing global features of redox regulation.
Biotech Pack BioScience, with its extensive experience in the field of proteomics research, provides high-quality mass spectrometry analysis services to clients. Whether for basic research or clinical applications, we are committed to customizing the optimal solutions for our clients, supporting scientific exploration and industrial innovation.
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