If you have been reading about epitalon 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 2025-07-31. 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 with the residue sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its monoisotopic mass is approximately 390.35 daltons, and it is usually supplied as a lyophilised trifluoroacetate or acetate salt. The compound was derived from a pineal gland extract called epithalamin, a heterogeneous preparation investigated in the former Soviet Union. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology described the tetrapeptide as a constituent fragment of that extract. Commercial material is offered as a laboratory reagent rather than as a finished pharmaceutical product.
Literature searches for this compound must account for several spelling variants. Indexing databases contain epitalon, epithalon, epithalone, and AEDG, and relevant records are scattered across Russian-language and English-language journals that do not consistently cross-cite. Early publications describe the parent extract as a mixture of many peptides, whereas later work addresses the single synthetic tetrapeptide. That shift in nomenclature complicates comparison between studies, because extract data and tetrapeptide data are sometimes cited interchangeably. A search strategy omitting the alternate spellings will return an incomplete set of references.
Reported biological findings come mainly from cell culture and rodent experiments. Those studies describe changes in telomerase catalytic subunit expression, melatonin rhythm amplitude, and antioxidant enzyme activity after peptide exposure. Human data are sparse and consist of small trials with limited blinding and inconsistent endpoints. The proposed mechanisms remain hypotheses rather than established facts, and there is no consensus on whether effects observed in animals carry over to people. Independent replication outside the original research groups is limited, which is a recognised gap in the published literature.
| 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 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.
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.
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.
25. Adv Gerontol. 2008;21(1):61-7. [Investigation of antihypoxic properties of short peptides]. [Article in Russian] Kozina LS. The data presented suggest that short regulatory peptides (vilon, epitalon, vesugen and pinealon) have manifested the antihypoxic properties in the model of hypobaric hypoxia. Pinealon (Glu-Asp-Arg) has the most pronounced effect among them. The capability of pinealon to increase the neuronal resistance to hypoxic stress in experiments with prenatal hypoxia has a complex nature. It is based not so much on the inhibition of ROS increase in cells in response to stress as on stimulation of internal antioxidative enzyme system and possibly limiting the excitotoxic effect of N-methyl-D-aspartate.
24. Adv Gerontol. 2008;21(1):68-73. [Biological activity of regulatory peptides in model experiments in vitro]. [Article in Russian] Kozina LS, Arutiunian AV, Stvolinskiĭ SL, Khavinson VKh. Biological effects of short regulatory peptides, pinealon, vesugen, vilon and epitalon were studied in model experiments in vitro. These peptides were found not to demonstrate direct antioxidant activity but be able to restrict lipid peroxidation of human lipoproteins by modification of their structure. The short peptides increase stability of red blood cell membranes toward osmotic hemolysis. They also elevate the stationary level of intracellular reactive oxygen species and at the same time decrease (all excepting epitalon) percent of dead cells in neuronal population. The suggestion was made that under in vivo conditions, short peptides may participate in apoptosis/necrosis regulation.
35. Adv Gerontol. 2006;19:66-71. [Influence of light regimens, melatonin, and epitalon on amylase activity in the pancreas and small intestine in rats of different age]. [Article in Russian] Svechkina EB, Tiutiunnik NN, Vinogradova IA. The study shows that keeping rats in different light modes has a different impact on pancreatic and intestine amylase activity and has its peculiarities in regard of age as well as geroprotectors' influence on it. Melatonin use entails pancreatic amylase activity increase in mature animals in natural light of the North-West of Russia (NL) and 24-hour constant light (LD) and on the contrary amylase activity drops in case of using epitalon. Simultaneously, the enzyme activity in young and old rats under LD, melatonin and epitalon decreases. Intestine amylase activity influenced by both preparations rises in NL and drops in LD mode with respect to the control group.
Sources: pubmed.ncbi.nlm.nih.gov
15. Biofizika. 2014 Sep-Oct;59(5):1023-6. [Main mechanisms of rhabdomyolysis-caused kidney injury and their correction by organospecific peptides]. [Article in Russian] Zamorskiĭ II, Shchudrova TS. The influence of the organospecific peptides--kidney tripeptides T-31 and T-35, pineal tetrapeptide epitalon on the main mechanisms of kidney injury caused by experimental rhabdomyolysis--toxic injury of tubular cells, development of oxidative stress and energetic misbalance, leading to significant disturbances of the functional state of kidneys and development of acute kidney failure was studied. The renoprotective effect of oligopeptides realized by impact on all of the indicated mechanisms of kidney injury and confirmed by correlation between them was estimated.
1. Int J Pharm Compd. 2026 Jul-Aug;30(4):329-336. Synthetic Peptides in Pharmacy Compounding: Analysis of PCAC Recommendations and Industry Safety Standards. Willis J(1), Vu N(2)(3). Author information: (1)University of Oklahoma College of Pharmacy. (2)ARL Bio Pharma, Oklahoma City, Oklahoma. Nvu@arlok.com. (3)University of Oklahoma College of Pharmacy, Oklahoma City, Oklahoma. Compounded peptides have quickly moved from a niche topic to a growing area of interest among patients and prescribers. These products are promoted for a wide range of uses, including tissue repair, inflammation, metabolic health, and healthy aging. This article examines the proposed uses of these peptides, the concerns raised during the review, and the practical implications for compounders. Copyright© by International Journal of Pharmaceutical Compounding, Inc.
56. Neuro Endocrinol Lett. 2002 Aug;23(4):365-8. Pineal-regulating tetrapeptide epitalon improves eye retina condition in retinitis pigmentosa. Khavinson V(1), Razumovsky M, Trofimova S, Grigorian R, Razumovskaya A. Author information: (1)St. Petersburg Institute of Bioregulation and Gerontology, North-Western Branch of the Russian Academy of Medical Sciences, 3 Dynamo Project, 197110 St. Petersburg, Russia. ibg@medport.ru We have studied the effect of tetrapeptide Epitalon (Ala-Glu-Asp-Gly) on the course of congenital pigmented degeneration of the retina. The application of Epitalon in Campbell rats is found to intensify the bioelectric and functional activity of the retina due to the preservation of its morphological structure. Epitalon therapy in patients with degenerative retinal lesions results in a positive clinical effect in 90% of the cases. The analysis of Epitalon effects suggests that the tetrapeptide participates in the mechanisms of transcription common for the epiphysis and retina.
Sources: pubmed.ncbi.nlm.nih.gov
39. Izv Akad Nauk Ser Biol. 2001 Sep-Oct;(5):517-21. [Rhythm of protein synthesis in cultures of hepatocytes from rats of different ages. Norm and effect of the peptide livagen]. [Article in Russian] Brodskiĭ VIa, Khavinson VKh, Zolotarev IuA, Nechaeva NV, Malinin VV, Novikova TE, Gvazava IG, Fateeva VI. The circumhoralian rhythm of protein synthesis was determined in a monolayer culture of hepatocytes from rats at the age of 1 to 24 months and weighing from 45 to 480 g, respectively. The peptide lyvagen (Lys-Glu-Asp-Ala) obtained by directed chemical synthesis on the basis of amino acid analysis of the liver polypeptide preparations increased the level of protein synthesis in the hepatocytes from rats of different ages; the highest effect was observed in the cells of old animals. In old rats, lyvagen increased the amplitude of protein synthesis fluctuations. The peptide epitalon (Ala-Glu-Asp-Gly) constructed on the basis of analysis of the epiphysis peptides did not change the intensity of protein synthesis in the cultured hepatocytes.
42. Adv Gerontol. 2004;14:105-13. [The influence of substances revealing geroprotective of spontaneous carcinogenesis in mice]. [Article in Russian] Popovich IG. The review presents the results of experimental studies conducted by the author. CBA, SHR, HER-2/neu and SAM mice revealed inhibition of age-related alterations in estrus function and spontaneous tumour development and showed life span extension under the influence of the pineal gland hormone Melatonin, synthetic peptide bioregulator Epitalon, delta-sleep-inducing peptide Deltaran, enterosorbent Aqualen and succinic acid containing preparation Neuronol (Noogam). The observed effect depended on the dose and conditions of administration, as well as genetic predisposition of the particular mice strains to tumour development.
1. Int J Pharm Compd. 2026 Jul-Aug;30(4):329-336. Synthetic Peptides in Pharmacy Compounding: Analysis of PCAC Recommendations and Industry Safety Standards. Willis J(1), Vu N(2)(3). Author information: (1)University of Oklahoma College of Pharmacy. (2)ARL Bio Pharma, Oklahoma City, Oklahoma. Nvu@arlok.com. (3)University of Oklahoma College of Pharmacy, Oklahoma City, Oklahoma. Compounded peptides have quickly moved from a niche topic to a growing area of interest among patients and prescribers. These products are promoted for a wide range of uses, including tissue repair, inflammation, metabolic health, and healthy aging. This article examines the proposed uses of these peptides, the concerns raised during the review, and the practical implications for compounders. Copyright© by International Journal of Pharmaceutical Compounding, Inc.
Sources: pubmed.ncbi.nlm.nih.gov
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.
It is based on epithalamin, a peptide-rich preparation obtained from pineal gland tissue and studied in the former Soviet Union. Researchers later identified the tetrapeptide AEDG as a constituent fragment of that material. Modern supplies are produced by chemical synthesis rather than tissue extraction.