The short version of AEDG fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-08-01. Anything still debated is marked as such rather than presented as settled.
Chemically, the molecule consists of four amino acid residues joined by three peptide bonds, with a free N-terminal amino group and a free C-terminal carboxyl group. Its molecular formula is C14H22N4O9, and its monoisotopic mass is approximately 390 daltons. The acidic glutamate and aspartate side chains give the peptide a net negative charge near neutral pH, a property that shapes its chromatographic behaviour and solubility profile. No disulfide bridges or other post-translational modifications are present, so the primary sequence alone defines the structure.
Most experimental work has been carried out in cell culture and animal models. Several reports describe changes in telomerase activity and proliferation in cultured cells, while rodent studies have examined lifespan, melatonin rhythm and reproductive endpoints. Human data remain limited, and much of the published clinical material consists of small trials with incomplete reporting of methods and controls. Whether the cell and animal findings translate into measurable effects in people is an open question, and the mechanistic basis of the reported telomerase changes is not fully established.
Discussions in the literature often conflate three distinct entities: the pineal extract epithalamin, the isolated tetrapeptide AEDG, and commercial preparations sold under similar names. Reviews citing older Russian-language studies sometimes omit detail on purity, route of administration and control groups, which makes cross-study comparison difficult. Researchers working with the compound generally note the need for independent replication, standardized enzyme assays, and clearer reporting of peptide identity. These caveats are relevant when weighing claims that appear in secondary sources rather than in primary reports.
Epitalon is a synthetic tetrapeptide whose sequence is alanine-glutamate-aspartate-glycine, written in single-letter code as AEDG. The four residues are joined by three peptide bonds, giving a linear backbone with no branching and no disulfide bridges. Its calculated molecular mass for the free form is approximately 390.3 daltons, a figure that rises when the compound is supplied as an acetate or trifluoroacetate salt. Because the chain is short, the molecule is defined entirely by its residue order rather than by any folded three-dimensional structure.
The compound is described in the literature as a derivative of epithalamin, a preparation obtained from bovine pineal tissue. Work on this peptide family was carried out mainly by a research group in Saint Petersburg beginning in the 1980s, and the substance was later registered for clinical use in Russia under the name Epitalon. Outside that region it is generally treated as a research chemical rather than an approved medicine. Statements about its biological activity rest on a relatively small number of studies, and independent replication remains limited.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Linear tetrapeptide | Four residues joined by three peptide bonds |
| Sequence | Ala-Glu-Asp-Gly | Commonly abbreviated AEDG |
| Molecular formula | C14H22N4O9 | Free acid form |
| Monoisotopic mass | Approximately 390 Da | Matches values reported from mass spectrometry |
| Net charge near neutral pH | Negative | Contributed by glutamate and aspartate side chains |
Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. It was designed at the St. Petersburg Institute of Bioregulation and Gerontology as a short, chemically defined analogue of epithalamin, a fraction obtained from bovine pineal tissue. Small peptide bioregulators of this type formed a long-running line of work there from the 1980s onward. Because the molecule is produced by solid-phase synthesis rather than extraction, its composition is exact and its purity can be measured directly.
The most frequently cited proposed action is induction of telomerase, the enzyme that adds repeat sequences to chromosome ends. Cell-culture work from the originating group reported higher telomerase reverse transcriptase expression and measurable telomere elongation in human somatic cells after exposure. How a four-residue peptide would reach nuclear gene regulation is not established, and no cell-surface receptor or uptake route has been identified. Additional reports describe changes in melatonin secretion, antioxidant enzyme activity and lipid peroxidation in aged animals, but these findings remain mechanistically unconnected to the telomerase observation.
Published evidence comes mainly from Russian-language journals and from a single research group, with small sample sizes and limited independent replication. A few laboratories outside that group have examined related peptides and reported weaker or absent telomerase effects, so the central claim is best described as contested rather than settled. Rodent studies report modest changes in some ageing markers and in survival, but designs vary and control conditions are often sparse. No large randomised trial in humans has been published, and long-term safety data in healthy populations are correspondingly thin.
Puillandre, N.; Meyer, C.P.; Bouchet, P.; Olivera, B.M. (2011). "Genetic divergence and geographical variation in the deep-water Conus orbignyi complex (Mollusca: Conoidea)". Zoologica Scripta. 40 (4): 350–363. doi:10.1111/j.1463-6409.2011.00478.x. PMC 3123138. PMID 21712968. Puillandre, N.; Duda, T.F.; Meyer, C.; Olivera, B.M.; Bouchet, P. (2015). "One, four or 100 genera? A new classification of the cone snails". Journal of Molluscan Studies. 81 (1): 1–23. doi:10.1093/mollus/eyu055. PMC 4541476. PMID 26300576. Puillandre, N.; et al. (2014). "Molecular phylogeny and evolution of the cone snails (Gastropoda, Conoidea)". Mol. Phylogenet. Evol. 78: 290–303. Bibcode:2014MolPE..78..290P. doi:10.1016/j.ympev.2014.05.023. PMC 5556946. PMID 24878223. Reeve L (1844). "Conchologia Iconica". Monograph of the genus Conus. Vol. 1. pp. 40–47. Sowerby, G. B., II. 1833. Conus. Conchological Illustrations pls. 36–37 Taylor, J. D.; Kantor, Yu. I.; Sysoev, A. V. (1993). "Foregut anatomy, feeding mechanisms, relationships and classification of Conoidea (Toxoglossa) (Gastropoda)". Bull. Nat. Hist. Mus. 59: 125–169. Tenorio MJ, Tucker JK, Chaney HW (2012). "The Families Conilithidae and Conidae. The Cones of the Eastern Pacific". In Poppe GT, Groh K (eds.). A Conchological Iconography. Hackenheim: ConchBooks. p. 112. Tucker J.K. & Tenorio M.J. (2009), Systematic Classification of Recent and Fossil Conoidean Gastropods, ConchBooks, Hankenheim, Germany, 295 pp. Van Mol JJ, Tursch B, Kempf M (1967). "Mollusques prosobranches: Les Conidae du Brésil.
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Sources: en.wikipedia.org
and Mw is the molecular mass. This plot acts as a calibration curve, which is used to approximate the desired compound's molecular weight. The Ve component represents the volume at which the intermediate molecules elute such as molecules that have partial access to the beads of the column. In addition, Vt is the sum of the total volume between the beads and the volume within the beads. The Vo component represents the volume at which the larger molecules elute, which elute in the beginning. Disadvantages are, for example, that only a limited number of bands can be accommodated because the time scale of the chromatogram is short, and, in general, there must be a 10% difference in molecular mass to have a good resolution.
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Sources: en.wikipedia.org
It is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, often abbreviated AEDG. The molecule is linear and contains no modified residues, so it is fully described by its sequence.
The compound came out of work on epithalamin, a peptide preparation derived from pineal tissue, conducted largely in Russian laboratories. Later studies in other countries examined it mainly in cell cultures and animal models.
The tetrapeptide sequence is a synthetic construct rather than a described circulating peptide. It was derived by analogy to peptide fractions obtained from tissue extracts, not isolated from blood or tissue as such.
The peptide contains four residues in the order alanine, glutamate, aspartate and glycine, abbreviated AEDG. The chain is linear and held together by three peptide bonds. Its calculated mass for the uncharged free form is about 390.3 daltons.