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Epitalon Background And Nomenclature — 2026 Update

By Editorial Desk · published 2025-10-16 · last reviewed 2025-11-05 · Blog

AEDG peptide comes up often in conversation and rarely with the context attached. Here we lay out the basics in order, then work through the practical considerations.

Updated 2025-11-05. Numbers and descriptions here follow the published literature rather than marketing material.

Epitalon Background and Nomenclature

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.

Epitalon Structure and Research Origin

(TG:@pojiaai)Epitalon is a synthetic linear tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. It emerged from work on epithalamin, a peptide fraction prepared from bovine pineal tissue, and was designed as a short, chemically defined analogue of that extract. Early publications came mainly from Russian laboratories studying pineal peptides and aging-related endpoints. The compound appears in the literature under several spellings, including epithalon and epithalone, which complicates systematic searching. Its small size makes solid-phase assembly and routine analytical characterization straightforward.

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.

Epitalon at a glance

PropertyValueNotes
Molecular formulaC14H22N4O9Computed for the free acid of Ala-Glu-Asp-Gly
Molecular massAbout 390.35 g/molFree peptide; salt forms shift the value
AppearanceWhite to off-white solidTypical of short peptides after freeze-drying
Solubility classFreely soluble in waterAqueous buffers are also commonly used
Common synonymsEpitalon, epithalone, AEDGAEDG is the single-letter sequence

Identity and Research Background

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.

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.

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Background and Proposed Mechanism

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.

Epitalon Peptide Background and Structure

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.

Chemical Identity and Research Background

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.

In its supplied form epitalon is a white to off-white powder, usually lyophilized and often hygroscopic. It dissolves readily in water and in aqueous buffers, and it is commonly handled as the acetate or trifluoroacetate salt to improve stability during purification and drying. The amide backbone is labile in aqueous media, so solutions are less durable than the dry solid. Handling notes in the chemical literature therefore emphasize keeping the powder dry, cool and shielded from light until it is dissolved.

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.

Background from the literature

Guillain–Barré syndrome and its chronic counterpart, chronic inflammatory demyelinating polyneuropathy Anti-MAG peripheral neuropathy Charcot–Marie–Tooth disease and its counterpart Hereditary neuropathy with liability to pressure palsy Copper deficiency-associated conditions (peripheral neuropathy, myelopathy, and rarely optic neuropathy) Progressive inflammatory neuropathy

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Nandrolone, also known as 19-nortestosterone, is an endogenous androgen. It is also an anabolic steroid (AAS) which is medically used in the form of esters such as nandrolone decanoate (brand name Deca-Durabolin) and nandrolone phenylpropionate (brand name Durabolin). Nandrolone esters are used in the treatment of anemias, cachexia (muscle wasting syndrome), osteoporosis, breast cancer, and for other indications. They are now used by oral administration or instead are given by injection into muscle or fat. Side effects of nandrolone esters include symptoms of masculinization like acne, increased hair growth, and voice changes. They are synthetic androgens and anabolic steroids and hence are agonists of the androgen receptor (AR), the biological target of androgens like testosterone and dihydrotestosterone (DHT). Nandrolone has strong anabolic effects and weak androgenic effects, which give them a mild side effect profile and make them especially suitable for use in women and children. There are metabolites of Nandrolone that act as long-lasting prodrugs in the body, such as 5α-Dihydronandrolone. Nandrolone esters were first described and introduced for medical use in the late 1950s. They are among the most widely used anabolic steroid worldwide. In addition to their medical use, nandrolone esters are used to improve physique and performance, and are said to be the most widely used anabolic steroid for such purposes. The drugs are controlled substances in many countries and so non-medical use is generally illicit.

Torsten Krude (Ed.); DNA Changing Science and Society (ISBN 0-521-82378-1) CUP 2003. (The Darwin Lectures for 2003, including one by Sir Aaron Klug on Rosalind Franklin's involvement in the determination of the structure of DNA). Robert Olby; The Path to The Double Helix: Discovery of DNA; first published in October 1974 by MacMillan, with foreword by Francis Crick; ISBN 0-486-68117-3; revised in 1994, with a 9-page postscript. Robert Olby; Oxford National Dictionary article: Crick, Francis Harry Compton (1916–2004). In: Oxford Dictionary of National Biography, Oxford University Press, January 2008. Anne Sayre. 1975. Rosalind Franklin and DNA. New York: W.W. Norton and Company. ISBN 0-393-32044-8. James D. Watson; The Double Helix: A Personal Account of the Discovery of the Structure of DNA, Atheneum, 1980, ISBN 0-689-70602-2 (first published in 1968) is a very readable firsthand account of the research by Crick and Watson. The book also formed the basis of the award-winning television dramatisation Life Story by BBC Horizon (also broadcast as Race for the Double Helix). [The Norton Critical Edition, which was published in 1980, edited by Gunther S. Stent: ISBN 0-393-01245-X] James D. Watson; Avoid Boring People and Other Lessons from a Life in Science, New York: Random House. ISBN 978-0-375-41284-4.

Sources: en.wikipedia.org

Reference notes

Growth hormone secretagogues or GH secretagogues (GHSs) are a class of drugs which act as secretagogues (i.e., induce the secretion) of growth hormone (GH). They include agonists of the ghrelin/growth hormone secretagogue receptor (GHSR), such as ghrelin (lenomorelin), pralmorelin (GHRP-2), GHRP-6, examorelin (hexarelin), ipamorelin, and ibutamoren (MK-677), and agonists of the growth hormone-releasing hormone receptor (GHRHR), such as growth hormone-releasing hormone (GHRH, somatorelin), CJC-1295, sermorelin, and tesamorelin. Many of them also induce the secretion of insulin-like growth factor 1 (IGF-1), as well as of other hypothalamic-pituitary hormones such as prolactin and cortisol. The main clinical application of these agents is the treatment of growth hormone deficiency.

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== External links == Clinical trial number NCT03422653 for "A Study to Evaluate the Safety and Efficacy of CR845 in Hemodialysis Patients With Moderate-to-Severe Pruritus (KALM-1)" at ClinicalTrials.gov Clinical trial number NCT03636269 for "CR845-CLIN3103: A Global Study to Evaluate the Safety and Efficacy of CR845 in Hemodialysis Patients With Moderate-to-Severe Pruritus (KALM-2)" at ClinicalTrials.gov

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Sources: en.wikipedia.org

Reference notes

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== Generation of endocrine progenitor cells from pancreatic islets == Similar to generation of Cancer Stem Cells, EMT was demonstrated to generate endocrine progenitor cells from human pancreatic islets. Initially, the human islet-derived progenitor cells (hIPCs) were proposed to be better precursors since β-cell progeny in these hIPCs inherit epigenetic marks that define an active insulin promoter region. However, later, another set of experiments suggested that labelled β-cells de-differentiate to a mesenchymal-like phenotype in vitro, but fail to proliferate; thus initiating a debate in 2007. Since these studies in human islets lacked lineage-tracing analysis, these findings from irreversibly tagged beta cells in mice were extrapolated to human islets. Thus, using a dual lentiviral and genetic lineage tracing system to label β-cells, it was convincingly demonstrated that adult human islet β-cells undergo EMT and proliferate in vitro. Also, these findings were confirmed in human fetal pancreatic insulin-producing cells, and the mesenchymal cells derived from pancreatic islets can undergo the reverse of EMT – MET – to generate islet-like cell aggregates. Thus, the concept of generating progenitors from insulin-producing cells by EMT or generation of Cancer Stem Cells during EMT in cancer may have potential for replacement therapy in diabetes, and call for drugs targeting inhibition of EMT in cancer.

Choriogonadotropin subunit beta (CG-beta) also known as chorionic gonadotrophin chain beta is a protein that in humans is encoded by the CGB gene. This gene is a member of the glycoprotein hormone beta chain family and encodes the beta 3 subunit of chorionic gonadotropin (CG). Glycoprotein hormones are heterodimers consisting of a common alpha subunit and a unique beta subunit which confers biological specificity. CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene.

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Sources: en.wikipedia.org

Frequently asked questions

What is epitalon made of?

It is a four-amino-acid peptide with the sequence alanine-glutamate-aspartate-glycine. The chain is unmodified and contains only standard proteinogenic residues, which makes it straightforward to produce by solid-phase synthesis and to characterise by standard peptide methods.

Why do two spellings appear in the literature?

Epitalon and epithalon both circulate, and the difference reflects transliteration of a name coined in Russian-language publications. Reference to the extract it derives from, epithalamin, explains the shared stem. Databases and suppliers are inconsistent, so a search for one spelling alone may miss relevant entries.

Is epitalon the same substance as epithalamin?

No. Epithalamin is a multi-component preparation obtained from pineal tissue, and its exact composition is not fully characterised. Epitalon is a single defined tetrapeptide described as a short synthetic counterpart of that extract, so the two are related in origin but not interchangeable in identity.

What is epitalon chemically?

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.

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