en · de · es · fr · pt
epitalon-notes.peptides4800.com › Data › Epitalon Structure And Research Origin — Practical Notes

Epitalon Structure And Research Origin — Practical Notes

By Editorial Desk · published 2025-10-03 · last reviewed 2025-11-22 · Data

A practical reference on AEDG: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.

Reviewed 2025-11-22. Anything still debated is marked as such rather than presented as settled.

Epitalon Structure and Research Origin

Chemically, the molecule consists of four amino acid residues joined by three peptide bonds, with a free N-terminal amino group and a free C-terminal carboxyl group. Its molecular formula is C14H22N4O9, and its monoisotopic mass is approximately 390 daltons. The acidic glutamate and aspartate side chains give the peptide a net negative charge near neutral pH, a property that shapes its chromatographic behaviour and solubility profile. No disulfide bridges or other post-translational modifications are present, so the primary sequence alone defines the structure.

Most experimental work has been carried out in cell culture and animal models. Several reports describe changes in telomerase activity and proliferation in cultured cells, while rodent studies have examined lifespan, melatonin rhythm and reproductive endpoints. Human data remain limited, and much of the published clinical material consists of small trials with incomplete reporting of methods and controls. Whether the cell and animal findings translate into measurable effects in people is an open question, and the mechanistic basis of the reported telomerase changes is not fully established.

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.

Epitalon at a glance

PropertyValueNotes
Chemical classLinear tetrapeptideFour residues joined by three peptide bonds
SequenceAla-Glu-Asp-GlyCommonly abbreviated AEDG
Molecular formulaC14H22N4O9Free acid form
Monoisotopic massApproximately 390 DaMatches values reported from mass spectrometry
Net charge near neutral pHNegativeContributed by glutamate and aspartate side chains

Epitalon Peptide Background and Structure

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.

The proposed relationship between epitalon and pineal function is a central part of its background. Khavinson's group reported that short peptides corresponding to regions of larger pineal proteins could influence gene expression in cells. Epitalon was framed as a synthetic analogue of an active fragment rather than a direct isolation product. Whether the tetrapeptide reproduces the effects of the parent extract is an open question, because comparative studies are limited and the parent extract itself is not a single defined substance.

Related pages on this site

Peptide Identity and Laboratory Handling

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.

Supporting material

=== Indirect discrimination === Although the Fair Work Act 2009 does not expressly distinguish direct and indirect discrimination as other federal legislation does, and state legislation does, if a rule that is neutral on its face has a disparate impact on one group, this will also be unlawful. For example, in Australian Iron & Steel Pty Ltd v Banovic an employer’s policy for redundancy based on “last in, first off” was held to be indirect discrimination against women, who at that mining workplace has mostly only been recently employed. Similarly in Song v Ainsworth Game Technology Pty Ltd a woman won a claim for indirect discrimination, after she was told she could not work full time, and also use her break time to transfer her child from school to after school care. Such a rule disparately impacted women, especially since it was found that other staff could take cigarette breaks without reducing their work hours.

== Further reading == Tucker H (2012). Blood Work: A Tale of Medicine and Murder in the Scientific Revolution. W. W. Norton & Company. ISBN 978-0-393-34223-9. "Milk as a Substitute for Blood Transfusion", historical account, Scientific American, 13 July 1878, p. 19

cell surface receptor Any of a class of receptor proteins embedded within or attached to the external surface of the cell membrane, with one or more binding sites facing the extracellular environment and one or more effector sites that couple the binding of a particular ligand to an intracellular event or process. Cell surface receptors are a primary means by which environmental signals are received by the cell and transmitted across the membrane into the cell interior. Some may also bind exogenous ligands and transport them into the cell in a process known as receptor-mediated endocytosis.

Sources: en.wikipedia.org

Notes from published material

Cytotoxic T cells (TC cells, CTLs, T-killer cells, killer T cells) destroy virus-infected cells and tumor cells, and are also implicated in transplant rejection. These cells are defined by the expression of the CD8 protein on their cell surface. Cytotoxic T cells recognize their targets by binding to short peptides (8-11 amino acids in length) associated with MHC class I molecules, present on the surface of all nucleated cells. Cytotoxic T cells also produce the key cytokines IL-2 and IFNγ. These cytokines influence the effector functions of other cells, in particular macrophages and NK cells.

Correct functioning of agouti requires DNA methylation. Methylation occurs in six guanine-cytosine (GC) rich sequences in the 5’ long terminal repeat of the IAP element in the viable yellow mutation. Methylation on a gene causes the gene to not be expressed because it will cause the promoter to be turned off. In utero, the mother's diet can cause methylation or demethylation. When this area is unmethylated, ectopic expression of agouti occurs, and yellow phenotypes are shown because the phaeomelanin is expressed instead of eumelanin. When the region is methylated, agouti is expressed normally, and grey and brown phenotypes (eumelanin) occur. The epigenetic state of the IAP element is determined by the level of methylation, as individuals show a wide range of phenotypes based on their degree of DNA methylation. Increased methylation is correlated with increased expression of the normal agouti gene. Low levels of methylation can induce gene imprinting which results in offspring displaying consistent phenotypes to their parents, as ectopic expression of agouti is inherited through non-genomic mechanisms. DNA methylation is determined in utero by maternal nutrition and environmental exposure. Methyl is synthesized de novo but attained through the diet by folic acid, methionine, betaine, and choline, as these nutrients feed into a consistent metabolic pathway for methyl synthesis. Adequate zinc and vitamin B12 are required for methyl synthesis as they act as cofactors for transferring methyl groups.

=== Health === DHIS2 is currently in use as a Health Management Information System in more than 75 low- and middle-income countries. 69 of these countries have deployed DHIS2 at national scale. DHIS2 is also used by national health authorities and international health programs and organizations for management of health programs related to specific diseases, such as HIV, TB, and Malaria, among others, as well as for general public health programs such as disease surveillance, routine immunization, and maternal and child health. In 2025, Bangladesh implemented an electronic health information system using the DHIS2 Tracker to manage and evaluate its national cervical screening program. In addition, during the COVID-19 pandemic, 55 countries rapidly deployed or extended DHIS2 for national pandemic response and/or vaccination.

Sources: en.wikipedia.org

Frequently asked questions

What is epitalon chemically?

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.

Where did epitalon research originate?

The compound came out of work on epithalamin, a peptide preparation derived from pineal tissue, conducted largely in Russian laboratories. Later studies in other countries examined it mainly in cell cultures and animal models.

Is epitalon a naturally occurring peptide?

The tetrapeptide sequence is a synthetic construct rather than a described circulating peptide. It was derived by analogy to peptide fractions obtained from tissue extracts, not isolated from blood or tissue as such.

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.

Network