Ovagen Research, Specifications & Scientific Information

Ovagen is the synthetic tripeptide Glu-Asp-Leu from the Khavinson bioregulator series, published in the primary literature only as the EDL peptide. Its entire identified primary record is two rat studies of acute kidney damage from one author group. No clinical study of it has been identified and it is not approved by the FDA for any indication.

Category: Peptide bioregulators

Introduction

Ovagen is a three-residue peptide, Glu-Asp-Leu, and its entire identified primary literature is two papers — both in rats, both about the kidney, both from one author group, published two years apart in the same journal [2, 1].

Two verifiable primary sources is the floor this library publishes at. This page is short because that is what the evidence supports, and padding it would mean writing sentences nothing stands behind.

Two naming problems make the record look even thinner than it is, and both have to be dealt with before anything else. The trade name belongs to something else. Ovagen is a long-established veterinary follicle-stimulating hormone preparation used to induce superovulation in sheep, goats and cattle; a literature search on the bare name returns that product almost to the exclusion of this one. The sequence is a substring. Glu-Asp-Leu sits inside Ala-Glu-Asp-Leu, which is Bronchogen, so a text search for the tripeptide returns tetrapeptide papers that are not about this compound. The primary studies here call it only the EDL peptide, and that is the label that finds them.

The family's shared limitations apply in full: one originating research programme, small studies, no independent replication, no clinical report of any design, and — in this case — no cell-culture work on the compound at all.

What Is Ovagen?

A synthetic tripeptide with free termini, EDL in single-letter code: L-alpha-glutamyl-L-alpha-aspartyl-L-leucine. PubChem carries it as compound identifier 444128. No CAS registry number and no FDA/NCATS unique ingredient identifier resolve for it.

Its place in the bioregulator series is stated only in the originating group's own review tables, which list Ovagen as EDL and attribute to it both a nephroprotective and a hepatoprotective role [3, 4]. The nephroprotective attribution is referenced in those tables to a published study. The hepatoprotective attribution is referenced to a patent application, not to a study — a distinction that matters, because a patent is a claim of invention examined for novelty rather than a result examined by peers.

The tripeptide has not been approved by the U.S. Food and Drug Administration for any indication. No marketing application for it is on record in the United States, and no study of it appears on ClinicalTrials.gov under its sequence.

Ovagen Specifications

Compound name
Ovagen
Full chemical name
L-alpha-glutamyl-L-alpha-aspartyl-L-leucine
Aliases
Glu-Asp-Leu, EDL, EDL peptide, H-Glu-Asp-Leu-OH
Development code
Not publicly characterised
CAS number
Not publicly characterised
PubChem CID
444128
UNII
Not publicly characterised
Compound type
Synthetic tripeptide
Peptide family
Khavinson peptide bioregulators — short synthetic peptides designed from the amino acid composition of tissue-specific polypeptide extracts
Amino acid sequence
EDL
Sequence length
3 residues
Molecular formula
C15H25N3O8
Molecular weight
375.37 g/mol
Primary target
Not publicly characterised
Secondary targets
Not publicly characterised
Receptor family
Not publicly characterised
Agonist / antagonist status
Not publicly characterised

PubChem carries the free tripeptide as compound identifier 444128, formula C15H25N3O8 and an average mass of 375.37 g/mol. No CAS registry number and no FDA/NCATS unique ingredient identifier resolve for it, so both fields are published as unknown rather than estimated. The trade name is a collision hazard: Ovagen is also a long-established veterinary follicle-stimulating hormone preparation used for superovulation in sheep, goats and cattle, and a literature search on the bare name returns that product almost exclusively. The identification of this trade name with the sequence Glu-Asp-Leu comes from the originating group's own review tables; the primary studies refer to the compound only as the EDL peptide. Note also that Glu-Asp-Leu is a substring of Ala-Glu-Asp-Leu, the sequence of Bronchogen, so a text search for the tripeptide returns tetrapeptide papers that are not about this compound.

Values that a public register does not carry are shown as not publicly characterised rather than estimated. Identifiers are reference values; the certificate of analysis supplied with a laboratory order is the record for a given lot.

How Does Ovagen Work?

Not established, and for this compound the answer is shorter than for any other page in this batch because less has been tried.

No receptor has been identified and none is proposed. The specification table above shows primary target, receptor family and agonist status as not publicly characterised, and those entries are accurate rather than unfinished.

No binding study of this tripeptide exists. The originating group's general hypothesis for the series is that these peptides act by binding DNA or histones directly, and that hypothesis has been tested — with fluorescence quenching, calorimetry and docking — for Epitalon, Pinealon, Bronchogen, Testagen and others. No such experiment on Glu-Asp-Leu has been located. Whatever support the series' mechanistic hypothesis has, none of it is specific to this compound.

What the two primary papers measure is physiology. Prevented oliguria and retention azotaemia; reduced proteinuria and sodium excretion; preserved antioxidant enzyme activity; suppressed lipid peroxidation; normalised the bioenergetic status of kidney cells [1]. Those are organ-level and tissue-level outcomes. Every one of them is several steps downstream of whatever the molecule did first, and the papers do not attempt the intervening steps.

No pharmacokinetic dataset exists, and the indexed abstracts do not state route or amount administered.

Preclinical Research on Ovagen

Animal research

Two models of acute kidney injury, 2017

The only study located whose subject is this tripeptide alone. Two mechanistically different insults were used: gentamicin-induced nephropathy, a toxic tubular injury, and ischaemia–reperfusion, a vascular one [1].

Reported across both models: prevention of oliguria and of retention azotaemia; decreased proteinuria and sodium excretion; prevention of a critical decrease in the activity of antioxidant enzymes; suppression of lipid peroxidation; and normalisation of energy supply to kidney cells.

Testing one compound against two different mechanisms of injury is a genuine design strength — a result that holds across a toxic and an ischaemic insult is less likely to be an artefact of one model. Against that: the indexed abstract states no group sizes, no route, no amount, no randomisation, no blinding and no statistical tests, and the authors' own conclusion is framed as confirming the prospects for further study rather than as establishing an effect.

Cisplatin-induced acute renal failure, 2015

Rats with cisplatin-induced acute renal failure received a kidney polypeptide complex or one of three short peptides — this one, AED or AEDG [2].

The three separated. AED decreased protein excretion and urinary electrolyte concentration, and nothing more. The kidney complex, this tripeptide and AEDG normalised a much wider set: diuresis, urinary creatinine concentration and excretion, glomerular filtration rate, absolute sodium resorption, urinary protein concentration and excretion, and urinary sodium and potassium. The authors single out this peptide as producing the potent nephroprotective effect [2].

Two points follow. A three-way comparison in which the compounds behave differently is more informative than a single-arm result, and it is consistent with the series' premise that sequence assigns tissue. And the comparison against the parent polypeptide complex is the one the series' founding claim actually needs — though the paper reports no potency difference between the complex and the peptides, only that both acted.

Findings in this section were obtained in rats. Nothing in them establishes anything about humans.

What Is Ovagen Being Researched For?

One thing, twice.

  • Acute kidney damage in rats — toxic, ischaemic and chemotherapeutic models, with renal function, antioxidant and cellular-metabolism endpoints [2, 1].

No other research area has an identifiable primary literature for this compound. The hepatoprotective role listed for it in the originating group's review tables traces to a patent application rather than to a published study [3], and is therefore not described on this page as a research area.

None of that is research into, or evidence about, research-grade material supplied for laboratory use.

Current Research Status

Regulatory status (United States)
Not approved. The tripeptide Glu-Asp-Leu has not been approved by the U.S. Food and Drug Administration for any indication, and no marketing application for it is on record in the United States. Regulatory and trial-register searches on the trade name return an unrelated veterinary gonadotrophin product.
Investigational status
No study of the tripeptide is registered on ClinicalTrials.gov and no clinical report of it has been identified. The identified primary record consists of two rat studies of acute kidney damage from the same author group, published in 2015 and 2017. The hepatoprotective role attributed to the compound in the originating group's review tables is referenced there to a patent application rather than to a study.
Highest research phase reached
No clinical study identified. The evidence is two rat studies of experimentally induced acute kidney damage.
Approved uses
None
Approval is compound-specific
Yes

Status as of . This block is rendered from maintained fields, not from prose, so it cannot go stale in one place and stay current in another.

Chemical & Molecular Characteristics

Leucine gives this tripeptide the only hydrophobic surface it has. The isobutyl side chain is the largest purely aliphatic group in the standard set. In a molecule of only three residues, two of which are acidic, it is the single feature that is not polar — and it confers real reversed-phase retention, so a purity figure by HPLC is more meaningful here than for the wholly polar tripeptides of this series.

Net charge is acidic. With no basic side chain, the N-terminal amine alone offsets the glutamate side chain, the aspartate side chain and the C-terminal carboxyl. The molecule is net negative at physiological pH.

No aromatic residue, so no absorbance at 280 nm. Quantification has to rely on peptide-bond absorbance near 214 nm, where solvents and buffers also absorb. Leucine, unlike tryptophan or tyrosine, contributes no useful chromophore.

Adjacent acidic residues make isomerisation the identity question. Glutamate followed directly by aspartate is the motif most prone to the alpha/beta and alpha/gamma rearrangements that affect Asp- and Glu-containing peptides, favoured by heat and by acid. The rearranged species have the same molecular formula and the same mass as the intended tripeptide, so a mass spectrum confirming 375.37 daltons is consistent with the intended compound and with several isomers of it. Only a sequencing method separates them.

The substring problem is also an analytical one. Because Glu-Asp-Leu is contained within Ala-Glu-Asp-Leu, a synthesis that fails to remove or to couple the N-terminal residue produces the other compound rather than an obvious failure — and the two differ in mass by 71 daltons, which a mass spectrum does resolve. That is one identity question that mass alone can answer, and it is worth answering.

Two register fields are empty and stay empty. No CAS registry number and no FDA/NCATS unique ingredient identifier resolve for this tripeptide; only the PubChem compound identifier does. They are shown as unknown above rather than filled from a neighbouring substance.

Frequently Asked Questions

What is Ovagen?
A synthetic tripeptide, Glu-Asp-Leu, written EDL. PubChem records it as compound identifier 444128; no CAS registry number and no unique ingredient identifier resolve for it. The identification of the trade name with this sequence comes from the originating group's own review tables [3, 4]; the primary studies of the compound refer to it only as the EDL peptide.
Is this the same Ovagen used in veterinary medicine?
No, and the collision is worth knowing before any search. Ovagen is a long-established veterinary follicle-stimulating hormone preparation used for superovulation in sheep, goats and cattle, and a literature search on the bare name returns that product almost to the exclusion of this one. A follicle-stimulating hormone preparation is a protein hormone product; this is a three-residue synthetic peptide. Nothing connects them but a name.
How does Ovagen work?
Not established. No receptor has been identified and none is proposed. The two primary studies report downstream physiological measurements — prevented oliguria and retention azotaemia, reduced proteinuria and sodium excretion, preserved antioxidant enzyme activity, suppressed lipid peroxidation and normalised the bioenergetic status of kidney cells [1] — rather than any interaction. The originating group's general hypothesis for the series is direct binding to nucleic acids, but no DNA- or histone-binding study of this particular tripeptide has been located.
Is Ovagen FDA approved?
No. The tripeptide has not been approved by the U.S. Food and Drug Administration for any indication, and no marketing application for it is on record in the United States. No study of it is registered on ClinicalTrials.gov. Any regulatory record returned by searching the bare name belongs to the veterinary gonadotrophin product.
Has Ovagen been studied in humans?
No clinical study of the tripeptide has been identified in the indexed literature, and none is registered on ClinicalTrials.gov. No cell-culture study of it has been located either: the entire identified primary record is two rat experiments.
What did the kidney studies report?
The 2017 study used two separate models — gentamicin-induced nephropathy and ischaemia–reperfusion insult — and reported that the peptide prevented oliguria and retention azotaemia, decreased proteinuria and sodium excretion, prevented a critical fall in antioxidant enzyme activity, suppressed lipid peroxidation, and normalised the bioenergetic status of kidney cells [1]. The 2015 study compared a kidney polypeptide complex against three short peptides in cisplatin-induced acute renal failure; this one was named by the authors as producing the potent nephroprotective effect, normalising diuresis, urinary creatinine, glomerular filtration rate and sodium handling [2].
How much published research exists on Ovagen specifically?
Two primary papers, both from the same author group, both in rats, both in the same journal, published in 2015 and 2017 [2, 1]. Beyond those, the compound appears only in the originating group's review tables. The hepatoprotective role attributed to it there is referenced to a patent application rather than to a study [3]. Two papers is the minimum this library will publish a page on, and this page is short because the literature is.
What identifiers are published for Ovagen?
PubChem compound identifier 444128, molecular formula C15H25N3O8, average mass 375.37 g/mol. No CAS registry number and no FDA/NCATS unique ingredient identifier resolve for the substance, so both fields are shown as unknown rather than estimated.

Scientific References

  1. Zamorskii II, Shchudrova TS, Lin'kova NS, et al.. Nephroprotective Effect of EDL Peptide at Acute Injury of Kidneys of Different Genesis Bulletin of experimental biology and medicine; 2017. PMID 28744634 doi:10.1007/s10517-017-3811-1
  2. Zamorskii II, Shchudrova TS, Lin'kova NS, et al.. Peptides Restore Functional State of the Kidneys During Cisplatin-Induced Acute Renal Failure Bulletin of experimental biology and medicine; 2015. PMID 26515176 doi:10.1007/s10517-015-3062-y
  3. Khavinson V, Linkova N, Kozhevnikova E, et al.. Transport of Biologically Active Ultrashort Peptides Using POT and LAT Carriers International journal of molecular sciences; 2022. PMID 35887081 doi:10.3390/ijms23147733
  4. Khavinson VK, Popovich IG, Linkova NS, et al.. Peptide Regulation of Gene Expression: A Systematic Review Molecules (Basel, Switzerland); 2021. PMID 34834147 doi:10.3390/molecules26227053

Every identifier above is resolved against PubMed, Crossref or ClinicalTrials.gov at build time, and the title returned by the register is compared with the title stored here. A page does not publish if a reference fails to resolve.

Research-Use Information