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Peptide Identity And Laboratory Handling — Reference Sheet

By Editorial Desk · published 2026-03-16 · last reviewed 2026-05-03 · Wiki

Epithalamin is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.

Updated 2026-05-03. Numbers and descriptions here follow the published literature rather than marketing material.

Peptide Identity and Laboratory Handling

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.

Chemical Identity and Research Background

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.

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 at a glance

PropertyValueNotes
Molecular formulaC14H22N4O9Free acid form of the tetrapeptide
Molecular massAbout 390.35 DaCalculated monoisotopic value
AppearanceWhite to off-white powderTypical lyophilized presentation
SolubilitySoluble in waterAlso dissolves in buffered saline
Storage temperatureMinus 20 degrees CelsiusDry, dark conditions; avoid repeated thawing

Epitalon Background And Identification

Literature searches for this compound must account for several spelling variants. Indexing databases contain epitalon, epithalon, epithalone, and AEDG, and relevant records are scattered across Russian-language and English-language journals that do not consistently cross-cite. Early publications describe the parent extract as a mixture of many peptides, whereas later work addresses the single synthetic tetrapeptide. That shift in nomenclature complicates comparison between studies, because extract data and tetrapeptide data are sometimes cited interchangeably. A search strategy omitting the alternate spellings will return an incomplete set of references.

Reported biological findings come mainly from cell culture and rodent experiments. Those studies describe changes in telomerase catalytic subunit expression, melatonin rhythm amplitude, and antioxidant enzyme activity after peptide exposure. Human data are sparse and consist of small trials with limited blinding and inconsistent endpoints. The proposed mechanisms remain hypotheses rather than established facts, and there is no consensus on whether effects observed in animals carry over to people. Independent replication outside the original research groups is limited, which is a recognised gap in the published literature.

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Epitalon Peptide Background and Structure

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.

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.

Structure, Naming and Discovery

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.

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.

Background and Proposed Mechanism

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 is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. It was designed at the St. Petersburg Institute of Bioregulation and Gerontology as a short, chemically defined analogue of epithalamin, a fraction obtained from bovine pineal tissue. Small peptide bioregulators of this type formed a long-running line of work there from the 1980s onward. Because the molecule is produced by solid-phase synthesis rather than extraction, its composition is exact and its purity can be measured directly.

Notes from published material

Around 20–40% of those with coeliac disease experience non-responsive coeliac disease (NRCD), which is the continuation of symptoms despite elimination of gluten from their diets for at least 6 to 12 months. The most common cause of NRCD is unintentional gluten ingestion; however other conditions such as small intestinal bacterial overgrowth, giardiasis, disaccharide or FODMAP intolerance, Crohn's disease, fructose intolerance, microscopic colitis, pancreatic insufficiency, irritable bowel syndrome, and lactose intolerance can cause persistent symptoms or villous atrophy despite adhering to the GFD.

Every day between one and two percent of muscle is broken down and rebuilt. Inactivity, malnutrition, disease, and aging can increase the breakdown leading to muscle atrophy or sarcopenia. Sarcopenia is commonly an age-related process that can cause frailty and its consequences. A decrease in muscle mass may be accompanied by a smaller number and size of the muscle cells as well as a lower myofibrillar protein content. Human spaceflight, involving prolonged periods of immobilization and weightlessness is known to result in muscle weakening and atrophy resulting in a loss of as much as 30% of mass in some muscles. Such consequences are also noted in some mammals following hibernation. Many diseases and conditions including cancer, AIDS, and heart failure can cause muscle loss known as cachexia.

=== Diabetes mellitus === GCK mutations reduce the functional efficiency of the glucokinase molecule. Heterozygosity for alleles with reduced enzyme activity results in a higher threshold for insulin release and persistent, mild hyperglycemia. This condition is referred to as maturity onset diabetes of the young, type 2 (MODY2). The most recent overview of GCK mutation that were observed in patients claims 791 mutations, of which 489 are thought to cause the MODY diabetes and therefore reduce the functional efficiency of the glucokinase molecule. Homozygosity for GCK alleles with reduced function can cause severe congenital insulin deficiency, resulting in persistent neonatal diabetes.

Sources: en.wikipedia.org

Background from the literature

Hoyle said the early revelations were a "supreme discourtesy to the House". 30 October – October 2024 United Kingdom budget. 31 October – 2024 Conservative Party leadership election: Voting closes for the election of the Conservative Party's next leader.

When applied to the tongue or to shaven skin, brilliant blue FCF can be absorbed directly into the bloodstream. However, in experiments with rodents, it was found that it is poorly absorbed from the gastrointestinal tract, and 95% of the ingested dye can be found in the feces.

It can be "fingerprinted" as different in origin from manmade depleted uranium by the 234U content, which is 55 ppm in uranium from the Oklo Mine as well as all other natural sources, but will be lower in depleted uranium in accordance with the degree of depletion.

Sources: en.wikipedia.org

Frequently asked questions

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.

Does epitalon occur naturally in the body?

No naturally occurring free form of the peptide has been described. The four-amino-acid sequence can appear as a fragment within larger proteins, but that is not the same as the intact compound being present as a circulating molecule. Materials used in research are synthetic.

How is epitalon purity checked?

Purity is usually checked by reverse-phase high-performance liquid chromatography, which separates the target peptide from related impurities. Mass spectrometry is commonly used alongside it to confirm molecular mass. Some suppliers also provide amino acid analysis for additional sequence confirmation.

Which amino acids make up epitalon?

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.

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