This is a working overview of epithalamin, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2025-11-20. Anything still debated is marked as such rather than presented as settled.
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9, and its calculated molar mass is approximately 390.35 grams per mole. The compound is a short fragment related to a peptide fraction isolated from bovine pineal gland extracts, and it is normally supplied as a lyophilised powder intended for laboratory research. It is not a registered pharmaceutical product in most countries.
The peptide emerged from research carried out in Saint Petersburg from the late 1980s onward, where investigators searched for shorter active fragments of a pineal preparation known as epithalamin. The name epitalon was chosen to reflect that parent extract. Early reports described effects on neuroendocrine markers and on the lifespan of laboratory animals. Much of that work appeared in Russian-language journals, with English translations following later, which affects how readily the original protocols can be assessed by outside groups.
Published studies on epitalon are dominated by a small number of research groups, and independent replication in other laboratories remains limited. Proposed mechanisms include activation of telomerase and modulation of melatonin rhythms, but the evidence for either rests mainly on cell cultures and animal models. Whether the peptide produces comparable effects in humans is an open question, and the absence of large controlled trials means the literature is best read as exploratory rather than settled.
Verification of a sample usually begins with reversed-phase high-performance liquid chromatography, which resolves the peptide from truncated sequences and other impurities and expresses purity as a percentage of total peak area. Mass spectrometry by electrospray ionisation or matrix-assisted laser desorption supplies an independent check, because the measured mass can be compared against the theoretical value for AEDG. Amino acid analysis or tandem mass spectrometry sequencing can confirm residue order. Each of these methods answers a different question: a purity figure does not establish identity, and an identity match does not establish how much of the material is intact peptide.
The molecule is a short, linear, hydrophilic peptide that dissolves readily in water or aqueous buffer. Its principal chemical liabilities are hydrolytic rather than oxidative, since it contains no cysteine, methionine, or tryptophan residues. The aspartate–glycine step is a recognised site for aspartimide formation under mildly acidic or basic conditions, generating isoaspartate and succinimide-related products over time. Desiccated lyophilised powder held at −20 °C is comparatively stable, whereas dilute solutions degrade faster and are best frozen as single-use aliquots rather than thawed repeatedly.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Derived from the four-residue sequence |
| Molar mass | About 390.35 g/mol | Free peptide, counter-ion not included |
| Appearance | White to off-white powder | Lyophilised solid from aqueous solution |
| Water solubility | Freely soluble | Short, polar peptide chain |
| Common synonyms | AEDG; epithalone | Catalogues use the names interchangeably |
Interest in epitalon is usually discussed within the broader field of short peptide bioregulators, a category that includes other synthetic di-, tri-, and tetrapeptides studied by the same research group. These compounds share a common rationale: that small fragments of tissue-derived proteins can retain biological activity and can be produced reproducibly. The category as a whole remains outside mainstream pharmacological consensus, and epitalon specifically has a limited presence in independent, non-Russian research literature, which shapes how its evidence base is described.
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.
Solubility is high in water, phosphate-buffered saline and normal saline, a pattern that follows from the two acidic residues in the chain. The peptide dissolves poorly in non-polar solvents such as hexane or chloroform. Stock solutions are often prepared in water first and then diluted into the buffer of interest. Because the molecule is small and hydrophilic, filtration through a low-protein-binding membrane is usually straightforward, and visible particulates are uncommon in freshly made solutions.
Identity and purity are established with reversed-phase high-performance liquid chromatography and mass spectrometry. The chromatogram shows the main peak and any truncated or oxidised by-products, while the mass spectrum confirms the expected 390 dalton mass. Amino acid analysis can corroborate composition when a sample's origin is uncertain. Counterion content, particularly residual trifluoroacetate from purification, is frequently reported alongside purity because it shifts the net mass of the solid.
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.
Storage recommendations center on limiting moisture, heat, and light. The dry powder is generally kept at minus 20 degrees Celsius, and some suppliers recommend minus 80 degrees for long-term archival. Once dissolved, solutions are usually aliquoted and frozen to avoid repeated freeze-thaw cycles, which can promote aggregation or degradation. Aqueous stability depends on pH and concentration, and buffered saline is often preferred over plain water for biological work. Stability data specific to epitalon remain limited, so general peptide-handling practices are applied by analogy rather than from product-specific validation.
== Reactions == Acrolein is a relatively electrophilic compound and a reactive one, hence its high toxicity. It is a good Michael acceptor, hence its useful reaction with thiols. It forms acetals readily, a prominent one being the spirocycle derived from pentaerythritol, diallylidene pentaerythritol. Acrolein participates in many Diels-Alder reactions, even with itself. Via Diels-Alder reactions, it is a precursor to some commercial fragrances, including myrac aldehyde ("lyral") and norbornene-2-carboxaldehyde. The monomer 3,4-epoxycyclohexylmethyl-3',4'-epoxycyclohexane carboxylate is also produced from acrolein via the intermediacy of tetrahydrobenzaldehyde.
== Human pathology == Accumulation of excess homogentisic acid and its oxide, named alkapton, is a result of the failure of the enzyme homogentisic acid 1,2-dioxygenase (typically due to a mutation) in the degradative pathway of tyrosine, consequently associated with alkaptonuria.
==== 900–999 ==== Act of Sederunt (Rules of the Court of Session Amendment No. 2) (Fees of Solicitors) 1993 (S.I. 1993/900) Further Education (Exclusion of Land from Transfer) Order 1993 (S.I. 1993/901) Greater Manchester and Lancashire (County and Metropolitan Borough Boundaries) Order 1993 (S.I. 1993/902) Dyfed-Powys Police (Amalgamation) (Amendment) Order 1993 (S.I. 1993/909) National Rivers Authority (Anglian Region) (Reconstitution of the Witham Third District Internal Drainage Board) Order 1993 (S.I. 1993/910) Plymouth Development Corporation (Area and Constitution) Order 1993 (S.I. 1993/911) Electricity (Restrictive Trade Practices Act 1976) (Exemption) Order 1993 (S.I. 1993/912) Child Support (Miscellaneous Amendments) Regulations 1993 (S.I. 1993/913) Act of Sederunt (Child Support Act 1991) (Amendment of Ordinary Cause and Summary Cause Rules) 1993 (S.I. 1993/919) Act of Sederunt (Child Support Rules) 1993 (S.I. 1993/920) Act of Sederunt (Bankruptcy Rules) 1993 (S.I. 1993/921) Land Registration (Scotland) Act 1979 (Commencement No. 7) Order 1993 (S.I. 1993/922) Dairy Produce Quotas Regulations 1993 (S.I. 1993/923) Education (Dissolution of the Council for National Academic Awards) Order 1993 (S.I. 1993/924) Child Support (Maintenance Assessments and Special Cases) Amendment Regulations 1993 (S.I. 1993/925) Greater Manchester and Lancashire (County and District Boundaries) Order 1993 (S.I. 1993/926) Secure Tenancies (Designated Courses) (Amendment) Regulations 1993 (S.I.
Sources: en.wikipedia.org
== Habitat and ecology == N. tabacum is a native of tropical and subtropical America, also appearing as a weed. N. tabacum is sensitive to temperature, air, ground humidity and the type of land. Temperatures of 20–30 °C (68–86 °F) are best for adequate growth; an atmospheric humidity of 80-to-85% and soil without a high level of nitrogen are also optimal.
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=== In the United Kingdom === Based on Appert's methods of food preservation, the tin can process was allegedly developed by Frenchman Philippe de Girard, who came to London and used British merchant Peter Durand as an agent to patent his own idea in 1810. Durand did not pursue food canning himself, selling his patent in 1811 to Bryan Donkin and John Hall, who were in business as Donkin Hall and Gamble, of Bermondsey. Bryan Donkin developed the process of packaging food in sealed airtight cans, made of tinned wrought iron. Initially, the canning process was slow and labour-intensive, as each large can had to be hand-made, and took up to six hours to cook, making canned food too expensive for ordinary people. The main market for the food at this stage was the British Army and Royal Navy. By 1817, Donkin recorded that he had sold £3000 (equal to £222,201 today) worth of canned meat in six months. In 1824, Sir William Edward Parry took canned beef and pea soup with him on his voyage to the Arctic in HMS Fury, during his search for a northwestern passage to India. In 1829, Admiral Sir James Ross also took canned food to the Arctic, as did Sir John Franklin in 1845. Some of his stores were found by the search expedition led by Captain (later Admiral Sir) Leopold McClintock in 1857.
Sources: en.wikipedia.org
It is a synthetic tetrapeptide built from alanine, glutamate, aspartate and glycine. The four residues are joined by standard peptide bonds, giving a linear chain rather than a branched structure.
The name derives from epithalamin, a pineal gland extract studied in the former Soviet Union. Researchers proposed that short fragments of that extract carried the biological activity of interest.
No major regulatory agency has approved it as a medicine. It is handled as a research chemical, and products sold under this name are not standardised drugs with defined clinical labelling.
Mass spectrometry provides the identity check, because the observed mass is compared with the theoretical mass of the AEDG sequence. Chromatography separates and quantifies impurities but does not by itself prove which peptide is present. The two techniques are normally used together.