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Epitalon Peptide Background And Structure — Deep Dive

By Editorial Desk · published 2026-05-03 · last reviewed 2026-05-30 · Wiki

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 2026-05-30. Where a claim depends on a specific study, the study is described rather than over-claimed.

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.

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.

Peptide Identity and Research Origin

Epitalon is a synthetic tetrapeptide with the sequence alanine–glutamate–aspartate–glycine, commonly abbreviated AEDG. Its design traces to epithalamin, a peptide fraction prepared from bovine pineal gland extracts that researchers in Saint Petersburg began investigating in the 1970s. The compound has a molecular formula of C14H22N4O9 and a nominal molecular mass near 390 daltons. It holds no approved drug status in the United States or the European Union, and material sold under this name is generally offered as a research chemical rather than a finished pharmaceutical product.

Proposed mechanisms centre on cell-culture observations rather than a defined receptor interaction. Several reports describe increased expression of the telomerase catalytic subunit after exposure of cultured human cells, and the authors attributed the effect to short peptide fragments entering the nucleus and influencing gene transcription. No receptor for the tetrapeptide has been identified, and the free peptide is expected to be degraded rapidly by plasma peptidases. Whether any measurable fraction reaches intact tissues after administration remains an unresolved question rather than an established finding.

Epitalon at a glance

PropertyValueNotes
Amino acid sequenceAla-Glu-Asp-GlyTetrapeptide, often abbreviated AEDG
Molecular formulaC14H22N4O9Free peptide, unmodified termini
Molecular weight~390.35 DaCalculated for the free acid form
AppearanceWhite to off-white powderTypical lyophilized product form
Solubility classFreely soluble in waterTwo acidic residues dominate ionic character

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.

Related pages on this site

Epitalon Background and Discovery

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.

Epitalon Background and Nomenclature

The compound is generally presented as a synthetic fragment of epithalamin, a pineal gland extract investigated in the former Soviet Union from the 1970s onward. Vladimir Khavinson and colleagues in Saint Petersburg developed short peptides modelled on such extracts, and epitalon became the most widely cited of those sequences. Most primary reports appeared in Russian-language journals or in proceedings with limited international circulation. Independent replication in laboratories outside that network remains sparse, and much repeated secondary material traces back to a small number of originating groups.

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.

Structure, Naming and Discovery

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.

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.

Further detail

=== Biosensing === SWCNTs have nanoscale dimensions that match the size of biological species. Due to this size compatibility and their large surface-to-volume ratio, they are sensitive to changes in their chemical environment. Through covalent and non-covalent surface functionalization, SWCNTs can be precisely tailored for selective molecular interactions with a target analyte. The SWCNT represents the transduction unit that converts the interaction into a signal change (optical or electrical). Due to continuous progress in the development of detection strategies, there are numerous examples of the use of SWCNTs as highly sensitive nanosensors (even down to the single molecule level) for a variety of important biomolecules. Examples include the detection of reactive oxygen and nitrogen species, neurotransmitters, other small molecules, lipids, proteins, sugars, DNA/RNA, enzymes as well as bacteria.

Department of Defense on human–animal bonding determined that there was an improvement and enrichment of life when animals were closely involved with humans. The study tested blood levels and noticed a rise in oxytocin in humans and animals which participated; oxytocin has the ability to lower stress, heart rate, and fear levels in humans and animals. Historically, animals were domesticated for functional use; for example, dogs for herding and tracking, and cats for killing mice or rats. Today, in Western societies, their function is primarily bonding. For example, current studies show that 60–80% of dogs sleep with their owners at night in the bedroom, either in or on the bed. Moreover, in the past the majority of cats were kept outside (barn cats) whereas today most cats are kept indoors (housecats) and considered part of the family. Currently, in the US, for example, 1.2 billion animals are kept as pets, primarily for bonding purposes. In addition, as of 1995, there were over 30 research institutions looking into the potential benefits of the human–animal bond.

===== Jovita Rivera ===== Jovita Rivera was one of the ten plaintiffs in the federal class action suit of Madrigal v. Quilligan. On October 12, 1973, Rivera went to the USC-LA hospital to give birth to her second child. She was under medication and in labor pains when medical staff misinformed her about the risk and chances of getting pregnant right after birth. She consented and a tubal ligation was done. Rivera, 27 at the time, states that during her stay at the hospital, while in advanced labor and under pain medication due to complications, her doctor told her she would be a burden to the government. Women like Rivera were offered the choice of sterilization under poor circumstances, under medication, and with no language assistance for translation. Some of the other plaintiffs for this case faced hostility from staff when told they could receive more pain medication if they signed papers consenting to sterilization. Rivera stated: "... the doctor told me that I had too many children, that I was poor, and a burden to the government and I should sign a paper not to have more children [...] The doctors told me that my tubes could be untied at a later time and I could still have children." While Rivera was under distress, she believed the process was reversible and consented. When Rivera and the other plaintiffs testified in court to prove that they had been coerced into getting a procedure, the judge did not rule in their favor.

Sources: en.wikipedia.org

Background from the literature

He argued that wounds should be cleaned and sealed up promptly. This was a radical idea; normally this would have been inviting gas gangrene, but Florey proposed leaving that to the penicillin. His recommendations were acted upon, and the War Office established a training course for pathologists and clinicians at the Royal Herbert Hospital, which made use of film that Florey shot in North Africa. Although he intended that penicillin be used to treat the seriously wounded, there were large numbers of venereal disease cases, against which penicillin was particularly effective, and from a military point of view being able to cure gonorrhea in 48 hours was a breakthrough. The supply situation improved, and 20 million units per day were made available for the Allied invasion of Italy in September. Two out of three gas gangrene casualties now survived.

However, the experimental chemistry of darmstadtium has not received as much attention as that of the heavier elements from copernicium to livermorium. The more neutron-rich darmstadtium isotopes are the most stable and are thus more promising for chemical studies. However, they can only be produced indirectly from the alpha decay of heavier elements, and indirect synthesis methods are not as favourable for chemical studies as direct synthesis methods. The more neutron-rich isotopes 276Ds and 277Ds might be produced directly in the reaction between thorium-232 and calcium-48, but the yield was expected to be low. Following several unsuccessful attempts, 276Ds was produced in this reaction in 2022 and observed to have a half-life less than a millisecond and a low yield, in agreement with predictions. Additionally, 277Ds was successfully synthesized using indirect methods (as a granddaughter of 285Fl) and found to have a short half-life of 3.5 ms, not long enough to perform chemical studies. The only known darmstadtium isotope with a half-life long enough for chemical research is 281Ds, which would have to be produced as the granddaughter of 289Fl.

== Research == His research proposed that peptide hormones are produced from large precursor proteins. In 1967, Chrétien first articulated the prohormone theory, proposing that peptide hormones are produced from larger precursors, a paradigm later widely confirmed and foundational for modern endocrinology. In 1976, his team discovered human β-endorphin, advancing understanding of endogenous opioid systems in pain and stress biology. In 1990, Chrétien and collaborators identified the family of proprotein convertases (PCs/PCSK1–9), endoproteases that activate many precursor proteins and hormones, helping to establish a field often termed “functional endoproteolysis.” A loss-of-function PCSK9 variant characterized in French-Canadian families by Chrétien’s group is associated with markedly low LDL cholesterol and cardioprotection, work that helped validate PCSK9 as a therapeutic target. Chrétien’s prohormone/convertase research has had broad clinical impact, informing therapies and biological understanding in diabetes, obesity, dyslipidemia, atherosclerosis, cancer, opiate use disorders, and Alzheimer’s disease. Between 1981 and 1990, he ranked among the world’s most-cited scientists (reported as seventh globally) reflecting the reach of his contributions.

Sources: en.wikipedia.org

Frequently asked questions

What is epitalon made of?

Epitalon is a synthetic tetrapeptide composed of four amino acids: alanine, glutamate, aspartate, and glycine. It is written as Ala-Glu-Asp-Gly. The free peptide has a molecular weight of about 390 daltons and is normally supplied as a lyophilized powder.

Is epitalon extracted from the pineal gland?

No. Epitalon is chemically synthesized, not extracted. It was designed as a short synthetic fragment conceptually related to larger pineal peptides studied in the same research tradition, particularly the extract known as epithalamin. The two are distinct materials with different compositions.

Why is epitalon described as a bioregulator?

The term bioregulator is used in this research tradition for short peptides proposed to influence gene expression or cell function. Epitalon is grouped with other synthetic short peptides under this label. The term reflects a proposed mechanism rather than an established drug classification.

Is epitalon the same as epithalamin?

No. Epithalamin is a heterogeneous peptide fraction obtained from pineal gland extract and contains many components. Epitalon is a single synthetic tetrapeptide with the sequence Ala-Glu-Asp-Gly. Researchers synthesised the shorter peptide while attempting to identify active sequences within the extract.

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