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Epitalon Background And Discovery — Questions and Answers

By Editorial Desk · published 2026-06-03 · last reviewed 2026-06-25 · Info

RP-HPLC raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.

This page was last updated on 2026-06-25 and is reviewed periodically as new material appears.

Epitalon Background and Discovery

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.

Laboratory Handling and Analytical Verification

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
Molecular formulaC14H22N4O9Derived from the four-residue sequence
Molar massAbout 390.35 g/molFree peptide, counter-ion not included
AppearanceWhite to off-white powderLyophilised solid from aqueous solution
Water solubilityFreely solubleShort, polar peptide chain
Common synonymsAEDG; epithaloneCatalogues use the names interchangeably

Epitalon Background and Nomenclature

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.

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.

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Handling, Storage and Analytical Checks

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.

Reference notes

=== Diagnostics === PAH is useful for the measurement of renal plasma flow. The renal extraction ratio of PAH in a normal individual is approximately 0.92. This means that unlike inulin and creatinine, which are filtered in the glomerulus and ignored by the rest of the kidney, aminohippuric acid is both filtered and secreted, being almost entirely removed from the bloodstream in a normal kidney.

Keegan, Sarah; Cortens, John P; Beavis, Ronald C; Fenyö, David (2016). "g2pDB: A Database Mapping Protein Post-Translational Modifications to Genomic Coordinates". Journal of Proteome Research. 15 (3): 983–990. doi:10.1021/acs.jproteome.5b01018. ISSN 1535-3893. PMID 26842767. McAfee, Alison; Harpur, Brock A.; Michaud, Sarah; Beavis, Ronald C.; Kent, Clement F.; Zayed, Amro; Foster, Leonard J. (2016). "Toward an Upgraded Honey Bee (Apis melliferaL.) Genome Annotation Using Proteogenomics". Journal of Proteome Research. 15 (2): 411–421. doi:10.1021/acs.jproteome.5b00589. ISSN 1535-3893. PMID 26718741. Fenyö, David; Beavis, Ronald C. (2015). "Selenocysteine: Wherefore Art Thou?". Journal of Proteome Research. 15 (2): 677–678. doi:10.1021/acs.jproteome.5b01028. ISSN 1535-3893. PMID 26680273. Liu, Fei; Koval, Michael; Ranganathan, Shoba; Fanayan, Susan; Hancock, William S.; Lundberg, Emma K.; Beavis, Ronald C.; Lane, Lydie; Duek, Paula; McQuade, Leon; Kelleher, Neil L.; Baker, Mark S. (2016). "Systems Proteomics View of the Endogenous Human Claudin Protein Family". Journal of Proteome Research. 15 (2): 339–359. doi:10.1021/acs.jproteome.5b00769. ISSN 1535-3893. PMC 4777318. PMID 26680015. Yan, Julia Fangfei; Kim, Hoguen; Jeong, Seul-Ki; Lee, Hyoung-Joo; Sethi, Manveen K.; Lee, Ling Y.; Beavis, Ronald C.; Im, Hogune; Snyder, Michael P.; Hofree, Matan; Ideker, Trey; Wu, Shiaw-lin; Paik, Young-Ki; Fanayan, Susan; Hancock, William S. (2015). "Integrated Proteomic and Genomic Analysis of Gastric Cancer Patient Tissues". Journal of Proteome Research. 14 (12): 4995–5006.

Rickets, a childhood disease, is characterized by impeded growth and soft, weak, deformed long bones that bend and bow under their weight as children start to walk. Maternal vitamin D deficiency can cause fetal bone defects from before birth and impairment of bone quality after birth. Rickets typically presents between 3 and 18 months of age. This condition can be caused by vitamin D, calcium or phosphorus deficiency. Vitamin D deficiency remains the main cause of rickets among young infants in most countries because breast milk is low in vitamin D, and darker skin, social customs, and climatic conditions can contribute to inadequate sun exposure. A post-weaning Western omnivore diet characterized by high intakes of meat, fish, eggs and vitamin-D–fortified milk is protective, whereas low intakes of those foods and high (unfortified) cereal/grain intake contribute to risk. For young children with rickets, supplementation with vitamin D plus calcium was superior to the vitamin alone for bone healing.

Sources: en.wikipedia.org

Notes from published material

== History == In 1948, Arne Tiselius was awarded the Nobel Prize in Chemistry for the discovery of the principle of electrophoresis as the migration of charged and dissolved atoms or molecules in an electric field. The use of a solid matrix (initially paper discs) in a zone electrophoresis improved the separation. The discontinuous electrophoresis of 1964 by L. Ornstein and B. J. Davis made it possible to improve the separation by the stacking effect. The use of cross-linked polyacrylamide hydrogels, in contrast to the previously used paper discs or starch gels, provided a higher stability of the gel and no microbial decomposition. The denaturing effect of SDS in continuous polyacrylamide gels and the consequent improvement in resolution was first described in 1965 by David F. Summers in the working group of James E. Darnell to separate poliovirus proteins. The current variant of the SDS-PAGE was described in 1970 by Ulrich K. Laemmli and initially used to characterise the proteins in the head of bacteriophage T4.

== Chromatographic methods == Reversed phase liquid chromatography (RPLC) is the most important chromatographic method for measuring solute hydrophobicity. The non polar stationary phase mimics biological membranes. Peptide usage has many advantages because partition is not extended by the terminal charges in RPLC. Also, secondary structures formation is avoided by using short sequence peptides. Derivatization of amino acids is necessary to ease its partition into a C18 bonded phase. Another scale had been developed in 1971 and used peptide retention on hydrophilic gel. 1-butanol and pyridine were used as the mobile phase in this particular scale and glycine was used as the reference value. Pliska and his coworkers used thin layer chromatography to relate mobility values of free amino acids to their hydrophobicities. About a decade ago, another hydrophilicity scale was published, this scale used normal phase liquid chromatography and showed the retention of 121 peptides on an amide-80 column. The absolute values and relative rankings of hydrophobicity determined by chromatographic methods can be affected by a number of parameters. These parameters include the silica surface area and pore diameter, the choice and pH of aqueous buffer, temperature and the bonding density of stationary phase chains.

Several international trade union organizations, including the International Trade Union Confederation, Trade Union Confederation of the Americas, and the World Federation of Trade Unions, condemned the attack. Environmental NGOs, including Greenpeace and Oil Change International, have criticised the United States' oil-motivated actions in Venezuela and reiterated calls for a just transition away from fossil fuels. The Federal Council of Switzerland decided to freeze any assets held in the country by Nicolás Maduro.

Sources: en.wikipedia.org

Frequently asked questions

What is epitalon made of?

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.

Why is it called epitalon?

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.

Is epitalon approved for medical use?

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.

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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