Cellular thiol-containing molecules (Thiols)

Cellular thiol-containing molecules, primarily represented by the tripeptide glutathione (GSH) and various protein-bound sulfhydryl groups, are critical components of the cellular antioxidant defense system and redox signaling network (Source: NIH, PubChem). These molecules maintain the intracellular reducing environment, protecting proteins, lipids, and nucleic acids from oxidative damage caused by reactive oxygen species (ROS) and electrophilic toxins (Source: PubMed). In many diseases, including cancer and neurodegeneration, the balance of these thiols is disrupted, often leading to increased oxidative stress or, conversely, providing cancer cells with resistance to therapy (Source: Journal of Biological Chemistry). Pharmacological intervention often involves modulating these thiol levels, such as using N-acetylcysteine to replenish glutathione during acetaminophen overdose or using depletion strategies like buthionine sulfoximine to sensitize tumor cells to chemotherapy (Source: StatPearls). Because this term encompasses a wide range of small molecules and proteins, it is generally considered a biochemical class or a collective metabolic pool rather than a single discrete therapeutic target (Source: Wikipedia).

Other names

Endogenous thiolsSulfhydryl-containing compoundsCellular mercaptansNon-protein thiols (NPSH)Protein thiols

Drugs modulate cellular thiols by acting as precursors for their synthesis (e.g., N-acetylcysteine providing cysteine for GSH synthesis), by undergoing direct conjugation to neutralize reactive metabolites (e.g., acetaminophen metabolites), by inhibiting enzymes responsible for thiol synthesis or recycling (e.g., buthionine sulfoximine), or by forming covalent adducts with protein thiols to alter signaling (e.g., dimethyl fumarate) (Source: PubMed, StatPearls).