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Epitalon Peptide Background And Structure — Beginner to Advanced

By Editorial Desk · published 2025-10-19 · last reviewed 2025-11-19 · Wiki

The short version of bioregulator fits in a sentence. The long version — which is the one that helps — is below.

This page was last updated on 2025-11-19 and is reviewed periodically as new material appears.

Epitalon Peptide Background and Structure

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.

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.

Stability Handling and Quality Control

Peptides of this size are generally stable as dry solids but degrade in solution over time. The principal routes are hydrolysis of the peptide backbone and oxidation, with hydrolysis favoured by elevated temperature and extreme pH. Aqueous solutions held at room temperature can show measurable loss of purity within days, while frozen aliquots are considerably more durable. Because the sequence contains neither cysteine nor methionine, oxidation is less of a concern than for many other peptides, but pH control during handling still matters.

Typical storage for the lyophilized powder is −20 °C or lower, in a sealed container protected from light and moisture. Hygroscopic material should be allowed to equilibrate to room temperature before the vial is opened, which limits condensation on the contents. Working solutions are commonly divided into single-use aliquots and frozen to avoid repeated freeze-thaw cycles. Dilute solutions are more prone to adsorption onto plastic surfaces and to loss during filtration, so procedures that minimize transfers and use low-binding labware are preferable.

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

Background and Chemical Identity

Epitalon is a synthetic linear tetrapeptide with the sequence alanine–glutamate–aspartate–glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and the calculated mass is approximately 390.35 g/mol. The compound is made by solid-phase peptide synthesis rather than extracted from tissue, although early work described it as a short fragment of a peptide fraction obtained from bovine pineal extract. In the research literature the spelling epitalon and the variant epithalone both appear, while AEDG is the standard code used in peptide nomenclature.

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.

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Handling, Storage and Analytical Checks

Reference material is normally supplied as a lyophilised powder in a sealed vial. Product literature typically recommends storage at minus twenty degrees Celsius or colder, protected from light and moisture. Freeze-thaw cycling is usually avoided because repeated condensation can introduce water into the vial. Working solutions are commonly prepared fresh, aliquoted, and kept cold for short periods rather than stored at ambient temperature. Labelling the date of opening helps track how long a vial has been in use.

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.

Background and Proposed Mechanism

The most frequently cited proposed action is induction of telomerase, the enzyme that adds repeat sequences to chromosome ends. Cell-culture work from the originating group reported higher telomerase reverse transcriptase expression and measurable telomere elongation in human somatic cells after exposure. How a four-residue peptide would reach nuclear gene regulation is not established, and no cell-surface receptor or uptake route has been identified. Additional reports describe changes in melatonin secretion, antioxidant enzyme activity and lipid peroxidation in aged animals, but these findings remain mechanistically unconnected to the telomerase observation.

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.

Further detail

== Applications == Cysteine, mainly the l-enantiomer, is a precursor in the food, pharmaceutical, and personal-care industries. One of the largest applications is the production of flavors. For example, the reaction of cysteine with sugars in a Maillard reaction yields meat flavors. l-Cysteine is also used as a processing aid for baking. In the field of personal care, cysteine is used for permanent-wave applications, predominantly in Asia. Again, the cysteine is used for breaking up the disulfide bonds in the hair's keratin. Cysteine is a very popular target for site-directed labeling experiments to investigate biomolecular structure and dynamics. Maleimides selectively attach to cysteine using a covalent Michael addition. Site-directed spin labeling for EPR or paramagnetic relaxation-enhanced NMR also uses cysteine extensively.

=== Mechanism of action === It is a selective inhibitor of the enzyme janus kinase 1 (JAK1). It inhibits JAK1 by 28 fold of selectivity over JAK2 and more than 340 fold of selectivity over JAK3. Two mechanisms are involved in atopic dermatitis, one involves epidermal barrier disruptions, and the other one is cutaneous inflammation due to the immune system over response. Acute inflammation in AD typically involves IL-13, IL-4, and IL-33. Consequently, inhibiting JAK1 results in suppressing the signaling cytokines IL-4, IL-3, and IL-31. Many other cytokines are involved in AD and mediated by JAK1 such as type II cytokine receptors for IL-22, IL-19, IL-10, IL-20 and glycoprotein 130 (gp130) including IL-6 and IL-12 which are also associated with JAK2 and TYK2; IFN-α and INF-β signal.

Stenosis and insufficiency/regurgitation represent the dominant functional and anatomic consequences associated with valvular heart disease. Irrespective of disease process, alterations to the valve occur that produce one or a combination of these conditions. Insufficiency and regurgitation are synonymous terms that describe an inability of the valve to prevent backflow of blood as leaflets of the valve fail to join (coapt) correctly. Stenosis is characterized by a narrowing of the valvular orifice that prevents adequate outflow of blood. Stenosis can also result in insufficiency if thickening of the annulus or leaflets results in inappropriate leaf closure.

Sources: en.wikipedia.org

Supporting material

== Popular culture == Tetrodotoxin serves as a plot device for characters to fake death, as in the films Hello Again (1987), The Serpent and the Rainbow (1988), The A-Team (2010), Captain America: The Winter Soldier (2014), and War (2019), and in episodes of Jane the Virgin, Miami Vice (1985), Nikita, MacGyver (season 7, episode 6, where the antidote is Datura stramonium leaf), CSI: NY (season 4, episode 9, "Boo"), and Chuck. In Law Abiding Citizen (2009), Alex Cross (2012), and Send Help (2026), paralysis is presented as a method of assisting torture. The toxin was also referenced in "synthetic form" in season 1, episode 2, of the series "FBI". The toxin is used as a weapon in both the second season of Archer, in Covert Affairs and in the Inside No. 9 episode "The Riddle of the Sphinx". In Columbo, episode 2 of season 7, fugu is used to kill the antagonist's victim. In The Apothecary Diaries light novel, as well as the respective manga and anime adaptations, fugu toxin is encountered across multiple mystery arcs. Based on the presumption that tetrodotoxin is not always fatal, but at near-lethal doses can leave a person extremely unwell with the person remaining conscious, tetrodotoxin has been alleged to result in zombieism, and has been suggested as an ingredient in Haitian Vodou preparations. This idea first appeared in the 1938 non-fiction book Tell My Horse by Zora Neale Hurston in which there were multiple accounts of purported tetrodotoxin poisoning in Haiti by a voodoo sorcerer called the bokor.

=== Requirements === The Food and Nutrition Board (FNB) of the U.S. Institute of Medicine set Recommended Dietary Allowances (RDAs) for essential amino acids in 2002. For leucine, for adults 19 years and older, 42 mg/kg body weight/day.

== History == Since NMR spectroscopy has been available to chemists, there have been numerous studies on the applications of this technique. One of these noted the difference in the chemical shift (i.e. the distance between the peaks) of two diastereomers. Conversely, two compounds that are enantiomers have the same NMR spectral properties. It was reasoned that if a mix of enantiomers could be converted into a mix of diastereomers by bonding them to another chemical that was itself chiral, it would be possible to distinguish this new mixture using NMR, and therefore learn about the original enantiomeric mixture. The first popular example of this technique was published in 1969 by Harry S. Mosher. The chiral agent used was a single enantiomer of MTPA (α-methoxy-α-(trifluoromethyl)phenylacetic acid), also known as Mosher's acid. The corresponding acid chloride is also known as Mosher's acid chloride, and the resultant diastereomeric esters are known as Mosher's esters. Another system is Pirkle's alcohol, developed in 1977.

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.

How should lyophilized epitalon be stored?

The powder is normally kept at −20 °C or below in a sealed, moisture-protected container. Letting the vial reach room temperature before opening helps prevent condensation on the contents.

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