epithalamin is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Updated 2025-11-26. Numbers and descriptions here follow the published literature rather than marketing material.
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.
Verification of a sample usually begins with reversed-phase high-performance liquid chromatography, which resolves the peptide from truncated sequences and other impurities and expresses purity as a percentage of total peak area. Mass spectrometry by electrospray ionisation or matrix-assisted laser desorption supplies an independent check, because the measured mass can be compared against the theoretical value for AEDG. Amino acid analysis or tandem mass spectrometry sequencing can confirm residue order. Each of these methods answers a different question: a purity figure does not establish identity, and an identity match does not establish how much of the material is intact peptide.
The molecule is a short, linear, hydrophilic peptide that dissolves readily in water or aqueous buffer. Its principal chemical liabilities are hydrolytic rather than oxidative, since it contains no cysteine, methionine, or tryptophan residues. The aspartate–glycine step is a recognised site for aspartimide formation under mildly acidic or basic conditions, generating isoaspartate and succinimide-related products over time. Desiccated lyophilised powder held at −20 °C is comparatively stable, whereas dilute solutions degrade faster and are best frozen as single-use aliquots rather than thawed repeatedly.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Derived from the four-residue sequence |
| Molar mass | About 390.35 g/mol | Free peptide, counter-ion not included |
| Appearance | White to off-white powder | Lyophilised solid from aqueous solution |
| Water solubility | Freely soluble | Short, polar peptide chain |
| Common synonyms | AEDG; epithalone | Catalogues use the names interchangeably |
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 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.
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.
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.
Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and its calculated monoisotopic mass is approximately 390.35 daltons. The compound does not occur naturally as a free peptide; it is produced by solid-phase peptide synthesis. Because it contains two acidic residues and no basic residues, the neutral form carries a net negative charge at physiological pH. This charge profile influences how the peptide behaves in solution and during chromatographic analysis.
Laboratory-grade epitalon is typically supplied as a lyophilized powder. Purity is commonly assessed with reverse-phase high-performance liquid chromatography, often paired with mass spectrometry to confirm molecular identity. Amino acid analysis and peptide mapping can provide additional confirmation of sequence. Certificates of analysis for research materials frequently report purity above 95 percent, although the methods behind such figures vary between suppliers. The absence of a pharmacopeial monograph means that no single standardized assay defines the compound, so reported results depend on the analytical protocol chosen.
Storage recommendations center on limiting moisture, heat, and light. The dry powder is generally kept at minus 20 degrees Celsius, and some suppliers recommend minus 80 degrees for long-term archival. Once dissolved, solutions are usually aliquoted and frozen to avoid repeated freeze-thaw cycles, which can promote aggregation or degradation. Aqueous stability depends on pH and concentration, and buffered saline is often preferred over plain water for biological work. Stability data specific to epitalon remain limited, so general peptide-handling practices are applied by analogy rather than from product-specific validation.
=== Center for Medicaid Services (CMS) === Under CLIA, it is the role of CMS to issue laboratory certificates and monitor, inspect, and enforce laboratory regulatory compliance based on the tests being performed. In total, CMS covers 260,000 laboratories.
In the case of subtilosin A, isolated from Bacillus subtilis 168, the Cα crosslinks between Cys4 and Phe31, Cys7 and Thr28, and Cys13 and Phe22 are not the only posttranslational modifications; the C- and N-termini form an amide bond, resulting in a circular structure that is conformationally restricted by the Cα bonds. Sactipeptides with antimicrobial activity are commonly referred to as sactibiotics (sulfur to alpha-carbon antibiotic).
Desmetramadol (INNTooltip International Nonproprietary Name), also known as O-desmethyltramadol (O-DSMT), is an opioid analgesic and the main active metabolite of tramadol. Tramadol is demethylated by the liver enzyme CYP2D6 to desmetramadol in the same way as codeine, and so similarly to the variation in effects seen with codeine, individuals who have a less active form of CYP2D6 will tend to have reduced analgesic effects from tramadol. Because desmetramadol itself does not need to be metabolized to induce an analgesic effect, it can be used in individuals with CYP2D6 inactivating mutations. Desmetramadol is commonly encountered as a designer drug online in powder form or as an ingredient in pressed pills due to being unscheduled in many jurisdictions. Outside of its role as a metabolite, a chemical used in research, and as a recreational drug, desmetramadol has a very limited history of human usage and is not approved for medicinal use in any country as of 2025.
Sources: en.wikipedia.org
"Clinical evaluation of De Marco formula as an adjunctive therapy for infected ischemic diabetic foot: a prospective randomized controlled trial". Can J Clin Pharmacol. 16 (2): e381–91. PMID 19966380. DeMarco Peter. "Treatment of Macular Degeneration." United States Patent Application, US 20040180090.
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Sources: en.wikipedia.org
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.
The name derives from epithalamin, a pineal gland extract studied in the former Soviet Union. Researchers proposed that short fragments of that extract carried the biological activity of interest.
No major regulatory agency has approved it as a medicine. It is handled as a research chemical, and products sold under this name are not standardised drugs with defined clinical labelling.
Mass spectrometry provides the identity check, because the observed mass is compared with the theoretical mass of the AEDG sequence. Chromatography separates and quantifies impurities but does not by itself prove which peptide is present. The two techniques are normally used together.