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 2025-09-16. Numbers and descriptions here follow the published literature rather than marketing material.
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.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Amino acid sequence | Ala-Glu-Asp-Gly | Linear tetrapeptide, also written AEDG |
| Molecular mass | About 390.35 g/mol | Value calculated from the sequence |
| Appearance | White to off-white powder | Lyophilised material forms a loose cake |
| Solubility | Freely soluble in water | Also dissolves in isotonic saline |
| Storage | -20 °C, desiccated | Aliquot solutions to avoid freeze–thaw cycling |
The parent extract epithalamin was characterised as a low-molecular-weight fraction of pineal tissue rather than a single defined chemical entity. Researchers fractionated it and tested successive fragments for activity, a screening approach typical of peptide discovery work in that era. Epitalon emerged from that process as one of the shorter sequences of interest. Because the original extract was never fully resolved into individual components, claims about which constituent drives a given effect rest on inference. This distinction matters when reading older reports that attribute extract observations to the tetrapeptide itself.
Epitalon is a synthetic tetrapeptide with the residue sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. Its monoisotopic mass is approximately 390.35 daltons, and it is usually supplied as a lyophilised trifluoroacetate or acetate salt. The compound was derived from a pineal gland extract called epithalamin, a heterogeneous preparation investigated in the former Soviet Union. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology described the tetrapeptide as a constituent fragment of that extract. Commercial material is offered as a laboratory reagent rather than as a finished pharmaceutical product.
Literature searches for this compound must account for several spelling variants. Indexing databases contain epitalon, epithalon, epithalone, and AEDG, and relevant records are scattered across Russian-language and English-language journals that do not consistently cross-cite. Early publications describe the parent extract as a mixture of many peptides, whereas later work addresses the single synthetic tetrapeptide. That shift in nomenclature complicates comparison between studies, because extract data and tetrapeptide data are sometimes cited interchangeably. A search strategy omitting the alternate spellings will return an incomplete set of references.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
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.
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.
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.
It is a synthetic tetrapeptide built from alanine, glutamate, aspartate and glycine. The four residues are joined by standard peptide bonds, giving a linear chain rather than a branched structure.