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Chemical Identity And Research Background — Research Overview

By Editorial Desk · published 2026-03-20 · last reviewed 2026-04-26 · News

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.

Updated 2026-04-26. Numbers and descriptions here follow the published literature rather than marketing material.

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.

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.

Analytical Characterization and Stability

Because epitalon has no pharmacopoeial monograph, quality assessment depends on supplier documentation and independent testing. Certificates of analysis typically report a purity figure from a single chromatographic run, a measured mass and sometimes an appearance description, but methods and acceptance criteria are not harmonised across vendors. Third-party laboratories can repeat identity and purity measurements, and mismatches between labelled and measured peptide content have been described for research peptides generally. What constitutes adequate identity confirmation for a molecule of this size stays an open question, since mass agreement alone does not separate closely related sequences.

Identity testing for epitalon relies on reversed-phase high-performance liquid chromatography for purity and mass spectrometry for mass confirmation. Because the sequence contains no tryptophan or tyrosine, ultraviolet detection at 280 nanometres is insensitive, so chromatographic methods usually monitor absorbance near 214 nanometres, where the peptide backbone absorbs. Electrospray ionisation or matrix-assisted laser desorption/ionisation then checks the intact mass against the expected value near 390 daltons. Peptide mapping or amino acid analysis after acid hydrolysis can supplement these measurements, although such confirmatory work is seldom reported on commercial certificates of analysis.

Stability of the tetrapeptide follows ordinary peptide chemistry rather than any unusual structural feature. The aspartate-glycine pair is prone to aspartimide formation under mildly basic or neutral conditions, and deamidation can follow, altering both mass and chromatographic retention. Dry lyophilised powder kept at or below minus twenty degrees Celsius is the usual handling recommendation, with repeated freeze-thaw cycles avoided. Once dissolved in neutral aqueous buffer, degradation proceeds over days to weeks depending on pH and temperature, while acidic conditions generally slow the aspartimide route. A formal stability-indicating study has not been published in the indexed literature.

Epitalon at a glance

PropertyValueNotes
Chemical classSynthetic tetrapeptideFour residues, linear chain
Residue sequenceAla-Glu-Asp-GlySingle-letter form AEDG
Calculated mass390.3 daltonsValue for the free, uncharged form
AppearanceWhite to off-white powderUsually supplied lyophilized
SolubilityFreely soluble in waterOften handled as a salt form

Background and Chemical Identity

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.

Material supplied for laboratory use is normally a lyophilised white to off-white powder that dissolves readily in water and in isotonic saline. Lyophilised cakes are hygroscopic and should be equilibrated to room temperature before opening to limit condensation on the solid. Solutions are typically prepared at milligram-per-millilitre concentrations and divided into single-use aliquots, because repeated freeze–thaw cycles degrade short peptides. Aqueous solutions are far less stable than the dry powder, and identity is usually verified by mass spectrometry alongside purity estimation from reversed-phase high-performance liquid chromatography.

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.

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Storage, Assay, and Regulatory Framework

Regulatory treatment differs by country. No formulation of epitalon holds a marketing authorisation as a medicine in the United States or the European Union, where material sold for laboratory use is handled as a research chemical and is not intended for human consumption. In Russia, several short peptide preparations from the same institute's peptide series are registered medicinal products, and epitalon appears in that national context. Elsewhere it is frequently offered as a cosmetic ingredient, a category with lighter requirements. Advertising claims about longevity or disease prevention are restricted in most jurisdictions, which limits how sellers describe the compound.

Freeze-dried epitalon is normally kept at minus twenty degrees Celsius in a sealed, desiccated container, protected from light. Short excursions at ambient temperature during shipping are generally tolerated, but repeated warming and cooling cycles encourage moisture uptake, which shortens shelf life. Once dissolved, the peptide is far less stable than the solid: aqueous solutions are subject to hydrolysis and to deamidation at the aspartate and glutamate residues. Working solutions are therefore held refrigerated and used within days, and repeated freezing and thawing of the same vial is best avoided.

Identity and Research Background

The peptide is a synthetic analogue of epithalamin, a preparation extracted from bovine pineal glands. Investigators sought a short, chemically defined molecule that would reproduce some of the endocrine and gerontological observations attributed to the glandular extract. Proposed mechanisms centre on induction of telomerase activity, an effect reported in cultured human somatic cells in the early 2000s, together with influences on melatonin secretion and neuroendocrine regulation. Those mechanisms remain incompletely characterised, and the reported telomerase response has not been consistently reproduced by independent groups working in comparable systems.

Published work on this compound consists mainly of in vitro experiments, animal studies, and small clinical investigations, a substantial share of which appeared in Russian-language journals. Sample sizes are generally small, control conditions differ between studies, and several endpoints rely on markers whose clinical meaning is itself debated. Reviews of the longevity field treat the peptide as an early example of telomerase-directed research rather than an established intervention. Regulatory treatment varies by country: some jurisdictions place it under prescription controls, others treat it as a laboratory material, and importation may be restricted regardless of local status.

Analytical Methods And Handling

Purity assessment of peptide reagents normally relies on reversed-phase high-performance liquid chromatography. A gradient of acetonitrile in water with trifluoroacetic acid, paired with a C18 stationary phase, separates the target tetrapeptide from truncated sequences and deletion analogues. Detection at 214 nanometres exploits absorbance of the peptide backbone, since the molecule contains no aromatic residue. Results are expressed as a percentage of total peak area. Values above ninety-five percent are typical for research-grade material, although reporting conventions vary between suppliers.

Identity confirmation uses mass spectrometry, usually electrospray ionisation in positive mode or matrix-assisted laser desorption. The protonated free peptide produces a signal near three hundred and ninety-one daltons, while salt adducts shift that value slightly. Tandem mass spectrometry or amino acid analysis supplies sequence-level confirmation, which a single mass measurement cannot. Peptides containing aspartate can cyclise into succinimide intermediates that hydrolyse to isoaspartate isomers of identical mass. Because those isomers are difficult to separate chromatographically, identity and purity results carry more weight when interpreted together.

Reference notes

== Causes == Hypothyroidism is caused by inadequate function of the gland itself (primary hypothyroidism), inadequate stimulation by thyroid-stimulating hormone from the pituitary gland (secondary hypothyroidism), or inadequate release of thyrotropin-releasing hormone from the brain's hypothalamus (tertiary hypothyroidism). Secondary and tertiary hypothyroidism are called "central" hypothyroidism. Primary hypothyroidism is about a thousandfold more common than central hypothyroidism. Iodine deficiency is the most common cause of primary hypothyroidism and endemic goiter worldwide. In areas of the world with sufficient dietary iodine, the autoimmune disease Hashimoto's thyroiditis (chronic autoimmune thyroiditis) is the most common cause of primary hypothyroidism. Hashimoto's may be associated with a goiter. It is characterized by infiltration of the thyroid gland with T lymphocytes and autoantibodies against specific thyroid antigens such as thyroid peroxidase, thyroglobulin and the TSH receptor. Hashimoto's thyroiditis is associated with other immune-mediated diseases such as type 1 diabetes, pernicious anemia, myasthenia gravis, celiac disease, rheumatoid arthritis, and systemic lupus erythematosus. It may occur as part of autoimmune polyendocrine syndrome (type 1 and type 2). After women give birth, about 5% develop postpartum thyroiditis which can occur up to nine months afterwards. This is characterized by a short period of hyperthyroidism followed by a period of hypothyroidism; 20–40% remain permanently hypothyroid.

Irritable bowel syndrome (IBS) Celiac disease. Inflammatory bowel diseases. Exercise-induced gastrointestinal syndrome and exercise-associated gastrointestinal symptoms. Small intestinal bacterial overgrowth. The low-FODMAP diet is intended to be used only after a full medical evaluation. This ensures correct diagnosis and treatment. Use of a low-FODMAP diet without medical advice can lead to serious health risks, including nutritional deficiencies and misdiagnosis of celiac disease. Sometimes the diet is used in phases. Firstly, FODMAPs below the threshold value are eliminated from the diet (restriction phase). The restriction phase does not usually last more than six weeks. After this stage, products that were eliminated are re-introduced into the diet one at a time. This allows for assessment of the effects of different types of FODMAP on the individual. The final stage involves creation of a long-term diet based on the evidence collected from the previous stage.

=== Medicine === MALDI-TOF spectra are often utilized in tandem with other analysis and spectroscopy techniques in the diagnosis of diseases. MALDI/TOF is a diagnostic tool with much potential because it allows for the rapid identification of proteins and changes to proteins without the cost or computing power of sequencing nor the skill or time needed to solve a crystal structure in X-ray crystallography. One example of this is necrotizing enterocolitis (NEC), which is a devastating disease that affects the bowels of premature infants. The symptoms of NEC are very similar to those of sepsis, and many infants die awaiting diagnosis and treatment. MALDI/TOF was used to identify bacteria present in the fecal matter of NEC positive infants. This study focused on characterization of the fecal microbiota associated with NEC and did not address the mechanism of disease. There is hope that a similar technique could be used as a quick, diagnostic tool that would not require sequencing. Another example of the diagnostic power of MALDI/TOF is in the area of cancer. Pancreatic cancer remains one of the most deadly and difficult to diagnose cancers. Impaired cellular signaling due to mutations in membrane proteins has been long suspected to contribute to pancreatic cancer. MALDI/TOF has been used to identify a membrane protein associated with pancreatic cancer and at one point may even serve as an early detection technique. MALDI/TOF can also potentially be used to dictate treatment as well as diagnosis.

=== Sniper: No Nation (2026) === A covert operation in Costa Verde explodes into an international scandal, and the U.S. government responds by disavowing the Global Response & Intelligence Team (G.R.I.T.), branding its operatives as terrorists. Hunted by the very country he served, Brandon Beckett goes AWOL only to learn that the Phoenix Rebellion, his last remaining allies, has been decimated by the Iron Legion, a mercenary force working for Costa Verde’s ruthless Prime Minister. With fellow soldiers imprisoned and scheduled for public execution, Brandon reunites with his father, legendary sniper Thomas Beckett, brother-in-arms Agent Zero, and a handful of rebels for an off-the-books rescue mission against impossible odds. As time runs out for his friends and global tensions rise, Brandon faces his most dangerous fight yet — without a flag, without backup, and without mercy.

Also included in the Health Services Division are LifeSolutions, an employee assistance program; EBenefits Solutions, a web-based human resources consulting and benefits administration services; and Askesis Development Group, a software development group for behavioral health care.

Sources: en.wikipedia.org

Notes from published material

==== Cyanobactins ==== Cyanobactin biosynthesis requires proteolytic cleavage of both N-terminal and C-terminal portions of the precursor peptide. The defining proteins are thus an N-terminal protease, referred to as the A protein, and a C-terminal protease, referred to as the G protein. The G protein is also responsible for macrocyclization. For cyanobactins, the precursor peptide is referred to as the E peptide. Minimally, the E peptide requires a leader peptide region, a core (structural) region, and both N-terminal and C-terminal protease recognition sequences. In contrast to most RiPPs, for which a single precursor peptide encodes a single natural product via a lone core peptide, cyanobactin E peptides can contain multiple core regions; multiple E peptides can even be present in a single gene cluster. Many cyanobactins also undergo heterocyclization by a heterocyclase (referred to as the D protein), installing oxazoline or thiazoline moieties from Ser/Thr/Cys residues prior to the action of the A and G proteases. The heterocyclase is an ATP-dependent YcaO homologue that behaves biochemically in the same manner as YcaO-domain cyclodehydratases in thiopeptide and linear azol(in)e-containing peptide (LAP) biosynthesis (described above). A common modification is prenylation of hydroxyl groups by an F protein prenyltransferase. Oxidation of azoline heterocycles to azoles can also be accomplished by an oxidase domain located on the G protein. Unusual for ribosomal peptides, cyanobactins can include D-amino acids; these can occur adjacent to azole or azoline residues.

==== Metabolites ==== Desmetramadol is metabolized in the liver into the active metabolite N,O-didesmethyltramadol via CYP3A4 and CYP2B6. The inactive tramadol metabolite N-desmethyltramadol is metabolized into the active metabolite N,O-didesmethyltramadol by CYP2D6.

== Manufacture == BCG is prepared from a strain of the attenuated (virulence-reduced) live bovine tuberculosis bacillus, Mycobacterium bovis, that has lost its ability to cause disease in humans. It is specially subcultured in a culture medium, usually Middlebrook 7H9. Because the living bacilli evolve to make the best use of available nutrients, they become less well-adapted to human blood and can no longer induce disease when introduced into a human host. Still, they are similar enough to their wild ancestors to provide some immunity against human tuberculosis. The BCG vaccine can be anywhere from 0 to 80% effective in preventing tuberculosis for 15 years; however, its protective effect appears to vary according to geography and the lab in which the vaccine strain was grown. Several companies make BCG, sometimes using different genetic strains of the bacterium. This may result in different product characteristics. OncoTICE, used for bladder instillation for bladder cancer, was developed by Organon Laboratories (since acquired by Schering-Plough, and in turn acquired by Merck & Co.). A similar application is the product of Onko BCG of the Polish company Biomed-Lublin, which owns the Brazilian substrain M. bovis BCG Moreau which is less reactogenic than vaccines including other BCG strains. Pacis BCG, made from the Montréal (Institut Armand-Frappier) strain, was first marketed by Urocor in about 2002. Urocor was since acquired by Dianon Systems. Evans Vaccines (a subsidiary of PowderJect Pharmaceuticals).

These illicit pills often contain "a mix of amphetamines, caffeine and various fillers", which are sometimes referred to as "captagon" (with a lowercase "c"). According to some leaks, militant groups export the drug in exchange for weapons and cash. According to Abdelelah Mohammed Al-Sharif, secretary general of the National Committee for Narcotics Control and assistant director of Anti-Drug and Preventative Affairs, forty percent of users between the ages of twelve and twenty-two in Saudi Arabia are addicted to fenethylline. In 2017, fenethylline was the most popular recreational drug in the Arabian Peninsula. In October 2015, a member of the Saudi royal family, Prince Abdel Mohsen Bin Walid Bin Abdulaziz, and four others were detained in Beirut on charges of drug trafficking after airport security discovered two tons of fenethylline pills and some cocaine on a private jet scheduled to depart for Riyadh, the capital of Saudi Arabia. The following month, Agence France-Presse reported that Turkish authorities had seized two tonnes of fenethylline—about eleven million pills—during raids in the Hatay region on the Syrian border. The pills had been produced in Syria and were being shipped to countries in the Arab states of the Persian Gulf. In December 2015, the Lebanese Army announced that it had discovered two large-scale drug production workshops in the north of the country and seized large quantities of fenethylline pills. Two days earlier, three tons of fenethylline and hashish were seized at Beirut Airport, concealed in school desks being exported to Egypt.

Sources: en.wikipedia.org

Frequently asked questions

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.

How does epitalon differ from epithalamin?

Epithalamin refers to a crude preparation derived from bovine pineal tissue, which contains many components. Epitalon is a single synthetic tetrapeptide identified from that material and produced by chemical synthesis. The two names are sometimes confused because early reports treated the synthetic peptide as an active fragment of the extract.

Is epitalon an approved pharmaceutical?

It has been registered for clinical use in Russia, where it is associated with a small family of short peptides. In most other jurisdictions it is not an approved medicine and is traded as a research chemical. Regulatory status varies by country and changes over time.

Why is ultraviolet detection at 214 nanometres used?

The molecule lacks aromatic residues, so it absorbs weakly near 280 nanometres, the wavelength applied to many other peptides. The peptide bond absorbs strongly below 220 nanometres, making 214 nanometres a practical compromise. Gradient methods must therefore use mobile phases with low ultraviolet absorbance to keep the baseline clean.

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