Glutathione disulfide (GSSG)

Glutathione disulfide (GSSG) is the oxidized dimer form of glutathione formed via a disulfide bond between two cysteine residues from separate glutathione molecules. It arises during the detoxification of peroxides by antioxidant enzymes such as glutathione peroxidases; these reactions convert reduced glutathione (GSH) into GSSG while neutralizing reactive oxygen species. The enzyme glutathione reductase catalyzes the reduction of GSSG back to two molecules of GSH using NADPH as an electron donor, maintaining cellular redox balance. The intracellular ratio between GSH and GSSG serves as a sensitive indicator of cellular oxidative status—a low ratio signals increased oxidative stress and has been linked with neurodegenerative conditions such as Parkinson's disease and Alzheimer's disease. At high concentrations, both reduced and oxidized forms can act as neuromodulators at certain neurotransmitter receptors but this does not constitute classical receptor-ligand pharmacology. Note: Glutathione disulfide (GSSG) is not considered a classical drug target such as an enzyme, receptor, transporter, or ion channel; rather it is primarily regarded as a metabolic intermediate/marker within antioxidant systems. If you are seeking information on targets involved in its metabolism or regulation—such as glutathione reductase—those would be considered valid therapeutic targets instead.

Other names

Oxidized glutathioneGlutathione disulphideDisulfide, glutathioneOxiglutatione

Not applicable—GSSG is not a therapeutic target but rather a metabolic product and redox indicator. Drugs that affect its levels do so indirectly by modulating redox enzymes or pathways.