Epitalon, also spelled Epithalon, is the synthetic tetrapeptide Ala-Glu-Asp-Gly (AEDG). It was designed by Vladimir Khavinson's group at the St. Petersburg Institute of Bioregulation and Gerontology from the amino acid composition of epithalamin, an extract of bovine pineal gland. It is not approved as a medicine by the FDA or, as far as published reviews report, anywhere else, and most of the research on it comes from a single group.
Much of what is written about Epitalon online is built on a small number of cell and animal studies. This profile keeps to what can be checked: the molecule's identity, its history, what the telomerase studies actually measured, where the evidence is thin, and how to handle the peptide in the lab.
Epitalon at a glance
| Property | Value |
|---|---|
| Sequence | Ala-Glu-Asp-Gly |
| One-letter code | AEDG |
| Length | 4 residues |
| Molecular formula | C14H22N4O9 |
| Molecular weight | 390.35 g/mol |
| CAS number | 307297-39-8 |
| PubChem CID | 219042 |
| Other names | Epithalon, Epithalone, AEDG peptide |
| Related extract | Epithalamin (bovine pineal extract) |
| Charge at neutral pH | Net negative (three carboxyl groups) |
| Oxidation-prone residues | None |
| Regulatory status | Not an approved medicine |
Formula, weight, CAS and CID values are from the PubChem record for Epitalon. Catalog material is described on the Epithalon page.
Where Epitalon came from
Epitalon grew out of research at the St. Petersburg Institute of Bioregulation and Gerontology on peptide extracts of animal organs. One of those extracts, epithalamin, was prepared from bovine pineal gland. According to a 2025 review in the International Journal of Molecular Sciences, the tetrapeptide was synthesized based on an amino acid composition analysis of epithalamin, with the work led by V. K. Khavinson and V. N. Anisimov, and was patented around 2000.
The same review notes a later development: the AEDG sequence was reported in 2017 to have been detected in pineal gland extract itself. Before that, it was a designed molecule based on the extract's composition rather than a peptide known to be present in it.
The approach is the same one this group applied to other tissues, producing short synthetic peptides associated with an organ extract. Anhydrolabs also lists other peptides from this tradition, including Pinealon and Thymalin. Other Russian research peptides with a different origin, Selank and Semax, are compared in Selank vs Semax.
The telomerase studies, described neutrally
Epitalon is best known for reports that it affects telomerase, the enzyme that adds repeats to the ends of chromosomes. Two studies define the discussion.
Khavinson and colleagues, 2003
In a short 2003 report in the Bulletin of Experimental Biology and Medicine, Khavinson, Bondarev and Butyugov added Epitalon to cultures of telomerase-negative human fetal fibroblasts. They reported expression of the telomerase catalytic subunit, telomerase enzymatic activity and telomere elongation in the treated cultures. The report is three pages long, and it comes from the group that developed the peptide. The authors' broader interpretation went beyond what a single cell-culture experiment can show, and it is not repeated here.
Al-dulaimi and colleagues, 2025
A 2025 study in Biogerontology, from Brunel University London, examined Epitalon in four human cell lines: two normal lines (IBR.3 fibroblasts and HMEC mammary epithelial cells) and two breast cancer lines (21NT and BT474). The authors measured:
- telomere length by quantitative PCR;
- telomerase activity by the TRAP assay;
- expression of hTERT, the telomerase catalytic subunit, by quantitative PCR;
- alternative lengthening of telomeres (ALT), a telomerase-independent mechanism, by C-circle assay and PML body immunofluorescence.
They reported longer telomeres in both normal and cancer lines. In the normal lines this was accompanied by increased hTERT expression and telomerase activity. In the cancer lines, telomerase activity did not change significantly, and the authors instead reported signs of ALT activity. They noted that the work was done in two-dimensional cultures and that three-dimensional cultures and animal models are needed.
What these studies do and do not show
| Question | What the evidence says |
|---|---|
| Does Epitalon change telomerase activity in cultured cells? | Reported in fetal fibroblasts (2003) and in two normal lines (2025) |
| Does it change telomere length in cultured cells? | Reported in both studies, by different methods |
| Is the mechanism the same in every cell type? | No; the 2025 study reported telomerase in normal lines and ALT activity in cancer lines |
| Has it been replicated outside the originating group? | Partly; the 2025 study is independent |
| Does this say anything about people? | No; these are cell-culture findings |
The finding in cancer lines deserves attention in its own right. ALT is one of the ways tumor cells maintain telomeres, so an increase in ALT markers in cancer lines is a question to investigate, not a reassurance.
Other research areas
The 2025 review groups the rest of the Epitalon literature into several areas, most of them from the originating institute:
- Pineal and melatonin research, following from the epithalamin origin.
- Antioxidant activity in cell and animal systems.
- Gene expression, including reports of changes in interleukin-2 and circadian genes.
- Chromatin and DNA interaction. The 2025 Biogerontology paper summarizes earlier reports that AEDG binds preferentially to methylated cytosine in DNA and interacts with histones H1.3 and H1.6.
The review's own assessment is cautious. It states that physico-chemical and structural studies of the peptide remain limited, that most work comes from one group, and that data on toxicity, genotoxicity and carcinogenic potential are lacking.
How to read claims about Epitalon
Four questions sort most of what is written about this peptide.
What system was it? Cell culture, animal model or person. The telomerase work discussed above is cell culture. Findings do not transfer automatically from one level to the next, and statements about people that rest on cell data should be treated as extrapolation.
Who did the work? Much of the literature comes from the institute that developed the peptide, and its authors say so. Independent studies, such as the 2025 Brunel work, carry particular weight because they test whether a finding holds up elsewhere.
What exactly was measured? "Telomerase activation" can mean mRNA for hTERT, enzyme activity in a TRAP assay, or telomere length, and these do not always move together. The 2025 cancer-line data are an example: telomeres lengthened without a significant change in telomerase activity.
Was it the same molecule? Epitalon is a defined tetrapeptide; epithalamin is a tissue extract. Papers on one are not evidence about the other. The same distinction applies to other organ extracts; for a porcine brain example, see our profile of Cerebrolysin, and for a thymus-derived peptide with a well-defined sequence, see thymosin alpha-1.
Chemistry of a very short acidic peptide
At four residues, Epitalon is among the smallest peptides in any catalog. Two of its four side chains (Glu and Asp), plus the C terminus, carry carboxyl groups, and only the N-terminal amine carries a positive charge, so it is highly polar and carries a net negative charge at neutral pH. There is no methionine, cysteine or tryptophan, so oxidation is not a practical concern.
The sequence contains one well-known weak point: an Asp-Gly bond. Asp-Gly is the classic site for aspartimide formation, both during solid-phase synthesis and in solution. The cyclic aspartimide can reopen to give isoaspartate, a structural isomer with the same mass as the intended peptide. Because the mass is unchanged, mass spectrometry alone will not detect it; HPLC separation is needed. For background on the backbone chemistry, see the peptide bond.
The 2025 review also notes that Epitalon is supplied as a free base or as a salt with acetate or trifluoroacetate counter-ions. For a peptide this small, the counter-ion is a noticeable share of the solid: a single acetate (about 60 g/mol) is roughly 13% of the mass of an Epitalon monoacetate. That is why net peptide content, stated on the certificate, matters when exact molar concentrations are needed.
Laboratory handling
Anhydrolabs supplies Epitalon as a lyophilized powder in vacuum-sealed vials, and also as 10-vial kits. Each vial is labeled by net content (for example, 10 mg).
Dissolving. Epitalon dissolves readily in water and in neutral buffers. Its acidity means that a solution in unbuffered water may be mildly acidic; check the pH if the assay is sensitive to it. Stock solutions are described by concentration, for example 1 mg/mL, which is about 2.56 mM at 390.35 g/mol before any correction for salt and water content.
Storage. Keep lyophilized vials at -20 °C, dry and away from light. In solution, the Asp-Gly site is the main route of slow change, and it proceeds faster at higher temperature and at neutral to basic pH. Aliquot stock solutions, freeze them and avoid repeated thawing. See how long peptides last for general stability guidance.
Purity and identity. Purity by HPLC is reported as the area of the principal peak relative to all integrated signals. Mass spectrometry confirms the 390 Da parent mass, but, as noted above, isoaspartate forms share that mass, so a clean mass spectrum does not rule them out.
All Anhydrolabs material is supplied for in-vitro laboratory research only; see research use.
