Multiple proteins via nonspecific reactive oxygen species-mediated oxidation (ROS-mediated protein oxidation)

Multiple proteins via nonspecific reactive oxygen species (ROS)-mediated oxidation refers to a broad mechanism of action where ROS induce damage across a wide array of cellular proteins rather than binding to a specific receptor or enzyme. This process involves the chemical modification of amino acid side chains, such as the formation of protein carbonyls or disulfide cross-links, which leads to protein misfolding, loss of enzymatic activity, and eventual cell death (PubMed: 17603810). While this is often a pathological feature of aging and neurodegeneration, it is therapeutically exploited in treatments like photodynamic therapy (PDT) and the use of certain antiseptics (NIH: PMC3634454). In these contexts, drugs or light-activated sensitizers generate high local concentrations of ROS to destroy cancer cells or pathogens nonspecifically. However, the lack of specificity poses significant challenges, as it can lead to collateral damage in healthy tissues and systemic oxidative stress (PubMed: 23626520). This mechanism is fundamentally different from targeted therapies, as it relies on overwhelming the cell's total antioxidant capacity to induce catastrophic failure of cellular machinery (PubMed: 25910080).

Other names

ROS-induced protein damageNonspecific oxidative protein modificationProtein carbonylationOxidative stress-induced proteotoxicity

Generation of reactive oxygen species (ROS) such as hydroxyl radicals or singlet oxygen that nonspecifically oxidize protein side chains, leading to structural denaturation, aggregation, and loss of biological activity.