Quick Answer
Ovagen is a synthetic tripeptide, Glu-Asp-Leu (EDL), from Vladimir Khavinson's bioregulator programme. By origin it is a liver peptide: the group reports it from a calf liver extract and patented it for liver tissue regeneration. Most of its indexed studies, however, test it in kidney cells and rat models of kidney injury. All of the work comes from one research network, and we found no peer-reviewed human data.
Ovagen's name gives no clue to its tissue, and the sources point to two. This article sets out what the primary literature says about its sequence and origin, why its research record leads to the kidney as much as the liver, and how much weight the evidence can bear.
Sequence and identity
Ovagen is glutamyl-aspartyl-leucine: Glu-Asp-Leu, or EDL in one-letter code. The Russian patent that introduced it, published in 2007, claims H-Glu-Asp-Leu-OH [1], and the group's 2021 review lists EDL under the name Ovagen [2]. Its molecular formula is C15H25N3O8, with a molecular weight of about 375.4. Structurally it is Bronchogen (Ala-Glu-Asp-Leu) without the first alanine. It should not be confused with Livagen (Lys-Glu-Asp-Ala), the other bioregulator assigned to the liver.
Origin and tissue association
By origin, Ovagen is a liver peptide. Khavinson's 2020 review states that EDL was detected by chromatography with mass spectrometry in Ventvil [3], a peptide complex extracted from calf liver [4], and the patent presents it as a peptide that stimulates regeneration of liver tissue [1]. That is why it is usually listed as a liver bioregulator.
The indexed research record points elsewhere. All six PubMed-indexed experimental papers on EDL that we found concern the kidney [5 to 10]. The group's own 2021 review summarises Ovagen's activity as regulation of renal cell function, hepatoprotection and DNA binding, and supports it with a kidney cell study [2, 5]. Despite the name, we found no primary source that links it to the ovary.
The proposed mechanism
The model is the family's usual one: a short peptide that enters the nucleus and adjusts gene activity. For EDL the direct support is computational. Docking studies from the group have proposed binding sites in DNA: an AT-rich site in the minor groove in one paper [6] and a CTCC motif, shared with Bronchogen, in another [11]. In young and aged renal cell cultures EDL was reported to increase proliferation, lower the senescence markers p16, p21 and p53, and raise SIRT6 [6], and in primary kidney cell cultures its main target among the markers measured was the matrix enzyme MMP-14 [5]. These are associations in culture. The step from DNA binding to those changes in gene activity has not been demonstrated.
What the studies show
Liver
The liver evidence is thin. The patent describes rat liver explants, rats after removal of two thirds of the liver, and rats with carbon tetrachloride-induced cirrhosis [1]. The 2020 review summarises the findings as more hepatocyte division and liver regrowth after partial liver removal, and faster recovery of liver function after toxic injury [3]. The patent also describes an observation in 34 people with chronic hepatitis. We found none of this in a peer-reviewed journal. Separately, a 2023 organotypic culture study from the same network found that EDL increased the growth of liver explants from young and old rats [12].
Kidney
- Cells and explants. In primary kidney cell cultures and in young and aged renal cell cultures, EDL (coded T-35 in some papers) changed markers of cell renewal and senescence [5, 6]. In organotypic kidney explants from young and old rats it stimulated proliferation and reduced apoptosis, though less than a peptide complex extracted from calf kidney [7].
- Rats. A group at Bukovinian State Medical University in Ukraine, publishing with Khavinson's institute, tested EDL in rats with kidney injury caused by the chemotherapy drug cisplatin [8], by the antibiotic gentamicin or by interrupted blood supply [9], and in old rats [10]. They report better preserved urine output and filtration, less protein in the urine and improved antioxidant status in kidney tissue, and saw no sign of kidney toxicity in the old rats.
A note on the name
Searching PubMed for "Ovagen" returns about 30 papers, none of them about this peptide. Many concern an unrelated commercial follicle-stimulating hormone preparation of the same name, used in livestock reproduction research [13]. Anyone surveying the literature should search by sequence as well as by name.
How strong is the evidence?
- Two tissues, one source. The kidney evidence is six papers, all with Khavinson's institute among the authors; the Ukrainian rat studies add a second laboratory but not an independent one. The liver evidence rests mainly on a patent and one explant study.
- Animal and cell models only. We found no peer-reviewed human data.
- Language. The patent, the 2020 review and four of the studies cited here are in Russian.
- No replication. None of the findings has been repeated by an unconnected group.
The fair summary is a peptide with a consistent preclinical story in rat kidney models and a thinner, largely patent-based one in liver, both awaiting independent confirmation.
Where Ovagen fits
Ovagen is one of a family of short peptides that share an origin story, a proposed DNA-binding mechanism and the same evidence gaps. For that wider context, including how the tissue labels were assigned and why they are best read as a record of origin rather than proof of action, see our guide to Khavinson bioregulator peptides.
References
- Khavinson VKh, et al. 2007. "Peptide stimulating regeneration of liver tissue, pharmaceutical composition based on it and method of its use" (in Russian). Russian patent RU 2297239. Google Patents
- Khavinson VK, et al. 2021. "Peptide Regulation of Gene Expression: A Systematic Review." Molecules 26(22):7053. PMID 34834147
- Khavinson VKh. 2020. "Peptide medicines: past, present, future" (in Russian). Klinicheskaya Meditsina 98(3):165-177. doi:10.30629/0023-2149-2020-98-3-165-177
- Ryzhak AP, et al. 2015. "Polypeptides influence on tissue cell cultures regeneration of various age rats" (in Russian). Advances in Gerontology 28(1):97-103. PMID 26390619
- Khavinson VKh, et al. 2014. "Peptides regulate expression of signaling molecules in kidney cell cultures during in vitro aging." Bulletin of Experimental Biology and Medicine 157(2):261-264. PMID 24958378
- Khavinson VKh, et al. 2014. "Tripeptides slow down aging process in renal cell culture" (in Russian). Advances in Gerontology 27(4):651-656. PMID 25946838
- Chalisova NI, et al. 2015. "Peptide Regulation of Cells Renewal Processes in Kidney Tissue Cultures from Young and Old Animals." Bulletin of Experimental Biology and Medicine 159(1):124-127. PMID 26033601
- Zamorskii II, et al. 2015. "Peptides Restore Functional State of the Kidneys During Cisplatin-Induced Acute Renal Failure." Bulletin of Experimental Biology and Medicine 159(6):736-739. PMID 26515176
- Zamorskii II, et al. 2017. "Nephroprotective Effect of EDL Peptide at Acute Injury of Kidneys of Different Genesis." Bulletin of Experimental Biology and Medicine 163(3):389-393. PMID 28744634
- Zamorskii II, et al. 2018. "The influence of peptides on the morphofunctional state of old rats kidneys" (in Russian). Advances in Gerontology 31(4):498-504. PMID 30607912
- Khavinson VK, et al. 2016. "Short Peptides Regulate Gene Expression." Bulletin of Experimental Biology and Medicine 162(2):288-292. PMID 27909961
- Chalisova NI, et al. 2023. "The stimulating effect of short peptides on cellular proliferation in organotypic tissue culture" (in Russian). Integrative Physiology 4(2):225-234. doi:10.33910/2687-1270-2023-4-2-225-234
- Gonzalez-Bulnes A, et al. 2000. "Effects of FSH commercial preparation and follicular status on follicular growth and superovulatory response in Spanish Merino ewes." Theriogenology 54(7):1055-1064. PMID 11131324