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Chemical Identity And Research Background — Questions and Answers

By Editorial Desk · published 2026-06-01 · last reviewed 2026-07-04 · Wiki

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

This page was last updated on 2026-07-04 and is reviewed periodically as new material appears.

Chemical Identity and Research Background

The compound is described in the literature as a derivative of epithalamin, a preparation obtained from bovine pineal tissue. Work on this peptide family was carried out mainly by a research group in Saint Petersburg beginning in the 1980s, and the substance was later registered for clinical use in Russia under the name Epitalon. Outside that region it is generally treated as a research chemical rather than an approved medicine. Statements about its biological activity rest on a relatively small number of studies, and independent replication remains limited.

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.

Background and Proposed Mechanism

Published evidence comes mainly from Russian-language journals and from a single research group, with small sample sizes and limited independent replication. A few laboratories outside that group have examined related peptides and reported weaker or absent telomerase effects, so the central claim is best described as contested rather than settled. Rodent studies report modest changes in some ageing markers and in survival, but designs vary and control conditions are often sparse. No large randomised trial in humans has been published, and long-term safety data in healthy populations are correspondingly thin.

Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, commonly abbreviated AEDG. It was designed at the St. Petersburg Institute of Bioregulation and Gerontology as a short, chemically defined analogue of epithalamin, a fraction obtained from bovine pineal tissue. Small peptide bioregulators of this type formed a long-running line of work there from the 1980s onward. Because the molecule is produced by solid-phase synthesis rather than extraction, its composition is exact and its purity can be measured directly.

The most frequently cited proposed action is induction of telomerase, the enzyme that adds repeat sequences to chromosome ends. Cell-culture work from the originating group reported higher telomerase reverse transcriptase expression and measurable telomere elongation in human somatic cells after exposure. How a four-residue peptide would reach nuclear gene regulation is not established, and no cell-surface receptor or uptake route has been identified. Additional reports describe changes in melatonin secretion, antioxidant enzyme activity and lipid peroxidation in aged animals, but these findings remain mechanistically unconnected to the telomerase observation.

Epitalon at a glance

PropertyValueNotes
Chemical classSynthetic tetrapeptideFour residues, linear chain
Residue sequenceAla-Glu-Asp-GlySingle-letter form AEDG
Calculated mass390.3 daltonsValue for the free, uncharged form
AppearanceWhite to off-white powderUsually supplied lyophilized
SolubilityFreely soluble in waterOften handled as a salt form

Epitalon Structure and Research Origin

(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.

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.

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Sources: en.wikipedia.org

Notes from published material

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==== MeSH D12.776.860.300.250 – collagen ==== MeSH D12.776.860.300.250.300 – fibrillar collagens MeSH D12.776.860.300.250.300.100 – Type I collagen MeSH D12.776.860.300.250.300.200 – Type II collagen MeSH D12.776.860.300.250.300.300 – Type III collagen MeSH D12.776.860.300.250.300.400 – Type V collagen MeSH D12.776.860.300.250.300.500 – Type XI collagen MeSH D12.776.860.300.250.400 – non-fibrillar collagens MeSH D12.776.860.300.250.400.100 – Type IV collagen MeSH D12.776.860.300.250.400.200 – Type VI collagen MeSH D12.776.860.300.250.400.300 – Type VII collagen MeSH D12.776.860.300.250.400.400 – Type VIII collagen MeSH D12.776.860.300.250.400.500 – Type X collagen MeSH D12.776.860.300.250.400.525 – Type XIII collagen MeSH D12.776.860.300.250.400.537 – Type XVIII collagen MeSH D12.776.860.300.250.400.537.500 – endostatins MeSH D12.776.860.300.250.400.550 – fibril-associated collagens MeSH D12.776.860.300.250.400.550.200 – Type IX collagen MeSH D12.776.860.300.250.400.550.300 – Type XII collagen MeSH D12.776.860.300.250.600 – procollagen MeSH D12.776.860.300.250.700 – tropocollagen

=== Aminoacyl-tRNA synthetase === Each of the 20 amino acids are recognized by its specific aminoacyl-tRNA synthetase. The synthetases are usually composed of one to four protein subunits. The enzymes vary considerably in structure although they all perform the same type of reaction by binding ATP, one specific amino acid and its corresponding tRNA. The most important activity of the aminoacyl-tRNA synthetase is to attach an amino acid to a tRNA, that can then interact with codons that identify its amino acid. Taking both similar acetylation function and amino acid motifs into consideration, 2 separate classes of aminoacyl-tRNA synthetases could be differentiated. Class I enzyme is normally monomeric and binds the tRNA acceptor stem from the minor groove. It adds amino acid to 2’-OH of the adenylate residue, moving it into the 3’-OH position. Meanwhile, Class II aminoacyl-tRNA synthetase is oligomeric and binds the tRNA acceptor stem from the major groove. The enzyme proceeds to add amino acid to the 3’-OH position directly. The aminoacyl-tRNA synthetases can distinguish between different tRNAs and this recognition doesn't follow the same pattern. An aminoacyl-tRNA synthetase recognizes a set of sequentinal elements and binds tRNA with the respective amino acid. Examples of these elements vary: 1 base in the anticodon, 1 of 3 base pairs in the acceptor stem and others. However, depending on the chirality of the amino acid, an aminoacyl-tRNA-synthase can actually disrupt the ester bond between D-amino acids and tRNA.

Slavery is the ownership of a person as property, especially in regard to their labour. It is an economic phenomenon and its history resides in economic history. Slavery typically involves compulsory work, with the slave's location of work and residence dictated by the party that holds them in bondage. Enslavement is the placement of a person into slavery, and the person is called a slave or an enslaved person. Many historical cases of enslavement occurred as a result of breaking the law, becoming indebted, suffering a military defeat, or exploitation for cheaper labor; other forms of slavery were instituted along demographic lines such as race or sex. Slaves would be kept in bondage for life, or for a fixed period of time after which they would be granted freedom. Although slavery is usually involuntary and involves coercion, there are also cases where people voluntarily enter into slavery to pay a debt or earn money due to poverty. In the course of human history, slavery was a common feature of civilization, and existed in most societies throughout history, but it is now outlawed in every country in the world except as a punishment for a crime. In general there were two types of slavery throughout human history: domestic and productive. In chattel slavery, the slave is legally rendered the personal property (chattel) of the slave owner. In economics, the term de facto slavery describes the conditions of unfree labour and forced labour that most slaves endure.

Sources: en.wikipedia.org

Frequently asked questions

Which amino acids make up epitalon?

The peptide contains four residues in the order alanine, glutamate, aspartate and glycine, abbreviated AEDG. The chain is linear and held together by three peptide bonds. Its calculated mass for the uncharged free form is about 390.3 daltons.

How does epitalon differ from epithalamin?

Epithalamin refers to a crude preparation derived from bovine pineal tissue, which contains many components. Epitalon is a single synthetic tetrapeptide identified from that material and produced by chemical synthesis. The two names are sometimes confused because early reports treated the synthetic peptide as an active fragment of the extract.

Is epitalon an approved pharmaceutical?

It has been registered for clinical use in Russia, where it is associated with a small family of short peptides. In most other jurisdictions it is not an approved medicine and is traded as a research chemical. Regulatory status varies by country and changes over time.

Is epitalon the same substance as epithalamin?

No. Epithalamin is a peptide-containing extract of bovine pineal glands, while epitalon is a single synthetic tetrapeptide. The extract contains many peptides and other tissue components, so its composition varies between batches in ways that a synthesised sequence does not.

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