Everything below concerns Khavinson. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Updated 2026-05-10. Numbers and descriptions here follow the published literature rather than marketing material.
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.
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.
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.
| Property | Value | Notes |
|---|---|---|
| Amino acid sequence | Ala-Glu-Asp-Gly | Tetrapeptide, often abbreviated AEDG |
| Molecular formula | C14H22N4O9 | Free peptide, unmodified termini |
| Molecular weight | ~390.35 Da | Calculated for the free acid form |
| Appearance | White to off-white powder | Typical lyophilized product form |
| Solubility class | Freely soluble in water | Two acidic residues dominate ionic character |
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.
Discussions in the literature often conflate three distinct entities: the pineal extract epithalamin, the isolated tetrapeptide AEDG, and commercial preparations sold under similar names. Reviews citing older Russian-language studies sometimes omit detail on purity, route of administration and control groups, which makes cross-study comparison difficult. Researchers working with the compound generally note the need for independent replication, standardized enzyme assays, and clearer reporting of peptide identity. These caveats are relevant when weighing claims that appear in secondary sources rather than in primary reports.
（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.
Most ABC transporters that mediate the uptake of nutrients and other molecules in bacteria rely on a high-affinity solute binding protein (BP). BPs are soluble proteins located in the periplasmic space between the inner and outer membranes of gram-negative bacteria. Gram-positive microorganisms lack a periplasm such that their binding protein is often a lipoprotein bound to the external face of the cell membrane. Some gram-positive bacteria have BPs fused to the transmembrane domain of the transporter itself. The first successful x-ray crystal structure of an intact ABC importer is the molybdenum transporter (ModBC-A) from Archaeoglobus fulgidus. Atomic-resolution structures of three other bacterial importers, E. coli BtuCD, E. coli maltose transporter (MalFGK2-E), and the putative metal-chelate transporter of Haemophilus influenzae, HI1470/1, have also been determined. The structures provided detailed pictures of the interaction of the transmembrane and ABC domains as well as revealed two different conformations with an opening in two opposite directions. Another common feature of importers is that each NBD is bound to one TMD primarily through a short cytoplasmic helix of the TMD, the "coupling helix". This portion of the EAA loop docks in a surface cleft formed between the RecA-like and helical ABC subdomains and lies approximately parallel to the membrane bilayer.
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Sources: en.wikipedia.org
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Sources: en.wikipedia.org
Epitalon is a synthetic tetrapeptide composed of four amino acids: alanine, glutamate, aspartate, and glycine. It is written as Ala-Glu-Asp-Gly. The free peptide has a molecular weight of about 390 daltons and is normally supplied as a lyophilized powder.
No. Epitalon is chemically synthesized, not extracted. It was designed as a short synthetic fragment conceptually related to larger pineal peptides studied in the same research tradition, particularly the extract known as epithalamin. The two are distinct materials with different compositions.
The term bioregulator is used in this research tradition for short peptides proposed to influence gene expression or cell function. Epitalon is grouped with other synthetic short peptides under this label. The term reflects a proposed mechanism rather than an established drug classification.
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.