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Identity And Research Background — Quick Reference

By Editorial Desk · published 2026-06-02 · last reviewed 2026-06-27 · News

reversed-phase HPLC 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 2026-06-27. Numbers and descriptions here follow the published literature rather than marketing material.

Identity and Research Background

The peptide is a synthetic analogue of epithalamin, a preparation extracted from bovine pineal glands. Investigators sought a short, chemically defined molecule that would reproduce some of the endocrine and gerontological observations attributed to the glandular extract. Proposed mechanisms centre on induction of telomerase activity, an effect reported in cultured human somatic cells in the early 2000s, together with influences on melatonin secretion and neuroendocrine regulation. Those mechanisms remain incompletely characterised, and the reported telomerase response has not been consistently reproduced by independent groups working in comparable systems.

Published work on this compound consists mainly of in vitro experiments, animal studies, and small clinical investigations, a substantial share of which appeared in Russian-language journals. Sample sizes are generally small, control conditions differ between studies, and several endpoints rely on markers whose clinical meaning is itself debated. Reviews of the longevity field treat the peptide as an early example of telomerase-directed research rather than an established intervention. Regulatory treatment varies by country: some jurisdictions place it under prescription controls, others treat it as a laboratory material, and importation may be restricted regardless of local status.

Epitalon is a synthetic tetrapeptide whose sequence is alanine–glutamate–aspartate–glycine, commonly abbreviated AEDG. It was developed in Russia during the 1980s and 1990s by investigators associated with the St. Petersburg Institute of Bioregulation and Gerontology, who studied short peptides as regulators of gene expression and tissue function. The alternative spelling epithalon appears interchangeably in the literature, and the two names refer to the same molecule. Outside Russia it is encountered chiefly as a research chemical rather than a licensed medicine, and it holds no approval from the United States Food and Drug Administration or the European Medicines Agency.

Laboratory Handling and Analytical Verification

Identity is normally established by reversed-phase high-performance liquid chromatography combined with mass spectrometry, a pairing that separates components and confirms molecular mass at once. Purity is quoted as a percentage from the chromatogram, and figures above ninety-five percent are a frequent commercial specification. Amino acid analysis or sequencing supplies further confirmation when required. Because many short peptides behave similarly under chromatography, retention time alone does not establish sequence; the mass measurement is what separates one tetrapeptide from another, and certificates should report both.

Short peptides such as AEDG are normally supplied as a freeze-dried solid and are kept dry, cold, and shielded from light. Holding at minus twenty degrees Celsius is common for the long term, while a refrigerator suffices for brief periods before use. The material takes up moisture to some degree, so containers should stay sealed and be allowed to reach room temperature before opening, which limits condensation on the contents. Repeated warming and cooling of a single container is discouraged because it admits water and can lower the amount of intact peptide.

Dissolution is usually performed in water or a suitable aqueous buffer, and the resulting liquid is divided into single-use portions before freezing. Freeze-thaw cycling is a recognised source of loss for short peptides, since each cycle can encourage aggregation or adsorption onto container walls. Working solutions are generally kept cold and used within a short window, although published stability data specific to epitalon are thin. Containers should be marked with concentration and date, and solutions examined for cloudiness before use.

Epitalon at a glance

PropertyValueNotes
Peptide sequenceAla-Glu-Asp-GlyOften abbreviated AEDG in research literature
Common synonymsEpithalon, epitalon, AEDGSpelling variants refer to the same tetrapeptide
Molecular formulaC14H22N4O9Theoretical monoisotopic mass near 390.35 Da
AppearanceWhite to off-white powderTypically supplied as a lyophilised solid
Solubility classFreely soluble in waterHydrophilic peptide; dissolves in aqueous buffer

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.

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Analytical Methods And Handling

Identity confirmation uses mass spectrometry, usually electrospray ionisation in positive mode or matrix-assisted laser desorption. The protonated free peptide produces a signal near three hundred and ninety-one daltons, while salt adducts shift that value slightly. Tandem mass spectrometry or amino acid analysis supplies sequence-level confirmation, which a single mass measurement cannot. Peptides containing aspartate can cyclise into succinimide intermediates that hydrolyse to isoaspartate isomers of identical mass. Because those isomers are difficult to separate chromatographically, identity and purity results carry more weight when interpreted together.

Storage practice centres on limiting moisture, oxygen, and repeated temperature cycling. Freeze-dried powder is generally held desiccated at minus twenty degrees Celsius or colder and protected from light. Reconstituted solutions are markedly less stable, and the aspartate-glycine junction is prone to succinimide formation at neutral to mildly alkaline pH. Portioning material into single-use aliquots reduces degradation compared with repeated freeze-thaw cycles. Stability data specific to this tetrapeptide remain scarce, so most handling guidance is extrapolated from general peptide chemistry rather than measured directly.

Chemical Identity and Research Background

In its supplied form epitalon is a white to off-white powder, usually lyophilized and often hygroscopic. It dissolves readily in water and in aqueous buffers, and it is commonly handled as the acetate or trifluoroacetate salt to improve stability during purification and drying. The amide backbone is labile in aqueous media, so solutions are less durable than the dry solid. Handling notes in the chemical literature therefore emphasize keeping the powder dry, cool and shielded from light until it is dissolved.

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.

Supporting material

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Surfactant molecules have either one tail or two; those with two tails are said to be double-chained. Amino acid-based surfactants are surfactants derived from an amino acid. Their properties vary and can be either anionic, cationic, or zwitterionic, depending on the amino acid used and which part of the amino acid is condensed with the alkyl/aryl chain. Gemini surfactants consist of two surfactant molecules linked together at or near their head groups. Compared to monomeric surfactants, they have much lower critical micelle concentrations.

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== Further reading == Robinson, David A. (2008), "Field Estimation of Soil Water Content: A Practical Guide to Methods, Instrumentation and Sensor Technology" (PDF), Soil Science Society of America Journal, 73 (4), Vienna, Austria: International Atomic Energy Agency: 131, Bibcode:2009SSASJ..73.1437R, doi:10.2136/sssaj2008.0016br, ISSN 1018-5518, IAEA-TCS-30 Wessel-Bothe, Weihermüller (2020): Field Measurement Methods in Soil Science. New practical guide to soil measurements explains the principles of operation of different moisture sensor types (independent of manufacturer), their accuracy, fields of application and how such sensors are installed, as well as subtleties of the data so obtained. Also deals with other crop-related soil parameters.

The science of collecting and analyzing biologic or health data using statistical methods. Biometry may be used to help learn the possible causes of a disease in a certain group of people. Also called biostatistics and biometrics. (NCI) Biostatistics

Sources: en.wikipedia.org

Supporting material

The amino acid positions of population variants and variants with known clinical relevance in the Ensembl Variation database as well as predicted benign and pathological variants from AlphaMissense can also be displayed.. The Interaction resource focuses on various aspects of human protein interactions, including reported experimental protein-protein interactions and their prediced three-dimensional structures as well as metabolic interactions and pathways. The data is based on external sources complemented with "in-house" analysis. Here you can explore: - Predicted 3D structures for consensus protein-protein interactions - Protein-protein interaction networks for most genes - Features such as subcellular location and expression specificity displayed on the interaction networks - Pathways/subsystems of metabolic genes and metabolic pathways from the Metabolic Atlas.

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== Further reading == Hassan, Shira; Lewis, Deana G. (2022). Saving our own lives: a liberatory practice of harm reduction. Chicago, IL: Haymarket Books. ISBN 978-1-64259-841-4. OCLC 1315537122. Szalavitz, Maia (2021). Undoing Drugs: How Harm Reduction Is Changing the Future of Drugs and Addiction. New York: Hachette Book Group. ISBN 978-0-7382-8575-7. Vakharia, Sheila P. (2024). The harm reduction gap: helping individuals left behind by conventional drug prevention and abstinence-only addiction treatment. New York: Routledge Taylor & Francis Group. ISBN 978-1-003-30174-5.

Sources: en.wikipedia.org

Supporting material

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Sources: Monocytes; Dendritic cells; Primary T cells; Mast cells; Granulocytes; Macrophages; Adipocytes; Endothelial cells Most complement systems are synthesized by hepatocytes in the liver, however, properdin is synthesized by neutrophils, monocytes, and T cells. Properdin is a positive regulator of the alternative pathway through its mechanism of stabilizing the C3 convertase (C3bBb). Primary T cells, monocytes, macrophages, dendritic cells, granulocytes, and mast cells synthesize mRNA to secrete properdin. Functional properdin is a product of human liver-derived HEP G2 cells. Properdin localized in the granules of neutrophils are released by TNF, TNF/fMLP, PMA, C5a, or IL-8. Additionally, neutrophils promote complement activation upon binding of cytokines, which stabilizes the alternative pathway via release of properdin, increasing defense against microorganisms. Properdin sourced from T cells promote phagocytosis of apoptotic T cells, which is an indication of their function in recognizing and clearing out apoptotic cells. Properdin is also sourced in endothelial cells along with the other complement proteins. Endothelial gene transcripts are induced when shear stress occurs, followed by properdin release into extracellular compartments. Properdin plays an important role in tissue regulation, energy metabolism, and lipid metabolism. An experiment in properdin deficient mice concluded that properdin deficiency results in fat storage and less energy output in comparison to wild-type mice. Properdin regulates fatty acid uptake into adipose tissue.

Sources: en.wikipedia.org

Frequently asked questions

What is epitalon?

Epitalon is a synthetic four-amino-acid peptide with the sequence alanine–glutamate–aspartate–glycine, also written AEDG. It was developed in Russian gerontology research and is studied for proposed effects on telomerase, melatonin regulation, and neuroendocrine function. It is not an approved pharmaceutical in the United States or the European Union.

Is epitalon the same as epithalamin?

No. Epithalamin is a peptide-rich extract prepared from bovine pineal glands, while epitalon is a short synthetic peptide designed as a defined analogue of it. The synthetic version was intended to provide a reproducible molecule with some of the same proposed biological activity.

Has epitalon been shown to lengthen telomeres in humans?

Telomere elongation and telomerase activation have been reported in cultured human somatic cells, but evidence from living human subjects is limited and has not been independently confirmed at scale. Reported findings come largely from small studies with differing designs, so the question remains open rather than settled.

How is epitalon identified in a laboratory?

Reversed-phase high-performance liquid chromatography is run alongside mass spectrometry. The chromatogram separates components and gives a purity figure, while the mass spectrum confirms that the measured molecular mass matches the expected sequence. Neither measurement on its own is treated as sufficient.

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