If you have been reading about AEDG peptide 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 2026-01-30. Numbers and descriptions here follow the published literature rather than marketing material.
Laboratory work has examined effects on telomerase activity in cultured cells, on melatonin rhythms in animals, and on markers of oxidative stress. Some experiments report measurable changes while others show none, and the reported findings rest largely on small studies. The absence of large independent trials means the generality of these results is unresolved rather than settled. Review articles occasionally apply the label geroprotector, a term that reflects a research hypothesis about ageing rather than an established clinical finding.
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.
（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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Computed for the free acid of Ala-Glu-Asp-Gly |
| Molecular mass | About 390.35 g/mol | Free peptide; salt forms shift the value |
| Appearance | White to off-white solid | Typical of short peptides after freeze-drying |
| Solubility class | Freely soluble in water | Aqueous buffers are also commonly used |
| Common synonyms | Epitalon, epithalone, AEDG | AEDG is the single-letter sequence |
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 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.
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.
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.
=== Usage === To obtain the greatest benefits from its use as a sudorific, it was recommended that copious drafts of some warm and harmless drink be ingested after the use of the powder. It was an ingredient in John Wyeth & Brother, Inc.'s La Grippe (flu) pills, circa 1906.
Some drugs have the capacity to bind with certain types of proteins that are carried in blood plasma. This is important as only drugs that are present in the plasma in their free form can be transported to the tissues. Drugs that are bound to plasma proteins therefore act as a reservoir of the drug within the organism and this binding reduces the drug's final concentration in the tissues. The binding between a drug and plasma protein is rarely specific and is usually labile and reversible. The binding generally involves ionic bonds, hydrogen bonds, Van der Waals forces and, less often, covalent bonds. This means that the bond between a drug and a protein can be broken and the drug can be replaced by another substance (or another drug) and that, regardless of this, the protein binding is subject to saturation. An equilibrium also exists between the free drug in the blood plasma and that bound to proteins, meaning that the proportion of the drug bound to plasma proteins will be stable, independent of its total concentration in the plasma. In vitro studies carried out under optimum conditions have shown that the equilibrium between a drug's plasmatic concentration and its tissue concentration is only significantly altered at binding rates to plasma proteins of greater than 90%. Above these levels the drug is "sequestered", which decreases its presence in tissues by up to 50%.
=== Competitive === The binding of oxygen is affected by molecules such as carbon monoxide (for example, from tobacco smoking, exhaust gas, and incomplete combustion in furnaces). CO competes with oxygen at the heme binding site. Hemoglobin's binding affinity for CO is 250 times greater than its affinity for oxygen. Since carbon monoxide is a colorless, odorless, and tasteless gas, and poses a potentially fatal threat, carbon monoxide detectors have become commercially available to warn of dangerous levels in residences. When hemoglobin combines with CO, it forms a very bright red compound called carboxyhemoglobin, which may cause the skin of CO poisoning victims to appear pink in death, instead of white or blue. When inspired air contains CO levels as low as 0.02%, headache and nausea occur; if the CO concentration is increased to 0.1%, unconsciousness will follow. In heavy smokers, up to 20% of the oxygen-active sites can be blocked by CO. In similar fashion, hemoglobin also has competitive binding affinity for cyanide (CN−), sulfur monoxide (SO), and sulfide (S2−), including hydrogen sulfide (H2S). All of these bind to iron in heme without changing its oxidation state, but they nevertheless inhibit oxygen-binding, causing grave toxicity. The iron atom in the heme group must initially be in the ferrous (Fe2+) oxidation state to support oxygen and other gases' binding and transport (it temporarily switches to ferric during the time oxygen is bound, as explained above).
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Sources: en.wikipedia.org
However, β-strands are rarely perfectly extended; rather, they exhibit a twist. The energetically preferred dihedral angles near (φ, ψ) = (–135°, 135°) (broadly, the upper left region of the Ramachandran plot) diverge significantly from the fully extended conformation (φ, ψ) = (–180°, 180°). The twist is often associated with alternating fluctuations in the dihedral angles to prevent the individual β-strands in a larger sheet from splaying apart. A good example of a strongly twisted β-hairpin can be seen in the protein BPTI. The side chains point outwards from the folds of the pleats, roughly perpendicularly to the plane of the sheet; successive amino acid residues point outwards on alternating faces of the sheet.
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1978 Genentech produces biosynthetic human insulin in Escherichia coli bacteria using recombinant DNA techniques, licenses to Eli Lilly 1981 Novo Nordisk chemically and enzymatically converts porcine to human insulin 1982 Genentech synthetic human insulin (above) approved 1983 Eli Lilly and Company produces biosynthetic human insulin with recombinant DNA technology, Humulin 1985 Axel Ullrich sequences a human cell membrane insulin receptor. 1988 Novo Nordisk produces recombinant biosynthetic human insulin 1996 Lilly Humalog "lispro" insulin analogue approved. 2000 Sanofi Aventis Lantus insulin "glargine" analogue approved for clinical use in the US and the EU. 2004 Sanofi Aventis Apidra insulin "glulisine" insulin analogue approved for clinical use in the US. 2006 Novo Nordisk Levemir "detemir" insulin analogue approved for clinical use in the US. 2008 Abbott laboratories " FreeStyle Navigator CGM" gets approved. 2013 The US Food and Drug Administration (FDA) requested more cardiac safety tests for Insulin degludec. 2015 Insulin degludec was approved by the FDA in September 2015.
== Clinical significance == Some can be useful in measuring rates of metabolic processes (for example, 3,4-dihydroxyphenylacetic acid or 3-aminoisobutyrate). Because they can represent unnatural points of entry into natural metabolic pathways, some (such as AICA ribonucleotide) are of interest to researchers in developing new therapies.
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Sources: en.wikipedia.org
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.
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.
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.
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.