If you have been reading about epithalamin 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.
Last reviewed on 2025-11-14. Where a claim depends on a specific study, the study is described rather than over-claimed.
The compound is generally described as a synthetic analogue of a fragment isolated from a pineal gland extract. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology introduced it during the 1980s and 1990s while studying short peptides from animal tissue. The original extract, called epithalamin, is a heterogeneous mixture, whereas epitalon is a single defined sequence. That distinction matters because findings reported for the extract are not automatically findings about the pure tetrapeptide, and claims about broader biological effects remain a separate question from the chemical identity described here.
Residue composition is the property that most cleanly separates verified material from mislabelled samples. Alanine, glutamate, aspartate and glycine appear in that order from the N-terminus, and the two acidic residues sit in the middle of the chain. Because the peptide is short, it can be produced by solid-phase synthesis and characterised by mass spectrometry without ambiguity. Any reported sample whose measured mass departs substantially from 390 daltons is a different compound or a degraded mixture rather than epitalon.
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.
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 |
|---|---|---|
| Molecular formula | C14H22N4O9 | Derived from the four constituent residues |
| Molecular mass | About 390.35 Da | Monoisotopic value, confirmed by mass spectrometry |
| Residue sequence | Ala-Glu-Asp-Gly | Read from the N-terminus to the C-terminus |
| Common synonyms | Epithalon; AEDG | Both forms appear in reference catalogues |
| Net charge near neutral pH | Negative | Two acidic side chains give a low isoelectric point |
Several names circulate for the same molecule, including epitalon, epithalone, epithalamin tetrapeptide, and the sequence code AEDG. A CAS registry number, 307297-39-8, is commonly cited for it, though catalogue entries should be checked against supplier documentation because mislabelled records occur. In its usual form the peptide carries free amino and carboxyl termini and is neither glycosylated nor lipidated. Researchers distinguish the defined tetrapeptide from epithalamin itself, a crude pineal preparation containing many peptides that is not chemically characterised.
Material supplied for laboratory use is normally a lyophilised white to off-white powder that dissolves readily in water and in isotonic saline. Lyophilised cakes are hygroscopic and should be equilibrated to room temperature before opening to limit condensation on the solid. Solutions are typically prepared at milligram-per-millilitre concentrations and divided into single-use aliquots, because repeated freeze–thaw cycles degrade short peptides. Aqueous solutions are far less stable than the dry powder, and identity is usually verified by mass spectrometry alongside purity estimation from reversed-phase high-performance liquid chromatography.
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.
The mechanism involves oxidation of the selenol of a selenocysteine residue by hydrogen peroxide. This process gives the derivative with a selenenic acid (RSeOH) group. The selenenic acid is then converted back to the selenol by a two step process that begins with reaction with glutathione (GSH) to form the GS-SeR and water. A second GSH molecule reduces the GS-SeR intermediate back to the selenol, releasing glutathione disulfide (GS-SG) as the by-product. A simplified representation is shown below:
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5-HT2, 5-HT6, 5-HT7: antipsychotic effects, sedation/anxiolysis, antidepressant effect, weight gain D1, D2, D3, D4, D5: antipsychotic effects, sedation, extrapyramidal side effects, prolactin increase, depression, apathy/anhedonia, weight gain H1: sedation, weight gain Muscarinic acetylcholine receptors: anticholinergic effects, inhibition of extrapyramidal side effects α1-Adrenergic: hypotension, sedation, anxiolysis Because of its potent serotonin 5-HT2A and muscarinic acetylcholine receptor antagonism, chlorprothixene causes relatively mild extrapyramidal symptoms. This is in contrast to most other typical antipsychotics. For this reason, chlorprothixene has sometimes been described instead as an atypical antipsychotic. Chlorprothixene has also been found to act as FIASMA (functional inhibitor of acid sphingomyelinase).
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Sources: en.wikipedia.org
It has been suggested that mutations that increase iron absorption, such as the ones responsible for hemochromatosis (see below), were selected for during Neolithic times as they provided a selective advantage against iron-deficiency anemia. The increase in systemic iron levels becomes pathological in old age, which supports the notion that antagonistic pleiotropy or "hyperfunction" drives human aging. Chronic iron toxicity is usually the result of more chronic iron overload syndromes associated with genetic diseases, repeated transfusions or other causes. In such cases the iron stores of an adult may reach 50 grams (10 times normal total body iron) or more. The most common diseases of iron overload are hereditary hemochromatosis (HH), caused by mutations in the HFE gene, and the more severe disease juvenile hemochromatosis (JH), caused by mutations in either hemojuvelin (HJV) or hepcidin (HAMP). The exact mechanisms of most of the various forms of adult hemochromatosis, which make up most of the genetic iron overload disorders, remain unsolved. So, while researchers have been able to identify genetic mutations causing several adult variants of hemochromatosis, they now must turn their attention to the normal function of these mutated genes.
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HT-2157 (former development code SNAP-37889) is a drug which acts as a selective non-peptide antagonist for the receptor GAL-3, which is usually activated by the neuropeptide galanin. Blocking this receptor with HT-2157 produced increased serotonin release, as well as producing antidepressant and anxiolytic effects in animal studies, and it was also being researched for treatment of cognitive dysfunction. All human clinical trials were terminated due to safety concerns however, and new GAL-3 antagonists are now being sought instead.
Sources: en.wikipedia.org
It is a four-amino-acid peptide built from alanine, glutamate, aspartate and glycine in that order. Its formula is C14H22N4O9, and it is made by chemical synthesis rather than extracted from tissue. The synthetic peptide is a single defined molecule, unlike the pineal extracts it is often compared with.
No. The two spellings refer to the same tetrapeptide, and the difference reflects transliteration from Russian. Laboratories and catalogues use both forms interchangeably. The material is also indexed as AEDG, taken from the one-letter codes of its residues.
Epithalamin is a mixed preparation derived from animal pineal tissue and contains many peptides. Epitalon is one synthetic sequence chosen for study from that broader mixture. Statements about one do not transfer directly to the other.
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.