A practical reference on AEDG: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-07-15. Anything still debated is marked as such rather than presented as settled.
Laboratory-grade epitalon is typically supplied as a lyophilized powder. Purity is commonly assessed with reverse-phase high-performance liquid chromatography, often paired with mass spectrometry to confirm molecular identity. Amino acid analysis and peptide mapping can provide additional confirmation of sequence. Certificates of analysis for research materials frequently report purity above 95 percent, although the methods behind such figures vary between suppliers. The absence of a pharmacopeial monograph means that no single standardized assay defines the compound, so reported results depend on the analytical protocol chosen.
Storage recommendations center on limiting moisture, heat, and light. The dry powder is generally kept at minus 20 degrees Celsius, and some suppliers recommend minus 80 degrees for long-term archival. Once dissolved, solutions are usually aliquoted and frozen to avoid repeated freeze-thaw cycles, which can promote aggregation or degradation. Aqueous stability depends on pH and concentration, and buffered saline is often preferred over plain water for biological work. Stability data specific to epitalon remain limited, so general peptide-handling practices are applied by analogy rather than from product-specific validation.
Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and its calculated monoisotopic mass is approximately 390.35 daltons. The compound does not occur naturally as a free peptide; it is produced by solid-phase peptide synthesis. Because it contains two acidic residues and no basic residues, the neutral form carries a net negative charge at physiological pH. This charge profile influences how the peptide behaves in solution and during chromatographic analysis.
The most frequently cited laboratory finding is that AEDG increased telomerase activity and extended telomere length in cultured human somatic cells. That work used fetal fibroblast strains and reported changes in enzyme activity alongside altered division counts. Replication by unrelated groups has been limited, and the published record is largely a single-laboratory series rather than a multi-centre programme. The result supports a hypothesis about peptide influence on gene expression in cell culture; it does not by itself establish an effect on telomere length in living animals or in people.
Animal and clinical reports appear mainly in Russian-language journals from the 1990s and 2000s, covering endpoints such as melatonin rhythm, lifespan in aged rodents, and retinal function. Many of these papers involve small groups, lack blinding or placebo comparison, and are difficult to retrieve through indexed databases. Review articles published in English generally summarise the claims without reanalysing the underlying data. Because no large randomised trial exists, the clinical importance of these reported effects stays unresolved and is properly described as an open question.
No national medicines regulator has approved epitalon as a therapeutic product. It is generally distributed as a research chemical, and in some jurisdictions selling peptides for human consumption without approval is restricted or prohibited. Certificates of analysis accompanying commercial material vary in which tests are performed, and independent verification of identity and purity is uncommon. Statements about anti-ageing or disease-prevention benefits on vendor pages are marketing claims rather than regulatory findings, a distinction that shapes how the compound is discussed in scientific and popular sources alike.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Free acid form of the tetrapeptide |
| Molecular mass | About 390.35 Da | Calculated monoisotopic value |
| Appearance | White to off-white powder | Typical lyophilized presentation |
| Solubility | Soluble in water | Also dissolves in buffered saline |
| Storage temperature | Minus 20 degrees Celsius | Dry, dark conditions; avoid repeated thawing |
The four residues give epitalon a molecular formula of C14H22N4O9 and a molecular weight near 390.35 daltons. The presence of two acidic residues, glutamate and aspartate, makes the free peptide strongly acidic, while the alanine and glycine ends provide neutral, nonpolar character. This combination produces a molecule with substantial water solubility. Because there are no cysteine, methionine, or tryptophan residues, the peptide lacks the most common oxidation-sensitive side chains, which simplifies handling compared with many longer peptides.
The proposed relationship between epitalon and pineal function is a central part of its background. Khavinson's group reported that short peptides corresponding to regions of larger pineal proteins could influence gene expression in cells. Epitalon was framed as a synthetic analogue of an active fragment rather than a direct isolation product. Whether the tetrapeptide reproduces the effects of the parent extract is an open question, because comparative studies are limited and the parent extract itself is not a single defined substance.
Interest in epitalon is usually discussed within the broader field of short peptide bioregulators, a category that includes other synthetic di-, tri-, and tetrapeptides studied by the same research group. These compounds share a common rationale: that small fragments of tissue-derived proteins can retain biological activity and can be produced reproducibly. The category as a whole remains outside mainstream pharmacological consensus, and epitalon specifically has a limited presence in independent, non-Russian research literature, which shapes how its evidence base is described.
Stability depends strongly on pH, temperature and the presence of oxygen and trace metals. Cleavage of the backbone proceeds faster under neutral to alkaline conditions, whereas acidic solutions tend to slow that reaction. The aspartate and glutamate side chains can undergo deamidation or imide formation over time, generating closely related impurities. Published stability data specific to epitalon are sparse, so the usable life of a given solution is best regarded as an open question that depends on buffer composition, concentration and storage temperature.
Identity and purity are usually assessed by reversed-phase high-performance liquid chromatography with ultraviolet detection, frequently near 214 nanometers where the peptide bond absorbs. Mass spectrometry, most often with electrospray ionization, confirms the observed molecular mass and helps separate the intact peptide from truncated or modified forms. Amino acid analysis or tandem mass spectrometry can establish residue order. Purity is commonly quoted as an area percentage, yet such values are method-dependent, and comparisons between laboratories require matching column, gradient and detection wavelength.
Published studies on epitalon are dominated by a small number of research groups, and independent replication in other laboratories remains limited. Proposed mechanisms include activation of telomerase and modulation of melatonin rhythms, but the evidence for either rests mainly on cell cultures and animal models. Whether the peptide produces comparable effects in humans is an open question, and the absence of large controlled trials means the literature is best read as exploratory rather than settled.
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9, and its calculated molar mass is approximately 390.35 grams per mole. The compound is a short fragment related to a peptide fraction isolated from bovine pineal gland extracts, and it is normally supplied as a lyophilised powder intended for laboratory research. It is not a registered pharmaceutical product in most countries.
The peptide emerged from research carried out in Saint Petersburg from the late 1980s onward, where investigators searched for shorter active fragments of a pineal preparation known as epithalamin. The name epitalon was chosen to reflect that parent extract. Early reports described effects on neuroendocrine markers and on the lifespan of laboratory animals. Much of that work appeared in Russian-language journals, with English translations following later, which affects how readily the original protocols can be assessed by outside groups.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Epitalon is a synthetic tetrapeptide built from four amino acids: alanine, glutamate, aspartate, and glycine. It is not extracted from a natural source but made in the laboratory by chemical synthesis. Its short length makes it relatively straightforward to produce at high purity.
No naturally occurring free form of the peptide has been described. The four-amino-acid sequence can appear as a fragment within larger proteins, but that is not the same as the intact compound being present as a circulating molecule. Materials used in research are synthetic.
Purity is usually checked by reverse-phase high-performance liquid chromatography, which separates the target peptide from related impurities. Mass spectrometry is commonly used alongside it to confirm molecular mass. Some suppliers also provide amino acid analysis for additional sequence confirmation.
Small studies with human participants have been reported, chiefly in Russian-language journals, but they are limited in size and design. No large randomised controlled trial with published results is available.