Glutathione Peptide 600mg

Key facts

01 What Is Glutathione?

The glutathione peptide is a tripeptide built from glutamate, cysteine and glycine, and few small molecules in biochemistry have been studied as heavily. Cells make it with enzymes, not on ribosomes. In many cell types it is the most abundant non-protein thiol ^[1][2].

The gamma bond in the glutathione peptide

The chemistry gets interesting at the first bond. Glutamate attaches to cysteine through its side-chain (gamma) carboxyl group instead of the usual alpha carboxyl, which is why the molecule is written gamma-Glu-Cys-Gly. That gamma linkage also explains why most ordinary peptidases can't break it down ^[1].

Here we treat the glutathione peptide strictly as a chemical entity: structure, its two main forms, the biochemistry literature, how it is analyzed, and how Vinnix batches are documented. We make no claim about any effect of the Vinnix product.

02 Glutathione Product Specifications

The glutathione peptide is supplied at 600 mg per vial (SKU GT600), for laboratory research only. Lot number, physical form, which form is supplied (reduced or oxidized) and the storage statement will all come with each batch record when it is published. For general background on how dry peptide material is kept, see peptide storage.

03 Glutathione Sequence and Molecular Information

The sequence is gamma-Glu-Cys-Gly. L-glutamate links through its gamma carboxyl to L-cysteine, and L-cysteine joins glycine through an ordinary peptide bond. The one-letter shorthand ECG hides that gamma bond and can mislead (see one-letter vs. three-letter amino acid codes), so we use the full name.

What amino acids make up glutathione?

Three amino acids: glutamate (glutamic acid), cysteine and glycine. Each has a job. Glutamate provides the free alpha-amino and alpha-carboxyl groups at one end. Cysteine provides the thiol (-SH) group, and that thiol drives most of the molecule's chemistry. Glycine supplies the C-terminal carboxyl. Our amino acids page covers these building blocks in more depth.

04 Reduced vs Oxidized Glutathione

Reduced glutathione (GSH) carries a free thiol on its cysteine. The oxidized form (GSSG) is two GSH molecules linked by a disulfide bond between their cysteines. These are different molecules, with different formulas, weights and identifiers.

Most of the glutathione peptide's chemistry comes down to switching between the two. Two thiols lose two hydrogens and form one disulfide; the reverse reaction gives the thiols back. GSH oxidizes when exposed to air, especially in solution. That makes the GSH to GSSG ratio a basic quality attribute for any material of this kind, and biochemists track the same ratio as a core measurement in their own experiments ^[2][4].

05 Published Research on Glutathione

The literature on the glutathione peptide is enormous. It covers more than a century of biochemistry, from the first chemical characterization through enzymology to analytical methods, and the main reviews group it into a few themes.

• Biosynthesis (review): it is assembled in two ATP-dependent steps, first by glutamate-cysteine ligase forming gamma-glutamylcysteine, then by glutathione synthetase adding glycine ^[3].
• Biochemical roles and metabolism (review): classic reviews describe its thiol-disulfide chemistry, its use as a substrate by enzyme families such as glutathione S-transferases, and the gamma-glutamyl pathway of its turnover ^[1][2].
• Measurement (review of analytical methods): a detailed review compares methods for determining GSH and GSSG in biological samples, including HPLC with various detectors and derivatization strategies ^[4].

All of this is basic biochemistry in cells and tissues. None of it is evidence about any research material, and preclinical findings should not be read as establishing safety or effectiveness in humans.

06 How Is Glutathione Analyzed?

HPLC does most of the work in characterizing the glutathione peptide, with mass spectrometry confirming identity. Analysts watch the oxidized form closely as a related substance.

The molecule is hard to see by UV. It has no aromatic residues, so HPLC methods either detect at low wavelengths or derivatize the thiol or amine group to boost the signal ^[4]. On a raw-material chromatogram, analysts look for GSSG and for related substances such as the dipeptides gamma-glutamylcysteine and cysteinylglycine.

By mass spectrometry, GSH gives a protonated ion near m/z 308.09 and GSSG one near m/z 613.16 (both calculated from PubChem monoisotopic masses). Notice the 305 Da gap between them. It isn't a simple doubling, because two hydrogens are lost when the disulfide forms.

07 Glutathione COA and Batch Documentation

Each Vinnix 600 mg batch of the glutathione peptide will be documented with a certificate of analysis linking the vial to its test results, published by batch number in the COA Library. Each report is expected to list:

• Lot number, quantity per vial and test date
• Form supplied (reduced or oxidized)
• HPLC purity, including GSSG (oxidized form) content
• Identity confirmation and the methods used

Need help with a specific field? Try Certificate of Analysis and Peptide Testing. To see where tripeptides sit in the wider peptide family, read What Are Peptides? or look at GHK-Cu, another tripeptide in the catalog.

REFScientific references

1. Meister A, Anderson ME. Glutathione. Annu Rev Biochem. 1983;52:711-760. PubMed 6137189
   review
2. Forman HJ, Zhang H, Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med. 2009;30(1-2):1-12. PubMed 18796312
   review
3. Lu SC. Glutathione synthesis. Biochim Biophys Acta. 2013;1830(5):3143-3153. PubMed 22995213
   review
4. Monostori P, Wittmann G, Karg E, Turi S. Determination of glutathione and glutathione disulfide in biological samples: an in-depth review. J Chromatogr B Analyt Technol Biomed Life Sci. 2009;877(28):3331-3346. PubMed 19560987
   review (analytical methods)