Compound monograph
Glutathione (reduced)
Reduced glutathione is γ-L-glutamyl-L-cysteinylglycine, an acyclic three-unit peptide with a free cysteine thiol. The first amide bond uses the glutamyl γ-carboxyl group.
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Identity & nomenclature
Reduced glutathione is γ-L-glutamyl-L-cysteinylglycine, an acyclic three-unit peptide with a free cysteine thiol. The first amide bond uses the glutamyl γ-carboxyl group.
GSH denotes the reduced, unconjugated parent in this record. Glutathione disulfide, sodium-containing material and covalent conjugates are separate chemical identities.
Canonical name: Glutathione.
Declared aliases and development codes: Reduced glutathione, GSH, γ-L-Glutamyl-L-cysteinylglycine.
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Molecular properties
| Molecular formula | C10H17N3O6S |
|---|---|
| Molecular mass | 307.321 Da |
| CAS Registry Number | 70-18-8 |
| PubChem CID | 124886 |
| UNII | GAN16C9B8O |
| Three-letter sequence | γ-Glu–Cys–Gly |
| Terminal groups | Free N-terminal amino group; Free C-terminal carboxyl group |
γ-Glu is one L-glutamyl unit whose γ-carboxyl carbonyl, rather than its α-carboxyl group, forms the amide bond to Cys2 nitrogen. Cys2 is L and forms the ordinary carboxyl-to-amino bond to achiral Gly3. No one-letter string is supplied because it would conceal the γ linkage.
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Structural characteristics
The γ-glutamyl linkage is an acyclic isopeptide bond; it does not form a side-chain lactam ring. Ko et al. examined mass-selected gas-phase anions and inferred neutral-parent structures by spectroscopy and calculations. That experiment does not independently determine residue stereochemistry or bulk crystal composition.
- Acyclic γ-glutamyl linkage between residues 1 and 2
- Free cysteine thiol at position 2
Terminal features: Free N-terminal amino group, Free C-terminal carboxyl group.
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Molecular targets & mechanisms
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Analytical considerations
The recorded 307.321 Da is the CIAAW 2024 average mass calculated from C10H17N3O6S. Görbitz (1987) reports a formula weight of 307.33, while Hübschle et al. (2018) report 307.32; GSRS records mwt 307.325. Their calculation tables or conventions remain unestablished. These source numbers are non-defining for the formula-derived field, and the 307.33 value differs from that calculation. No oxidized, salt or conjugate composition is included in the parent formula.
What the studies reported
No verified findings are published for this record under Content Policy v1.
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Verified bibliography
Cited studies by type
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Reference 1
Intrinsic neutral and anionic structures of glutathione.Ko YJ, Wang H, Li X, Bowen KH, Lecomte F, Desfrançois C, Poully JC, Grégoire G, Schermann JP
Chemphyschem : a European journal of chemical physics and physical chemistry · 2009-12-07 · Journal Article
current
Study models of these references
What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.
| Reference | Study models |
|---|---|
| Ko YJ et al. 2009 | Chemical, structural or analytical study; no biological model reported |
Record history
Published 2026-10-20.
- : Sequence and structure, Analytical notes
Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.
Cite this record: Purely Peptides Research Library. Glutathione (reduced). Published 2026-10-20; updated 2026-10-20. https://purelypeptides.org/research/compounds/glutathione/
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Methodology & citation verification
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