If you have been reading about AEDG and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Updated 2026-06-28. Numbers and descriptions here follow the published literature rather than marketing material.
Epitalon is a synthetic tetrapeptide with the amino acid sequence alanine-glutamate-aspartate-glycine, abbreviated Ala-Glu-Asp-Gly or AEDG. It was developed by the Russian researcher Vladimir Khavinson and colleagues during work on peptide bioregulators derived from the pineal gland. The compound is short enough to be produced by standard solid-phase peptide synthesis and is typically handled as a lyophilized white powder. Its small size distinguishes it from larger pineal peptides such as epithalamin, a complex extract from which the tetrapeptide was conceptually derived.
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.
Epitalon is a synthetic tetrapeptide whose sequence is alanine–glutamate–aspartate–glycine, commonly abbreviated AEDG. It was developed in Russia during the 1980s and 1990s by investigators associated with the St. Petersburg Institute of Bioregulation and Gerontology, who studied short peptides as regulators of gene expression and tissue function. The alternative spelling epithalon appears interchangeably in the literature, and the two names refer to the same molecule. Outside Russia it is encountered chiefly as a research chemical rather than a licensed medicine, and it holds no approval from the United States Food and Drug Administration or the European Medicines Agency.
The peptide is a synthetic analogue of epithalamin, a preparation extracted from bovine pineal glands. Investigators sought a short, chemically defined molecule that would reproduce some of the endocrine and gerontological observations attributed to the glandular extract. Proposed mechanisms centre on induction of telomerase activity, an effect reported in cultured human somatic cells in the early 2000s, together with influences on melatonin secretion and neuroendocrine regulation. Those mechanisms remain incompletely characterised, and the reported telomerase response has not been consistently reproduced by independent groups working in comparable systems.
Published work on this compound consists mainly of in vitro experiments, animal studies, and small clinical investigations, a substantial share of which appeared in Russian-language journals. Sample sizes are generally small, control conditions differ between studies, and several endpoints rely on markers whose clinical meaning is itself debated. Reviews of the longevity field treat the peptide as an early example of telomerase-directed research rather than an established intervention. Regulatory treatment varies by country: some jurisdictions place it under prescription controls, others treat it as a laboratory material, and importation may be restricted regardless of local status.
| Property | Value | Notes |
|---|---|---|
| Amino acid sequence | Ala-Glu-Asp-Gly | Tetrapeptide, often abbreviated AEDG |
| Molecular formula | C14H22N4O9 | Free peptide, unmodified termini |
| Molecular weight | ~390.35 Da | Calculated for the free acid form |
| Appearance | White to off-white powder | Typical lyophilized product form |
| Solubility class | Freely soluble in water | Two acidic residues dominate ionic character |
Epitalon is the common name for a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, usually abbreviated AEDG. All four residues are proteinogenic amino acids, and the free peptide has a calculated mass near 390 grams per mole. Because the chain is short and carries no modifications, it is assembled readily by solid-phase synthesis and is distributed mainly as a freeze-dried solid for laboratory work. Catalogue listings use the spellings epitalon, epithalone, and simply AEDG, and the three refer to the same sequence.
The compound is generally presented as a synthetic fragment of epithalamin, a pineal gland extract investigated in the former Soviet Union from the 1970s onward. Vladimir Khavinson and colleagues in Saint Petersburg developed short peptides modelled on such extracts, and epitalon became the most widely cited of those sequences. Most primary reports appeared in Russian-language journals or in proceedings with limited international circulation. Independent replication in laboratories outside that network remains sparse, and much repeated secondary material traces back to a small number of originating groups.
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== Bibliography == Wergedahl, H; Liaset, B; Gudbrandsen, OA; Lied, E; Espe, M; Muna, Z; Mørk, S; Berge, RK (2004). "Fish protein hydrolysate reduces plasma total cholesterol, increases the proportion of HDL cholesterol, and lowers acyl-CoA:cholesterol acyltransferase activity in liver of Zucker rats". The Journal of Nutrition. 134 (6): 1320–7. doi:10.1093/jn/134.6.1320. PMID 15173391. Wu, Hui-Chun; Chen, Hua-Ming; Shiau, Chyuan-Yuan (2003). "Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus)". Food Research International. 36 (9–10): 949–957. doi:10.1016/S0963-9969(03)00104-2. INIST 15251156. Marchbank, T.; Limdi, J. K.; Mahmood, A.; Elia, G.; Playford, R. J. (2008). "Clinical trial: Protective effect of a commercial fish protein hydrolysate against indomethacin (NSAID)-induced small intestinal injury". Alimentary Pharmacology & Therapeutics. 28 (6): 799–804. doi:10.1111/j.1365-2036.2008.03783.x. PMID 19145735. S2CID 31397. Nesse, Knut Olav; Nagalakshmi, A. P.; Marimuthu, P.; Singh, Mamta (2011). "Efficacy of a Fish Protein Hydrolysate in Malnourished Children". Indian Journal of Clinical Biochemistry. 26 (4): 360–5. doi:10.1007/s12291-011-0145-z. PMC 3210250. PMID 23024471. Kristinsson, Hordur G.; Rasco, Barbara A. (2000). "Fish Protein Hydrolysates: Production, Biochemical, and Functional Properties". Critical Reviews in Food Science and Nutrition. 40 (1): 43–81. doi:10.1080/10408690091189266. PMID 10674201. S2CID 28085824. Webb, K. E.; Bergman, E. N. (1991).
Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Emmanuel Philibert, also known under the nickname of Iron Head (Testa 'd Fer), made Turin the capital of the Duchy of Savoy in 1563. Piazza Reale (named Piazza San Carlo today) and Via Nuova (current Via Roma) were added along with the first enlargement of the walls, in the first half of the 17th century; in the same period the Palazzo Reale (Royal Palace of Turin) was also built. In the second half of that century, a second enlargement of the walls was planned and executed, with the building of the arcaded Via Po, connecting Piazza Castello with the bridge on the Po through the regular street grid. In 1706, during the Battle of Turin, the French besieged the city for 117 days without conquering it. By the Treaty of Utrecht the Duke of Savoy acquired Sicily, soon traded for Sardinia, and part of the former Duchy of Milan, and obtained the title of King of Sardinia; thus Turin became the capital of a European kingdom. The architect Filippo Juvarra began a major redesign of the city; Turin had about 90,000 inhabitants at the time.
=== Postgraduate students === During the course of his career Sanger supervised more than ten PhD students, two of whom went on to also win Nobel Prizes. His first graduate student was Rodney Porter who joined the research group in 1947. Porter later shared the 1972 Nobel Prize in Physiology or Medicine with Gerald Edelman for his work on the chemical structure of antibodies. Elizabeth Blackburn studied for a PhD in Sanger's laboratory between 1971 and 1974. She shared the 2009 Nobel Prize in Physiology or Medicine with Carol W. Greider and Jack W. Szostak for her work on telomeres and the action of telomerase.
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Sources: en.wikipedia.org
Epitalon is a synthetic tetrapeptide composed of four amino acids: alanine, glutamate, aspartate, and glycine. It is written as Ala-Glu-Asp-Gly. The free peptide has a molecular weight of about 390 daltons and is normally supplied as a lyophilized powder.
No. Epitalon is chemically synthesized, not extracted. It was designed as a short synthetic fragment conceptually related to larger pineal peptides studied in the same research tradition, particularly the extract known as epithalamin. The two are distinct materials with different compositions.
The term bioregulator is used in this research tradition for short peptides proposed to influence gene expression or cell function. Epitalon is grouped with other synthetic short peptides under this label. The term reflects a proposed mechanism rather than an established drug classification.
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine–glutamate–aspartate–glycine, also written AEDG. It was developed in Russian gerontology research and is studied for proposed effects on telomerase, melatonin regulation, and neuroendocrine function. It is not an approved pharmaceutical in the United States or the European Union.