This is a working overview of AEDG, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2026-05-25 and is reviewed periodically as new material appears.
Animal and clinical reports appear mainly in Russian-language journals from the 1990s and 2000s, covering endpoints such as melatonin rhythm, lifespan in aged rodents, and retinal function. Many of these papers involve small groups, lack blinding or placebo comparison, and are difficult to retrieve through indexed databases. Review articles published in English generally summarise the claims without reanalysing the underlying data. Because no large randomised trial exists, the clinical importance of these reported effects stays unresolved and is properly described as an open question.
No national medicines regulator has approved epitalon as a therapeutic product. It is generally distributed as a research chemical, and in some jurisdictions selling peptides for human consumption without approval is restricted or prohibited. Certificates of analysis accompanying commercial material vary in which tests are performed, and independent verification of identity and purity is uncommon. Statements about anti-ageing or disease-prevention benefits on vendor pages are marketing claims rather than regulatory findings, a distinction that shapes how the compound is discussed in scientific and popular sources alike.
Epitalon is a synthetic tetrapeptide whose four residues are alanine, glutamate, aspartate and glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9 and its monoisotopic mass is near 390.35 daltons. The peptide carries two acidic side chains, so it is neutral to negatively charged in most aqueous buffers. Published reference summaries usually list it under both spellings, epitalon and epithalon, and treat the two names as the same material.
The compound is generally described as a synthetic analogue of a fragment isolated from a pineal gland extract. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology introduced it during the 1980s and 1990s while studying short peptides from animal tissue. The original extract, called epithalamin, is a heterogeneous mixture, whereas epitalon is a single defined sequence. That distinction matters because findings reported for the extract are not automatically findings about the pure tetrapeptide, and claims about broader biological effects remain a separate question from the chemical identity described here.
| Property | Value | Notes |
|---|---|---|
| Regulatory status | Not an approved drug | Marketed in most countries as a research chemical |
| Main literature language | Russian and English | Early reports concentrated in Russian journals |
| Typical stated purity | ≥95% by HPLC | Supplier declaration, seldom independently verified |
| Principal studied endpoint | Telomerase activity in vitro | Measured in cultured human cells |
| Reported administration routes | Subcutaneous, intranasal | Described in exploratory use reports |
Regulatory status varies by country and is not harmonized. Epitalon is not an approved drug in major Western jurisdictions. In some countries it is sold as a research chemical, and in others it has appeared in products marketed for other categories. This inconsistent status means that purity, labeling accuracy, and documentation differ widely between suppliers, and verification of identity and purity through independent analysis is the usual way buyers assess a given lot.
Epitalon appears in the literature primarily through a small number of research groups, most of them associated with the St. Petersburg Institute of Bioregulation and Gerontology. Publications describe cell culture experiments, animal studies, and a limited number of small human studies. Independent replication outside this network is sparse. As a result, reviews of the topic usually separate descriptive reports of observed effects from the question of whether those effects generalize, and they note the difficulty of comparing studies that use different preparations and endpoints.
Analytical characterization of epitalon relies on standard peptide methods. Reverse-phase high-performance liquid chromatography is used to assess purity, and mass spectrometry confirms identity by checking the observed mass against the expected value near 390 daltons. Amino acid analysis can verify composition. Because the peptide is short and hydrophilic, it elutes early on many reverse-phase columns, so method development often requires ion-pairing reagents to achieve adequate retention and resolution from related impurities.
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.
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.
Stability of the tetrapeptide follows ordinary peptide chemistry rather than any unusual structural feature. The aspartate-glycine pair is prone to aspartimide formation under mildly basic or neutral conditions, and deamidation can follow, altering both mass and chromatographic retention. Dry lyophilised powder kept at or below minus twenty degrees Celsius is the usual handling recommendation, with repeated freeze-thaw cycles avoided. Once dissolved in neutral aqueous buffer, degradation proceeds over days to weeks depending on pH and temperature, while acidic conditions generally slow the aspartimide route. A formal stability-indicating study has not been published in the indexed literature.
Because epitalon has no pharmacopoeial monograph, quality assessment depends on supplier documentation and independent testing. Certificates of analysis typically report a purity figure from a single chromatographic run, a measured mass and sometimes an appearance description, but methods and acceptance criteria are not harmonised across vendors. Third-party laboratories can repeat identity and purity measurements, and mismatches between labelled and measured peptide content have been described for research peptides generally. What constitutes adequate identity confirmation for a molecule of this size stays an open question, since mass agreement alone does not separate closely related sequences.
Identity testing for epitalon relies on reversed-phase high-performance liquid chromatography for purity and mass spectrometry for mass confirmation. Because the sequence contains no tryptophan or tyrosine, ultraviolet detection at 280 nanometres is insensitive, so chromatographic methods usually monitor absorbance near 214 nanometres, where the peptide backbone absorbs. Electrospray ionisation or matrix-assisted laser desorption/ionisation then checks the intact mass against the expected value near 390 daltons. Peptide mapping or amino acid analysis after acid hydrolysis can supplement these measurements, although such confirmatory work is seldom reported on commercial certificates of analysis.
The classic click reaction is the copper-catalyzed reaction of an azide with an alkyne to form a 5-membered C2N3 ring. This reaction is the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC). The first triazole synthesis, from diethyl acetylenedicarboxylate and phenyl azide, was reported by Arthur Michael in 1893. Later, in the middle of the twentieth century, this family of 1,3-dipolar cycloadditions took on Rolf Huisgen's name after his studies of their reaction kinetics and conditions.
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== Clinical significance == The proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions. More recently, more effort has been made to consider the proteasome for the development of novel diagnostic markers and strategies. An improved and comprehensive understanding of the pathophysiology of the proteasome should lead to clinical applications in the future. The proteasomes form a pivotal component for the ubiquitin–proteasome system (UPS) and corresponding cellular Protein Quality Control (PQC). Protein ubiquitination and subsequent proteolysis and degradation by the proteasome are important mechanisms in the regulation of the cell cycle, cell growth and differentiation, gene transcription, signal transduction and apoptosis. Proteasome defects lead to reduced proteolytic activity and the accumulation of damaged or misfolded proteins, which may contribute to neurodegenerative disease, cardiovascular diseases, inflammatory responses and autoimmune diseases, and systemic DNA damage responses leading to malignancies.
Sources: en.wikipedia.org
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Activation energies consistent with proline isomerization, which typically has an activation of about 20 kcal/mol. Two-state folding kinetics indicative of both fast-folding and slow-folding populations in the unfolded or denatured state. "Double-jump" assays in which proline-containing proteins are unfolded and refolded, and the population of non-native proline conformations are studied as a function of the extent of folding. Acceleration of the in vitro folding rate by the addition of a prolyl isomerase. Acceleration of the in vitro folding rate in mutant protein variants with one or more proline residues replaced by another amino acid. Not every proline peptide bond is critical to the structure or function of a protein, and not every such bond has a significant influence on folding kinetics, especially trans bonds. Furthermore, some prolyl isomerases have a degree of sequence specificity and therefore may not catalyze the isomerization of prolines in certain sequence contexts.
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==== Croatian ==== Croatian Catholic Union of the United States of America and Canada - Founded in 1921. Headquarters in Hobart, Indiana. Convention meets quadrennially. In 1978 membership was described as being open to Croats and their spouses who are Latin or Greek rite Catholics. In 1997 it was described as open to all Latin or Greek rite Catholics in the United States and Canada. In 1965 the union had 13,772. In 1978 the Union had 119 local units in 16 states and Canada with about 13,500 in 1978. In 1988 it was reported to have 13,000. The union assists the Catholic church, theology students, scholarships, and disaster relief. In addition, the union performs "works of mercy" extended to members who are ill or hospitalized, and arranges sporting events. Merged with the Croatian Fraternal Union in 2006. Croatian Fraternal Union
Sources: en.wikipedia.org
Small studies with human participants have been reported, chiefly in Russian-language journals, but they are limited in size and design. No large randomised controlled trial with published results is available.
The most reproducible biochemical observation comes from cultured cells, where the peptide was reported to raise telomerase activity. Whether this translates into measurable health effects in animals or humans is not established.
It is offered as a research chemical for laboratory use, which places it outside the approval pathways applied to medicines. Buyers should expect documentation to differ between suppliers.
It is a four-amino-acid peptide built from alanine, glutamate, aspartate and glycine in that order. Its formula is C14H22N4O9, and it is made by chemical synthesis rather than extracted from tissue. The synthetic peptide is a single defined molecule, unlike the pineal extracts it is often compared with.