epithalamin comes up often in conversation and rarely with the context attached. Here we lay out the basics in order, then work through the practical considerations.
Updated 2025-10-12. Numbers and descriptions here follow the published literature rather than marketing material.
Documentation accompanying research peptides usually includes a certificate of analysis listing the batch number, purity figure, and test methods applied. Buyers comparing suppliers should check whether the reported purity refers to chromatographic area or to a mass-balance calculation, because the two are not equivalent. Counter-ion content, residual solvents, and water content are sometimes omitted from such certificates even though they affect the actual peptide mass present. Independent verification through a second laboratory is the most direct way to confirm that a supplied material matches its label.
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.
Discussions in the literature often conflate three distinct entities: the pineal extract epithalamin, the isolated tetrapeptide AEDG, and commercial preparations sold under similar names. Reviews citing older Russian-language studies sometimes omit detail on purity, route of administration and control groups, which makes cross-study comparison difficult. Researchers working with the compound generally note the need for independent replication, standardized enzyme assays, and clearer reporting of peptide identity. These caveats are relevant when weighing claims that appear in secondary sources rather than in primary reports.
(TG:@pojiaai)Epitalon is a synthetic linear tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. It emerged from work on epithalamin, a peptide fraction prepared from bovine pineal tissue, and was designed as a short, chemically defined analogue of that extract. Early publications came mainly from Russian laboratories studying pineal peptides and aging-related endpoints. The compound appears in the literature under several spellings, including epithalon and epithalone, which complicates systematic searching. Its small size makes solid-phase assembly and routine analytical characterization straightforward.
| Property | Value | Notes |
|---|---|---|
| Appearance | White to off-white powder | Freeze-dried solid |
| Solubility class | Freely soluble in water | Aqueous buffers also suitable |
| Typical storage temperature | Minus 20 degrees Celsius or colder | Desiccated and light protected |
| Typical analytical method | RP-HPLC with UV detection | 214 nm on C18 column |
| Identity confirmation | Electrospray mass spectrometry | Sequence verified separately |
Material sold for research use varies widely in documented quality. A useful verification package includes a certificate of analysis that states peptide content rather than only net weight, the chromatographic method and column used, and a mass spectrum consistent with the expected mass. Independent testing by a third-party laboratory is occasionally reported. Statements of identity resting only on a supplier label provide little assurance, and the gap between nominal mass and actual peptide content can be substantial once counterions and residual water are counted.
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.
Residue composition is the property that most cleanly separates verified material from mislabelled samples. Alanine, glutamate, aspartate and glycine appear in that order from the N-terminus, and the two acidic residues sit in the middle of the chain. Because the peptide is short, it can be produced by solid-phase synthesis and characterised by mass spectrometry without ambiguity. Any reported sample whose measured mass departs substantially from 390 daltons is a different compound or a degraded mixture rather than epitalon.
Epitalon is a synthetic tetrapeptide whose four residues are alanine, glutamate, aspartate and glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9 and its monoisotopic mass is near 390.35 daltons. The peptide carries two acidic side chains, so it is neutral to negatively charged in most aqueous buffers. Published reference summaries usually list it under both spellings, epitalon and epithalon, and treat the two names as the same material.
The compound is generally described as a synthetic analogue of a fragment isolated from a pineal gland extract. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology introduced it during the 1980s and 1990s while studying short peptides from animal tissue. The original extract, called epithalamin, is a heterogeneous mixture, whereas epitalon is a single defined sequence. That distinction matters because findings reported for the extract are not automatically findings about the pure tetrapeptide, and claims about broader biological effects remain a separate question from the chemical identity described here.
Identity and purity are established with reversed-phase high-performance liquid chromatography and mass spectrometry. The chromatogram shows the main peak and any truncated or oxidised by-products, while the mass spectrum confirms the expected 390 dalton mass. Amino acid analysis can corroborate composition when a sample's origin is uncertain. Counterion content, particularly residual trifluoroacetate from purification, is frequently reported alongside purity because it shifts the net mass of the solid.
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.
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.
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.
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===== Stable Isotope Labeling by Amino Acids in Cell Culture ===== One method uses a variant of Stable isotope labeling by amino acids in Cell Culture (SILAC). SILAC labels proteins with stable isotopes to allow quantification, comparing labelled and unlabeled peptides for quantification. Pulse SILAC (pSILAC) only allows peptides created during the pulse to be labelled. In theory, this allows a capture of only nascent peptides for quantification. SILAC, however, requires similar levels of labelled and unlabelled proteins for accurate quantification. As such, pSILAC pulses have to run much longer than the translation process, making quantification of nascent peptides inaccurate.
==== Metabolism ==== The compound is metabolized by liver enzymes, CYP2D6 and CYP2C9 via aromatic ring oxidation and glucuronidation, then further conjugated by glucuronidation and sulfation. The three active metabolites exhibit only one-tenth of the vasodilating effect of the parent compound. However, the 4'-hydroxyphenyl metabolite is about 13-fold more potent in β-blockade than the parent.
Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Reversed-phase high-performance liquid chromatography with ultraviolet detection at 214 nanometres is the usual approach. Peak area percentage provides a purity figure relative to other components in the sample. Mass spectrometry is then applied to confirm identity.
Aspartate can cyclise into a succinimide intermediate that later hydrolyses back as isoaspartate. Both forms share the same molecular mass, so mass spectrometry alone cannot tell them apart. This shapes how purity data should be interpreted.
Freeze-dried material is normally kept desiccated below minus twenty degrees Celsius and shielded from light. Solutions are prepared shortly before use and held cold. Repeated thawing is avoided because it accelerates aggregation and degradation.
It is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, often abbreviated AEDG. The molecule is linear and contains no modified residues, so it is fully described by its sequence.