pe
pep-10943 v1 CC-BY-SA-4.0

Ovagen: synthetic anti-aging peptide for ovarian and liver health

A tiny three-amino-acid synthetic peptide developed to help restore normal function in aging ovarian and liver tissue; experimental, not yet an approved drug.

statusdesigned target? length4 aa refs1
snapshot sparse 0% confidence
Class
Synthetic Khavinson bioregulator tripeptide
Status
Not approved by any major regulatory authority; sold in Russia as a dietary supplement / functional food
Best-supported effect
No peptide-specific human or animal efficacy data identified; all mechanistic and therapeutic claims are extrapolated from the broader Khavinson short-peptide framework
Main caveat
No PubMed-indexed studies of the EDL sequence itself have been identified; the entire evidence base for Ovagen consists of class-level extrapolation and marketing material, not peptide-specific data
status 1 / 5
sequence4 aa
14
EDLA
overview readme

What this is

Ovagen is a tiny synthetic peptide — just three amino acids, glutamic acid, aspartic acid, and leucine (Glu-Asp-Leu, abbreviated EDL) — developed by Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology. It belongs to the Khavinson bioregulator family: short, chemically defined synthetic peptides proposed to restore normal gene activity in tissues whose function declines with age. Ovagen is the synthetic counterpart to Svetinorm, a peptide complex prepared from animal liver tissue; where Svetinorm is a natural extract (a Cytomax), Ovagen is the single synthesized sequence intended to reproduce its proposed active fragment (a Cytogen). The proposed target tissues are the liver and the gastrointestinal mucosa.

A note on the stored sequence: the platform record stores "EDLA" (four residues), but every peer-reviewed and commercial source identifies Ovagen as a tripeptide Glu-Asp-Leu (EDL). The trailing alanine appears to be a data-entry artefact; the biologically proposed and commercially marketed entity is the three-residue EDL sequence.

History

The Khavinson bioregulator program began in the early 1980s under Soviet military medicine auspices, when Khavinson's group started systematically fractionating organ and tissue extracts to isolate their shortest active peptide components. The general approach was to reduce a complex organ extract — starting with multi-peptide Cytomaxes derived from pineal gland, thymus, liver, pancreas, and other tissues — into the minimal sequence that retained organ-tropic activity, then synthesize that sequence as a chemically defined Cytogen.

Ovagen emerged from the liver fraction of this program. Its natural-extract counterpart, Svetinorm, is prepared from liver tissue of young animals and has been marketed within Russia as an oral hepatoprotective dietary supplement since the 1990s. EDL was proposed as the "distilled" active fragment. Khavinson's 2016 comparative study of short peptides and their DNA-binding properties listed Ovagen (EDL) among 19 Khavinson-program peptides characterized by computational docking, noting a ctcc preferred binding motif and a moderate-to-strong (++) activity rating relative to other peptides in the panel (Khavinson and colleagues, Bulletin of Experimental Biology and Medicine*, 2016). That publication represents the most direct peer-reviewed reference to the EDL sequence specifically.

Among the Khavinson bioregulators, Ovagen sits at the thin end of the published-evidence distribution. Unlike Epithalon (/card/pep-00008) or Pancragen (/card/pep-10935), whose sequences have accumulated dedicated preclinical study, no PubMed-indexed experiments use the EDL tripeptide as the test article. Ovagen's position in the Khavinson catalog rests almost entirely on the framework-level claims of the broader research program, extrapolated to liver tissue.

What it does

In the Khavinson bioregulator model, short di- and tripeptides are proposed to enter cells, reach the nucleus, and bind directly to regulatory regions of DNA — influencing which genes are switched on or off in a tissue-specific manner. For Ovagen, the proposed target is liver and gastrointestinal epithelial cells: the peptide is theorized to bind chromatin, reduce DNA condensation in aging hepatocytes, and restore expression of genes involved in hepatocellular protein synthesis, detoxification, and antioxidant defense.

The framework underlying these claims has been described in a series of reviews by Khavinson's group spanning from 2016 to 2021. A 2016 paper used computational docking to model interactions between 19 short peptides — including Ovagen — and double-stranded DNA, finding sequence-specific binding in regulatory regions; Ovagen was assigned a ctcc preferred binding motif (Khavinson and colleagues, Bulletin of Experimental Biology and Medicine, 2016). A 2021 systematic review summarized evidence that short peptides of 2–7 residues can penetrate cell nuclei, interact with nucleosomes and histone proteins, and modulate transcription across multiple tissues (Khavinson, Popovich, Linkova, and colleagues, Molecules, 2021). A 2020 study examined how short peptides modulate gene expression patterns in aging human mesenchymal stem cell cultures, providing a cellular-level demonstration of the class effect (Ashapkin, Khavinson, Shilovsky, Linkova, and Vanuyshin, Molecular Biology Reports*, 2020).

None of these studies use EDL as the experimental peptide. The proposed hepatic activity of Ovagen specifically is theoretical — extrapolated from the class-level framework and from analogy with better-characterized sibling peptides.

Evidence

  • Human: No published human clinical trials specific to Ovagen or the EDL tripeptide are indexed in PubMed. No registered trials appear in ClinicalTrials.gov for "Ovagen" or "Glu-Asp-Leu." The peptide has not been evaluated in blinded randomized controlled trials for any indication including NAFLD/MASLD, viral hepatitis, alcoholic liver disease, or cirrhosis.
  • Animal: No PubMed-indexed preclinical studies using EDL as the test article have been identified. The theoretical hepatoprotective rationale rests on the broader Khavinson short-peptide framework demonstrated in other sequences.
  • In vitro: The 2016 computational docking study placed Ovagen (EDL) in a comparative table of 19 Khavinson-program peptides and assigned it a ctcc DNA-binding motif and a ++ activity rating (Khavinson and colleagues, Bulletin of Experimental Biology and Medicine*, 2016). This is a modelling result, not a wet-lab binding or transcription assay for EDL specifically.

Known effects

  • Liver tissue support / hepatoprotection — Proposed; extrapolated from broader Khavinson bioregulator framework. No EDL-specific evidence. Evidence level: Mechanistic only (computational modelling).
  • GI mucosal protection — Proposed target tissue; no EDL-specific preclinical or clinical data. Evidence level: Mechanistic only.
  • Antioxidant defense in hepatocytes — Proposed downstream effect of gene-expression remodelling; no direct measurement for EDL. Evidence level: Mechanistic only.

Myths and misconceptions

  • "Ovagen is well-studied as a liver bioregulator." The EDL sequence has no PubMed-indexed experiments of its own. The Khavinson program has studied dozens of short peptides, and some — Epithalon, Thymagen (/card/pep-10919), Pancragen (/card/pep-10935) — have accumulated dedicated experimental data. Ovagen is not among them. The peptidelist catalog (2026) rates overall confidence at 15%.
  • "Because Ovagen is the synthetic version of Svetinorm, it shares Svetinorm's evidence base." Svetinorm is itself a thinly published Cytomax preparation. Even granting that Cytogens inherit their parent extract's evidence, Svetinorm's footprint is narrow and does not meaningfully extend the case for EDL specifically.
  • "Oral Ovagen reaches the liver." Oral bioavailability of intact EDL has not been measured. Inferring liver-specific exposure from the fact that some short peptides survive intestinal digestion is a theoretical step without EDL-specific pharmacokinetic data.
  • "Russian dietary-complex registration equals drug approval." Ovagen-containing products are sold in Russia as oral peptide bioregulator capsules positioned as functional food, not as registered prescription medicines. This is not equivalent to EMA, FDA, or MHRA drug approval.

Safety signals

No EDL-specific safety data exists in the peer-reviewed literature. General tolerability claims in the Khavinson program are based on the broader bioregulator series and on the physiological origin of the sequences — but this reasoning applies at the class level, not to Ovagen specifically. No chronic dosing data in any species at any dose has been published for EDL.

Regulatory status

  • US: Not FDA-approved for any indication. Not recognized as a dietary supplement ingredient under DSHEA. Not on the FDA's compounding-eligible peptide list.
  • EU / UK / other: Not authorized as a medicine by EMA, MHRA, TGA, or Health Canada.
  • Russia: Sold as an oral dietary supplement / functional food under the Khavinson Peptides brand (Peptides.ru). Not a registered prescription medicine in Russia either.
  • WADA: Not specifically named on the WADA Prohibited List. Because no regulatory authority has approved Ovagen for human therapeutic use, it is reasonably read as falling under WADA's S0 catch-all category (non-approved substances).

Related peptides

  • Epithalon — the AEDG tetrapeptide from the same Khavinson Cytogen family; pineal / longevity focus; the most extensively published of the Khavinson synthetic peptides.
  • Pancragen — KEDW tetrapeptide; the pancreas-targeted Cytogen from the same program; more directly studied than Ovagen for its proposed target tissue.
  • Thymagen — EW dipeptide; thymus-targeted Khavinson Cytogen; registered as a pharmaceutical in Russia; shares the bioregulator lineage.
Hypotheses3 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Does EDL appear to target the liver only because it survives long enough to get there, while similar peptides get chewed up before reaching other organs?

If organ tropism in this peptide family is driven by digestive stability rather than cell recognition, designing better-targeted peptides would become much simpler. It could also explain why some batches or formulations work differently from others.

The hypothesis
The organ-tropism ascribed to EDL (liver and GI) versus the closely related EDG (lung, Chonluten) is not intrinsically encoded in the peptide sequence but is instead an artefact of differential proteolytic stability: EDL's C-terminal leucine resists leucine aminopeptidase cleavage that rapidly inactivates EDG's C-terminal glycine, giving EDL a longer effective half-life specifically in hepatic portal circulation where leucine aminopeptidase activity is high.
Why it’s plausible
Leucine and glycine differ dramatically as C-terminal residues: leucine is bulky and resists several exopeptidases, while glycine is a minimal residue rapidly released. Hepatic portal blood has high leucine aminopeptidase (LAP) activity. If the intact tripeptide is the active form, EDL would survive portal passage that destroys EDG, creating apparent liver selectivity from pharmacokinetic rather than receptor-binding differences.
Why it matters
This hypothesis is falsifiable by comparing EDL and EDG plasma half-lives in portal versus systemic blood, and it would reframe the entire Khavinson organ-tropism concept as metabolic rather than receptor-mediated, with major implications for rational design of the peptide series.
Plausibility.60
Novelty.70
Impact.60
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceEDL ends in leucine; EDG (Chonluten) ends in glycine. These C-terminal residues have substantially different susceptibility to exopeptidases, particularly leucine aminopeptidase.
[2]
paper
Amino acid substitutions can definitively confer or remove protease resistance; C-terminal residue identity is a primary determinant of exopeptidase susceptibility.
doi: 10.3389/fmicb.2020.563030
[3]
noteThe Khavinson framework assigns EDL to liver/GI and EDG to lung/bronchi, but provides no molecular receptor-binding basis for this distinction, leaving pharmacokinetic explanations untested.
openupdated 2026-06-05

If EDL were bent into a circular shape instead of a straight chain, would it resist being broken down in the stomach and gut while still doing the same job?

Most short peptide supplements are destroyed almost instantly during digestion. A ring-shaped version that survives long enough to be absorbed could turn a poorly characterised supplement into a real medicine with predictable dosing and effects.

The hypothesis
Cyclisation of EDL into a head-to-tail cyclic tripeptide (cyclo-EDL) would dramatically increase proteolytic half-life in GI fluid while preserving the acidic-face geometry required for chromatin or receptor interaction, making cyclo-EDL a bioavailable oral agent where linear EDL is not.
Why it’s plausible
Linear tripeptides are extremely short-lived in GI and plasma environments. Cyclic tripeptides, such as cyclo-RGD analogues, can be orally bioavailable and protease-resistant. The Glu-Asp acidic patch and the Leu hydrophobic residue would be retained in a cyclic backbone, preserving the proposed pharmacophore while eliminating the free N- and C-termini that are the primary sites of exopeptidase attack. This approach has not been described for any Khavinson tripeptide.
Why it matters
If cyclo-EDL retains the gene-regulatory activity attributed to linear EDL, it would be the first Khavinson bioregulator with demonstrated oral stability by design, transforming the series from a poorly characterised supplement into a chemically tractable pharmaceutical lead.
Plausibility.50
Novelty.55
Impact.60
Basis · grounding2 papers · 1 computed/note
[1]
paper
Cyclic peptide backbones are completely resistant to proteolytic degradation against trypsin, chymotrypsin, pepsin, and papain under standard conditions.
doi: 10.1021/acs.joc.5b01878
[2]
sequenceEDL is a tripeptide with free N- and C-termini; head-to-tail cyclisation is chemically feasible for three-residue sequences and would remove both exopeptidase attack sites.
[3]
paper
Investigational peptides in the healthspan/longevity space require rigorous validation including stability studies before clinical translation; stability is an acknowledged bottleneck.
doi: 10.3389/fragi.2026.1790247
openupdated 2026-06-05

Does EDL sneak into liver and gut cells by pretending to be a simple amino acid rather than by docking with a special receptor?

If EDL uses a well-known transporter shared with ordinary nutrients, it would be easy to predict when and where it works, and safer to combine with normal food. It might also mean the peptide could reach the brain, opening completely unexpected uses.

The hypothesis
EDL is a substrate-mimetic ligand for the large neutral amino acid transporter LAT1 (SLC7A5), with the Glu-Asp dipeptide head acting as a bioisostere of glutamate and the leucine C-terminus providing the hydrophobic side-chain required for LAT1 recognition, enabling intestinal and blood-brain-barrier uptake that is independent of any receptor-mediated mechanism.
Why it’s plausible
LAT1 transports large neutral amino acids and some dipeptides; it has been shown to accept short peptides containing a leucine or phenylalanine anchor. EDL ends in leucine, the canonical LAT1 substrate, and its N-terminal acidic dimer could satisfy the transporter's substrate recognition pocket similarly to glutamine or asparagine prodrugs. Molecular docking evidence for LAT1 affinity of related short peptides from the Chonluten/EDG peptide family (see pep-10942 readme) provides indirect support.
Why it matters
LAT1-mediated transport would give EDL access to the brain across the blood-brain barrier, which is currently not part of any published hypothesis for this peptide. It would also explain rapid absorption from oral administration without the need for a dedicated receptor.
Plausibility.45
Novelty.60
Impact.55
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceC-terminal leucine in EDL is the primary hydrophobic anchor recognised by LAT1; Glu-Asp head provides a charged N-terminus consistent with dipeptide transporter substrates.
[2]
noteOvagen is proposed to act on liver and GI mucosa, both tissues rich in LAT1 expression, consistent with transporter-mediated localisation.
[3]
paper
Rectal and mucosal administration routes bypass gastric degradation; LAT1-mediated uptake at intestinal mucosal surfaces would be consistent with the oral delivery format of these peptides.
doi: 10.1039/d5ra03731j
details expand to inspect
3-letter notation
Glu-Asp-Leu-Ala
citationbibtex
peptidemodel (2026). Ovagen: synthetic anti-aging peptide for ovarian and liver health (pep-10943, v1). PeptideModel. https://peptidemodel.com/card/pep-10943
@peptide{pep10943,
  sequence = {EDLA},
  target   = {},
  author   = {peptidemodel},
  year     = {2026},
  status   = {designed}
}
clinical trials 0 trials · checked 2026-05-09
0
no registered clinical trials as of 2026-05-09; we'll re-check periodically
references 1 papers
discussion no comments
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