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Background And Chemical Identity — Deep Dive

By Editorial Desk · published 2026-02-20 · last reviewed 2026-03-15 · Data

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

Reviewed 2026-03-15. Anything still debated is marked as such rather than presented as settled.

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.

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.

Epitalon at a glance

PropertyValueNotes
Amino acid sequenceAla-Glu-Asp-GlyLinear tetrapeptide, also written AEDG
Molecular massAbout 390.35 g/molValue calculated from the sequence
AppearanceWhite to off-white powderLyophilised material forms a loose cake
SolubilityFreely soluble in waterAlso dissolves in isotonic saline
Storage-20 °C, desiccatedAliquot solutions to avoid freeze–thaw cycling

Peptide Identity and Research Origin

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.

The published literature is dominated by a small number of research groups, much of it in Russian-language journals, and independent replication outside those groups is limited. Studies are typically small, use cultured cells or rodent models, and report endpoints that differ between papers, which makes comparison difficult. Large randomised human trials have not appeared in the indexed literature. Questions about absorption, distribution and clearance are therefore still treated as open in reviews that mention the compound.

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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.

Epitalon Background and Discovery

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.

Published studies on epitalon are dominated by a small number of research groups, and independent replication in other laboratories remains limited. Proposed mechanisms include activation of telomerase and modulation of melatonin rhythms, but the evidence for either rests mainly on cell cultures and animal models. Whether the peptide produces comparable effects in humans is an open question, and the absence of large controlled trials means the literature is best read as exploratory rather than settled.

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.

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.

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.

Reference notes

== Drying of porous silicon == Porous silicon is systematically prone to presence of cracks when the water is evaporated. The cracks are particularly evident in thick or highly porous silicon layers. The origin of the cracks has been attributed to the large capillary stress due to the minute size of the pores. In particular, it has been known that cracks will appear for porous silicon samples with thickness larger than a certain critical value. Bellet concluded that it was impossible to avoid cracking in thick porous silicon layers under normal evaporating conditions. Hence, several appropriate techniques have been developed to minimize the risk of cracks formed during drying.

Blood sugar levels are regulated by negative feedback in order to keep the body in balance. The levels of glucose in the blood are monitored by many tissues, but the cells in the pancreatic islets are among the most well understood and important. Granule docking is an important glucose-dependent step in human insulin secretion that does not work properly in type 2 diabetes.

During the Second World War penicillin became an important part of the Allied war effort, saving thousands of lives. Alexander Fleming, Howard Florey and Ernst Chain shared the 1945 Nobel Prize in Physiology or Medicine for the discovery and development of penicillin. After the end of the war in 1945, penicillin became widely available. Dorothy Hodgkin determined its chemical structure, one of the achievements for which she received the Nobel Prize in Chemistry in 1964. This led to the development of semisynthetic penicillins that were more potent and effective against a wider range of bacteria. The drug was synthesised in 1957, but cultivation of mould remains the primary means of production. It was discovered that adding penicillin to animal feed increased weight gain, improved feed-conversion efficiency, promoted more uniform growth and facilitated disease control. Agriculture became a major user of penicillin. Shortly after their discovery of penicillin, the Oxford team reported penicillin resistance in many bacteria. Research that aims to circumvent and understand the mechanisms of antibiotic resistance continues.

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=== Defense against infections === PGLYRP2 plays a limited role in host defense against infections. PGLYRP2-deficient mice are more sensitive to Pseudomonas aeruginosa-induced keratitis and Streptococcus pneumoniae-induced pneumonia and sepsis. However, PGLYRP2-deficient mice did not show a changed susceptibility to systemic Escherichia coli, Staphylococcus aureus, and Candida albicans infections or intestinal Salmonella enterica infection, although the latter was accompanied by increased inflammation in the cecum. Although PGLYRP2 is not directly bacteriolytic, it has antibacterial activity against both Gram-positive and Gram-negative bacteria and Chlamydia trachomatis. Human and mouse PGLYRP2 promote hepatitis B virus (HBV) clearance in vitro in hepatocytes and in HBV-infected mice. PGLYRP2 through its HBV DNA-binding domain recognizes covalently closed circular DNA (cccDNA) of HBV sequestering it in the nucleus and separating it from the cellular viral replication machinery. Additionally, PGLYRP2 suppresses HBV capsid assembly by directly interacting through its PGRP domain with the viral capsid and promoting secretion of the PGLYRP2-HBV capsid complexes.

Sources: en.wikipedia.org

Notes from published material

The Rush website, newly redesigned on March 12, 2007, to support the new album, also announced that the band would embark on a tour to begin in the summer. Snakes & Arrows was released on May 1, 2007, in North America, where it debuted at No. 3 on the Billboard 200 with approximately 93,000 units sold in its first week. It peaked at No. 3 in Canada and No. 13 in the UK, selling an estimated 611,000 copies worldwide. Coinciding with the beginning of Atlantic Ocean hurricane season, "Spindrift" was released as the official second radio single on June 1, 2007, while "The Larger Bowl (A Pantoum)" came out as a single on June 25, 2007. "The Larger Bowl" peaked within the top 20 of both the Billboard Mainstream Rock and Mediabase Mainstream charts, but "Spindrift" failed to appear on any commercial chart. The planned intercontinental tour in support of Snakes & Arrows began on June 13, 2007, in Atlanta, coming to a close on October 29, 2007, at Hartwall Arena in Helsinki, Finland. The 2008 portion of the Snakes & Arrows tour began on April 11, 2008, in San Juan, Puerto Rico, at José Miguel Agrelot Coliseum, and concluded on July 24, 2008, in Noblesville, Indiana at the Verizon Wireless Music Center. On April 15, 2008, the band released Snakes & Arrows Live, a double live album documenting the first leg of the tour, recorded at the Ahoy arena in Rotterdam, Netherlands on October 16 and 17, 2007. A DVD and Blu-ray recording of the same concerts was released on November 24, 2008.

== Signs and symptoms == Signs and symptoms of MSUD vary between patients and are greatly related to the amount of residual enzyme activity. Some characteristics of MSUD include maple syrup odor to the urine or earwax, neurological disorders, psychological disorders, feeding problems, and metabolic acidosis. If left untreated, it may lead to metabolic crisis. Metabolic crises can be life-threatening and should be treated immediately.

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The characteristics of seed lotus cultivars are a large number of carpels and seed sets as well as large seeds with better nutritional properties. Roots of these varieties are thin, fibrous, and do not form good rhizomes. The main popular cultivars for seed production in China are Cunsanlian, Xianglian 1, Zilian 2, Jianlian, Ganlian 62, and Taikong 36. The average yield of these cultivars in China is 1.05–1.9 t/ha (0.5–0.8 tons/acre) of dry seeds and weight of thousand seeds between 1,020 and 1,800 g (36 and 63 oz). Green Jade and Vietnam-Red are recommended cultivars for seed production in Australia.

Sources: en.wikipedia.org

Frequently asked questions

Is epitalon a natural substance?

It is a synthetic tetrapeptide. Its sequence was derived from research on peptide fractions of bovine pineal extract, and the intact AEDG sequence has not been demonstrated as an abundant free peptide in human tissue.

What does the abbreviation AEDG mean?

AEDG is the one-letter code for the four amino acids alanine, glutamate, aspartate and glycine in that order. The same molecule is written in three-letter form as Ala-Glu-Asp-Gly.

How is the identity of epitalon confirmed in a laboratory?

Identity is normally confirmed by mass spectrometry against the calculated mass of roughly 390.35 g/mol. Purity is then estimated by reversed-phase high-performance liquid chromatography with ultraviolet detection.

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.

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