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Epitalon Background And Nomenclature — Quick Reference

By Editorial Desk · published 2026-04-10 · last reviewed 2026-05-02 · Wiki

If you have been reading about Pineal 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 2026-05-02. Numbers and descriptions here follow the published literature rather than marketing material.

Epitalon Background and Nomenclature

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.

Peptide Identity and Laboratory Handling

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.

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

Chemical Identity and Research Background

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.

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Epitalon Background And Identification

The parent extract epithalamin was characterised as a low-molecular-weight fraction of pineal tissue rather than a single defined chemical entity. Researchers fractionated it and tested successive fragments for activity, a screening approach typical of peptide discovery work in that era. Epitalon emerged from that process as one of the shorter sequences of interest. Because the original extract was never fully resolved into individual components, claims about which constituent drives a given effect rest on inference. This distinction matters when reading older reports that attribute extract observations to the tetrapeptide itself.

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.

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.

Structure, Naming and Discovery

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.

Epitalon is a synthetic tetrapeptide whose four residues are alanine, glutamate, aspartate and glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9 and its monoisotopic mass is near 390.35 daltons. The peptide carries two acidic side chains, so it is neutral to negatively charged in most aqueous buffers. Published reference summaries usually list it under both spellings, epitalon and epithalon, and treat the two names as the same material.

Background from the literature

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Sources: en.wikipedia.org

Reference notes

Carbonyl sulfide is the chemical compound with the linear formula O=C=S. It is a colorless flammable gas with an unpleasant odor. It is a linear molecule consisting of a carbonyl double bonded to a sulfur atom. Carbonyl sulfide can be considered to be intermediate between carbon dioxide and carbon disulfide, both of which are valence isoelectronic with it.

Two years later the Madras and Bombay armies lost their posts of Commander-in-Chief. In 1895, the Presidency Armies were abolished and the Indian Army created thereby was grouped into four commands: Bengal, Madras (including Burma), Bombay (including Sind, Quetta, and Aden), and the Punjab (including the North-West Frontier and the Punjab Frontier Force). Each was under the command of a lieutenant general, who answered directly to the C-in-C, India. The Presidency armies were abolished with effect from 1 April 1895 by a notification of the Government of India through Army Department Order Number 981 dated 26 October 1894, unifying the three Presidency armies into a single Indian Army. The armies were amalgamated into four commands, Northern, Southern, Eastern, and Western. The Indian Army, like the Presidency armies, continued to provide armed support to the civil authorities, both in combating banditry and in case of riots and rebellion. One of the first external operations the new unified army faced was the 1899 to 1901 Boxer Rebellion in China. The 1st, 4th, and 14th Sikhs; 3rd Madras Native Infantry, 4th Goorkas, 22nd and 30th Bombay Native Infantry, 24th Punjab Infantry, 1st Madras Pioneers, No. 2 Company Bombay Sappers, No. 3 Company Madras Sappers, No. 4 Company Bengal Sappers, and the 1st Bengal Lancers, among other Indian units, all served during the Rebellion. Numerous Indian soldiers earned the China War Medal 1900 with the "Relief of Pekin" clasp for contributing to the relief of Peking and the International Legations from 10 June to 14 August 1900.

Drosophila melanogaster can be distinguished from related species by the following combination of features: gena ~1/10 diameter of eye at greatest vertical height; wing hyaline and with costal index 2.4; male protarsus with a single row of ~12 setae forming a sex comb; male epandrial posterior lobe small and nearly triangular; female abdominal tergite 6 with dark band running to its ventral margin; female oviscapt small, pale, without dorsodistal depression and with 12–13 peg-like outer ovisensilla.

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=== Deep Learning === More recently, deep learning techniques have been applied to solve the de novo peptide sequencing problem. The first breakthrough was DeepNovo, which adopted the convolutional neural network structure, achieved major improvements in sequence accuracy, and enabled complete protein sequence assembly without assisting databases Subsequently, additional network structures, such as PointNet (PointNovo), have been adopted to extract features from a raw spectrum. The de novo peptide sequencing problem is then framed as a sequence prediction problem. Given previously predicted partial peptide sequence, neural-network-based de novo peptide sequencing models will repeatedly generate the most probable next amino acid until the predicted peptide's mass matches the precursor mass. At inference time, search strategies such as beam search can be adopted to explore a larger search space while keeping the computational cost low. Comparing with previous methods, neural-network-based models have demonstrated significantly better accuracy and sensitivity. Moreover, with a careful model design, deep-learning-based de novo peptide sequencing algorithms can also be fast enough to achieve real-time peptide de novo sequencing. PEAKS software incorporates this neural network learning in their de novo sequencing algorithms.

Sources: en.wikipedia.org

Reference notes

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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 made of?

Epitalon is a synthetic tetrapeptide built from four amino acids: alanine, glutamate, aspartate, and glycine. It is not extracted from a natural source but made in the laboratory by chemical synthesis. Its short length makes it relatively straightforward to produce at high purity.

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