A practical reference on epithalamin: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
This page was last updated on 2025-11-16 and is reviewed periodically as new material appears.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Calculated from the four residues with three water losses |
| Molecular mass | About 390.35 g/mol | Monoisotopic mass near 390.14, used for mass-spectrometric identification |
| Peptide sequence | Ala-Glu-Asp-Gly | Single-letter form AEDG; no disulfide bonds or modified residues |
| Appearance | White to off-white solid | Supplied as a dried powder |
| Isoelectric point | Around 4 | Estimated from aspartate and glutamate side-chain pKa values |
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.
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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=== Primer extension === Primer extension is a two step process that first involves the hybridization of a probe to the bases immediately upstream of the SNP nucleotide followed by a ‘mini-sequencing’ reaction, in which DNA polymerase extends the hybridized primer by adding a base that is complementary to the SNP nucleotide. This incorporated base is detected and determines the SNP allele. Because primer extension is based on the highly accurate DNA polymerase enzyme, the method is generally very reliable. Primer extension is able to genotype most SNPs under very similar reaction conditions making it also highly flexible. The primer extension method is used in a number of assay formats. These formats use a wide range of detection techniques that include MALDI-TOF mass spectrometry (see Sequenom) and ELISA-like methods. Generally, there are two main approaches which use the incorporation of either fluorescently labeled dideoxynucleotides (ddNTP) or fluorescently labeled deoxynucleotides (dNTP). With ddNTPs, probes hybridize to the target DNA immediately upstream of SNP nucleotide, and a single, ddNTP complementary to the SNP allele is added to the 3’ end of the probe (the missing 3'-hydroxyl in didioxynucleotide prevents further nucleotides from being added). Each ddNTP is labeled with a different fluorescent signal allowing for the detection of all four alleles in the same reaction. With dNTPs, allele-specific probes have 3’ bases which are complementary to each of the SNP alleles being interrogated.
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Sources: en.wikipedia.org
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===== Volumetric method ===== The changing of amount of hydrogen stored in the MOF is measured by detecting the varied pressure of hydrogen at constant volume. The volume of adsorbed hydrogen in the MOF is then calculated by subtracting the volume of hydrogen in free space from the total volume of dosed hydrogen.
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Sources: en.wikipedia.org
No. Epithalamin is a peptide-containing extract of bovine pineal glands, while epitalon is a single synthetic tetrapeptide. The extract contains many peptides and other tissue components, so its composition varies between batches in ways that a synthesised sequence does not.
It is not recognised as an endogenous peptide hormone. The four-residue sequence can appear inside larger proteins and in digestive fragments of dietary protein, but no dedicated pathway producing it as a signalling molecule has been identified.
Several cell-culture reports describe increased telomerase activity after treatment, measured by enzyme assays or by transcript levels. Results differ between cell types and laboratories, and measured telomere lengthening has been reported in some studies but not in others, which leaves the physiological relevance open.
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.