Other compounds

Vilon

Updated · 32 sources · Editorial policy

Vilon is the trade name for a synthetic dipeptide, a chain of just two amino acids: lysine and glutamic acid. In the scientific literature it appears as Lys-Glu or KE. It comes from Vladimir Khavinson’s group at the St. Petersburg Institute of Bioregulation and Gerontology in Russia, which describes it as an immune-system “bioregulator” and a “thymomimetic” (a substance meant to mimic thymus hormones). Online it is marketed for immunity and “anti-aging.”

The single most important fact: no randomized, placebo-controlled trial of vilon has been published in the indexed literature, and nearly every study comes from one research group and its collaborators. The evidence consists of cell-culture and rodent experiments plus a few small Russian clinical reports without described controls. One of the group’s own mouse studies found that vilon increased breast cancer in a cancer-prone strain. Vilon is not an FDA-approved drug.

This page summarizes what the published laboratory, animal and human reports show. It is for education only and is not medical advice.

Property Detail
Class Synthetic dipeptide (Lys-Glu); one of the Khavinson “peptide bioregulators”
Other names KE, KE peptide, Lys-Glu, L-lysyl-L-glutamic acid
Formula and weight C₁₁H₂₁N₃O₅, 275.30 g/mol (PubChem)
CAS number 45234-02-4 (PubChem synonym list)
Origin Described by its developers as a newly synthesized immunomodulatory dipeptide; later called an active component of the calf thymus extract thymalin
Human data A few small Russian reports in type 1 diabetes and elderly cancer patients; no randomized, placebo-controlled trial found
Studied doses Rodent studies only report doses: 0.1–1 µg per mouse by injection under the skin, 5 days a month; 10 µg/kg and 1 mg/kg in mice; 50 µg per rat
Half-life Unknown. We found no published pharmacokinetic study in humans or animals
US status Not an FDA-approved drug; no product found in FDA’s drug approval or NDC databases
WADA Not named on the 2026 list; class S0 covers substances with no government approval for human therapeutic use

What it is

Vilon is the dipeptide L-lysyl-L-glutamic acid. PubChem lists “Vilon,” “Peptide vilon” and “KE dipeptide” as synonyms of the same compound (PubChem). With only two amino acids, it is one of the smallest molecules the group promotes.

The developers’ accounts of its origin differ. A 1997 review by Morozov and Khavinson says thymogen (Glu-Trp) was isolated from the calf thymus extract thymalin, while vilon was “a novel immunomodulatory dipeptide” that was synthesized (Morozov and Khavinson, Int J Immunopharmacol 1997). A 2023 paper from the same institute calls KE and EW (Glu-Trp) the “active substances” of thymalin (Linkova et al., Int J Mol Sci 2023). That paper relied on computer modeling and cell culture, and does not report measuring KE in the extract.

Vilon belongs to a family of short peptides the group promotes as tissue-specific bioregulators. Related pages in the library:

  • Thymalin, the calf thymus extract that vilon is linked to.
  • Thymagen (thymogen, Glu-Trp), the other thymus dipeptide from the same group.
  • Epitalon (Ala-Glu-Asp-Gly), the pineal tetrapeptide that was often tested side by side with vilon.
  • Cartalax (Ala-Glu-Asp) and pinealon (Glu-Asp-Arg), tripeptides promoted for cartilage and brain.

Each is a different molecule with its own, separate research.

How it works in the body

Nobody has shown how vilon acts in people. The group proposes that short peptides enter cells, reach the nucleus and bind DNA, switching genes on or off. The evidence offered for vilon includes:

  • Computer docking. Models predicted that Lys-Glu binds short DNA sequences in the promoter regions (the “on switches”) of genes for the immune signals CD5 and IL-2 and other proteins (Khavinson et al., Bull Exp Biol Med 2013), and of the aging-related genes SIRT1, PARP1 and PARP2 (Khavinson et al., Adv Gerontol 2023).
  • Peptide versus its parts. In rat spleen tissue culture, Lys-Glu stimulated cell growth, while a plain mixture of lysine and glutamic acid inhibited it. Docking predicted that the intact peptide binds DNA more strongly than either amino acid (Khavinson et al., Bull Exp Biol Med 2015).
  • Ultra-low doses. A 2003 paper reported a second peak of activity on thymus cells at 10⁻¹⁷–10⁻¹⁵ mol/L. The authors proposed that at such concentrations the signal is carried by the surrounding water, without the peptide binding any receptor (Grigor’ev et al., Radiats Biol Radioecol 2003). This idea falls outside established pharmacology and has not been tested independently.

In a 2016 paper the group itself wrote that the molecular mechanism by which short peptides regulate genes “remains unclear” (Khavinson et al., Bull Exp Biol Med 2016). Docking models predict binding; they do not show that it happens inside living cells.

Pharmacokinetics

We found no published study measuring vilon’s absorption, distribution, half-life or excretion, in people or in animals. The only work on how it might enter cells is a computer modeling study suggesting that KE and other short peptides could fit the binding sites of the LAT1, LAT2 and PEPT1 transporters (Khavinson et al., Biomolecules 2023). Whether intact vilon survives digestion after oral use, or how long it lasts in blood after injection, has not been reported. Half-life figures quoted online are not based on published measurements.

Regulatory status

  • Not an approved drug in the US. Searches of FDA’s drug approvals database (Drugs@FDA) and National Drug Code directory via openFDA returned no product containing vilon. We found no FDA or EMA approval.
  • Compounding. Vilon was not named on FDA’s page of bulk substances that may present significant safety risks when we checked; that page does name the related peptide epitalon (FDA, 2026). Absence from that page does not mean vilon has been reviewed or found safe.
  • Sport. Vilon is not named on the 2026 WADA Prohibited List. Class S0 bans, at all times, any pharmacological substance “with no current approval by any governmental regulatory health authority for human therapeutic use” (WADA 2026 Prohibited List). We found no WADA ruling specific to vilon.

What the research shows

Almost every study below has Khavinson or staff of his St. Petersburg institute as authors. The few papers from outside Russia, by groups in Georgia and Italy, also list Khavinson as a co-author (Lezhava et al., Biogerontology 2004; Avolio et al., Int J Mol Sci 2022). We found no independent replication. Many papers are short Russian-language articles for which only an abstract is available.

Human evidence

We found no randomized, placebo-controlled trial of vilon. The human reports we found are summarized below. None of the abstracts gives the number of patients, the dose, or describes randomization or blinding.

Study Who Reported result
Kuznik et al., Adv Gerontol 2006 Patients of different ages with unstable type 1 diabetes Vilon added to standard treatment reduced or abolished signs of chronic disseminated intravascular coagulation (widespread abnormal clotting activity); the effect was weaker in elderly patients with severe disease
Kuznik et al., Adv Gerontol 2007 Elderly patients with type 1 diabetes Higher levels of the natural anticoagulants antithrombin III and protein C; “in most cases” a lower insulin dose was needed; shifts in several immune cell counts
Ias’kevich et al., Adv Gerontol 2005 Elderly patients with stage III rectal and colon cancer Described as “pioneer experience” with “preliminary results”; the authors recommend vilon to improve 2-year survival, but the abstract gives no survival data

A 2013 Russian review by Khavinson and colleagues summarizes the group’s clinical experience with vilon and other peptide bioregulators as geroprotectors (Khavinson et al., Adv Gerontol 2013). The abstract gives no trial designs, patient numbers or outcomes for vilon.

In white blood cells taken from people aged 75–88 and grown in culture, vilon “unrolled” tightly packed chromatin (the DNA-protein complex in chromosomes) and reactivated ribosomal genes (Lezhava et al., Biogerontology 2004). This is a laboratory finding in donated cells, not a treatment study.

Immune and other cells in culture

Study Cells Reported finding
Khavinson et al., Bull Exp Biol Med 2002 Mouse thymus cells (thymocytes) Vilon had the strongest effect of three peptides in boosting thymocyte growth alongside a mitogen; epitalon was weaker and cortagen had none
Avolio et al., Int J Mol Sci 2022 Human THP-1 monocyte cell line (a leukemia-derived line) Vilon and four other Khavinson peptides lowered TNF and IL-6 release after bacterial endotoxin and reduced cell adhesion to activated blood-vessel cells
Linkova et al., Int J Mol Sci 2023 Human blood immune cells from four donors Thymalin, KE and EW lowered IL-1β, IL-6 and TNF-α after endotoxin by 1.4–6.0-fold
Khavinson et al., Adv Gerontol 2023 Human mesenchymal stem cells during replicative aging KE raised SIRT1 gene expression 6-fold and protein 8.2-fold in “young” cells; lowered PARP1 and PARP2 in aging cells
Ashapkin et al., Mol Biol Rep 2020 Human fetal bone-marrow stem cells in two aging models KE, AED and KED raised IGF1 gene expression 3.5–5.6-fold and raised NF-κB gene expression; KE doubled FOXO1 expression in one model only
Fridman et al., Bull Exp Biol Med 2020 Human skin fibroblasts during replicative aging KE lowered IL-1, NF-κB and TGF-β and raised sirtuin-6
Ivko et al., Adv Gerontol 2020 Aging human thymus cells KE raised mitochondrial staining 1.5-fold and lowered the ribosomal protein L7A by 15%

Not every result was favorable. In a 2008 Russian study, vilon and three related peptides showed no direct antioxidant activity and raised the resting level of reactive oxygen species inside nerve cells, while lowering the share of dead cells (Kozina et al., Adv Gerontol 2008). All of these results come from cells in a dish, mostly measured by staining and microscopy, and none tested whether the changes translate into better immune function in a living person.

Lifespan in mice

The group’s headline claim is that vilon extends lifespan. The two reports do not fully agree:

Study Design Reported result
Khavinson et al., Bull Exp Biol Med 2000 Female CBA mice given vilon under the skin from the 6th month of life Vilon “prolonged the lifespan,” increased activity and endurance and prevented spontaneous tumors; no figures in the abstract
Anisimov et al., Mech Ageing Dev 2001 Female CBA mice, 0.1 µg per mouse under the skin for 5 days each month from 6 months of age until death, vs saline or epitalon Lys-Glu increased physical activity and lowered spontaneous lung adenomas; the abstract reports a significant survival gain (mean +5.3%) only for epitalon

Cancer studies in rodents

Vilon’s effects on tumors varied by model, and one study found harm.

Model Main reported result
HER-2/neu transgenic mice, which develop breast cancer spontaneously; 1 µg per mouse under the skin for 5 days each month (Anisimov et al., Int J Cancer 2002) Vilon increased breast cancer incidence, shortened the time until tumors appeared and raised the total number of tumors compared with saline (all statistically significant). Epitalon reduced tumor number and size
Same model, Russian report (Alimova et al., Vopr Onkol 2002) Two or more tumors per mouse in 95% on vilon vs 75% on saline and 56% on epitalon; lung metastases 2.6 times more frequent with vilon than with epitalon
Rats given a bladder carcinogen (Pliss et al., Bull Exp Biol Med 2001) Bladder tumors in 56% on vilon vs 75.5% of controls
Mice given the colon carcinogen dimethylhydrazine; 10 µg/kg (Pliss et al., Vopr Onkol 2005) Tumors in 14.3% of surviving mice on vilon vs 60% of controls
Mice with transplanted Lewis lung carcinoma (Barykina et al., Adv Gerontol 2003) Vilon at 1 mg/kg increased survival, but given at the same time as the chemotherapy drug cyclophosphamide it decreased survival

Other animal studies

Model Main reported result
Rats after whole-body gamma irradiation (6 Gy) (Khavinson et al., Bull Exp Biol Med 2001) Vilon stimulated thymus cell growth and intestinal stem cell activity, read as faster recovery of radiation-sensitive organs
Old male rats with one testis removed, a model of age-related decline in sexual function; 50 µg per rat (Kudriavtseva et al., Adv Gerontol 2006) Vilon “activates sexual function”; changes in LH, prolactin and ACTH, with a notable fall in prolactin
Rats aged 3 and 11 months given vilon by mouth (Khavinson et al., Bull Exp Biol Med 2001) Changed activity of several digestive enzymes, most in the older rats

Group sizes, and often doses and routes, are missing from these abstracts. The rodent doses cannot be translated into human doses, and none of these studies was designed to test safety.

Side effects and risks

No human safety data

No published study has systematically assessed vilon’s safety in people. There are no reported toxicology studies (acute, repeat-dose, reproductive or genotoxicity), no dose-response data, and no drug interaction data. Its effects in pregnancy, breastfeeding, children and people with cancer, autoimmune disease, or kidney or liver disease are unknown. The 2000 mouse study states that long-term vilon “caused no unfavourable effects” (Khavinson et al., Bull Exp Biol Med 2000), but that is a single animal study, not human safety evidence.

Cancer signal

The clearest warning comes from the developers’ own work. In HER-2/neu mice, vilon raised breast cancer incidence and tumor number and shortened time to tumor onset (Anisimov et al., Int J Cancer 2002). In stem cell cultures it raised expression of IGF1, a growth-promoting gene, and NF-κB, a central switch for inflammation (Ashapkin et al., Mol Biol Rep 2020). Other rodent studies reported fewer tumors, so the direction of effect depends on the model. Whether vilon affects cancer risk in people has never been studied.

Interaction with chemotherapy

In mice with lung tumors, vilon given at the same time as cyclophosphamide shortened survival, and the authors concluded the two should not be given together (Barykina et al., Adv Gerontol 2003). No human interaction data exist.

Product quality

Products sold online as vilon are not regulated drugs in the US. Their identity, purity, dose per capsule or vial, and (for injectable forms) sterility are not independently verified. Injected peptides with impurities or aggregates can trigger immune reactions, a concern FDA has raised for similar research peptides such as epitalon (FDA, 2026).

Key takeaways

  • A two-amino-acid peptide. Vilon is the trade name for Lys-Glu (KE), developed by Khavinson’s group in St. Petersburg as a thymus “bioregulator” and linked by the group to the calf thymus extract thymalin.
  • Not an approved drug. We found no FDA or EMA approval, and WADA’s S0 class bans substances without any government approval for human therapy.
  • No controlled human trials. Human data are a few small Russian reports in diabetes and elderly cancer patients, without stated patient numbers, doses, randomization or placebo.
  • Evidence is from one research network. Nearly every study involves the same institute or co-authors from it, often as abstract-only Russian papers.
  • Mixed animal results, including harm. Vilon was reported to reduce some induced tumors in rodents, but it increased breast cancer in a cancer-prone mouse strain and shortened survival when combined with chemotherapy.
  • Pharmacokinetics and safety are unknown. No half-life, absorption or toxicology data have been published.

Sources

  1. National Center for Biotechnology Information. PubChem compound summary for CID 7010502, Lys-Glu (vilon). PubChem.
  2. Morozov VG, Khavinson VK. Natural and synthetic thymic peptides as therapeutics for immune dysfunction. Int J Immunopharmacol. 1997;19(9-10):501–505. PubMed.
  3. Linkova N, Khavinson V, Diatlova A, et al. The Influence of KE and EW Dipeptides in the Composition of the Thymalin Drug on Gene Expression and Protein Synthesis Involved in the Pathogenesis of COVID-19. Int J Mol Sci. 2023;24(17):13377. PubMed.
  4. Khavinson VKh, Tarnovskaya SI, Linkova NS, et al. Short cell-penetrating peptides: a model of interactions with gene promoter sites. Bull Exp Biol Med. 2013;154(3):403–410. PubMed.
  5. Khavinson VK, Linkova NS, Ashapkin VV, et al. KE peptide regulates SIRT1, PARP1, PARP2 gene expression and protein synthesis in human mesenchymal stem cells aging. In Russian. Adv Gerontol. 2023;36(3):302–312. PubMed.
  6. Khavinson VKh, Tarnovskaya SI, Lin’kova NS, et al. Role of peptide bond in the realization of biological activity of short peptides. Bull Exp Biol Med. 2015;158(4):551–554. PubMed.
  7. Grigor’ev EI, Khavinson VKh, Malinin VV, et al. The study of the role of the water medium in the mechanism of action of peptides in low and ultra low doses. In Russian. Radiats Biol Radioecol. 2003;43(3):358–362. PubMed.
  8. Khavinson VK, Lin’kova NS, Tarnovskaya SI. Short Peptides Regulate Gene Expression. Bull Exp Biol Med. 2016;162(2):288–292. PubMed.
  9. Khavinson VK, Linkova NS, Rudskoy AI, et al. Feasibility of Transport of 26 Biologically Active Ultrashort Peptides via LAT and PEPT Family Transporters. Biomolecules. 2023;13(3):552. PubMed.
  10. Food and Drug Administration. Certain bulk drug substances for use in compounding that may present significant safety risks. Content current as of April 22, 2026. FDA.
  11. World Anti-Doping Agency. The 2026 Prohibited List. In effect January 1, 2026. WADA.
  12. Lezhava T, Khavison V, Monaselidze J, et al. Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people. Biogerontology. 2004;5(2):73–79. PubMed.
  13. Avolio F, Martinotti S, Khavinson VK, et al. Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line. Int J Mol Sci. 2022;23(7):3607. PubMed.
  14. Kuznik BI, Kolesnichenko LR, Kliuchereva NN, et al. Effect of thymomimetic vilon on blood coagulation system and fibrinolisis in diabetes mellitus type 1 patients of different age. In Russian. Adv Gerontol. 2006;19:107–115. PubMed.
  15. Kuznik BI, Isakova NV, Kliuchereva NN, et al. Effect of vilon on the immunity status and coagulation hemostasis in patients of different age with diabetes mellitus. In Russian. Adv Gerontol. 2007;20(2):106–115. PubMed.
  16. Ias’kevich LS, Krutilina NI, Kostetskaia TV, et al. Application of peptide bioregulator in complex treatment of elderly cancer patients. In Russian. Adv Gerontol. 2005;16:97–100. PubMed.
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  18. Khavinson VKh, Rybakina EG, Malinin VV, et al. Effects of short peptides on thymocyte blast transformation and signal transduction along the sphingomyelin pathway. Bull Exp Biol Med. 2002;133(5):497–499. PubMed.
  19. Ashapkin V, Khavinson V, Shilovsky G, et al. Gene expression in human mesenchymal stem cell aging cultures: modulation by short peptides. Mol Biol Rep. 2020;47(6):4323–4329. PubMed.
  20. Fridman NV, Linkova NS, Kozhevnikova EO, et al. Comparison of the Effects of KE and AED Peptides on Functional Activity of Human Skin Fibroblasts during Their Replicative Aging. Bull Exp Biol Med. 2020;170(1):154–157. PubMed.
  21. Ivko OM, Drobintseva AO, Leont’eva DO, et al. The influence of AEDG and KE peptides on mitochondries stain and L7A ribosomes protein expression during human pineal gland and thymus cell senescence in vitro. In Russian. Adv Gerontol. 2020;33(4):741–747. PubMed.
  22. Kozina LS, Arutiunian AV, Stvolinskiĭ SL, et al. Biological activity of regulatory peptides in model experiments in vitro. In Russian. Adv Gerontol. 2008;21(1):68–73. PubMed.
  23. Khavinson VK, Anisimov VN, Zavarzina NY, et al. Effect of vilon on biological age and lifespan in mice. Bull Exp Biol Med. 2000;130(7):687–690. PubMed.
  24. Anisimov VN, Khavinson VK, Mikhalski AI, et al. Effect of synthetic thymic and pineal peptides on biomarkers of ageing, survival and spontaneous tumour incidence in female CBA mice. Mech Ageing Dev. 2001;122(1):41–68. PubMed.
  25. Anisimov VN, Khavinson VK, Provinciali M, et al. Inhibitory effect of the peptide epitalon on the development of spontaneous mammary tumors in HER-2/neu transgenic mice. Int J Cancer. 2002;101(1):7–10. PubMed.
  26. Alimova IN, Bashurin DA, Popovich IG, et al. Effect of Epitalon and Vilon treatment on mammary carcinogenesis in transgenic erbB-2/NEU mice. In Russian. Vopr Onkol. 2002;48(1):57–60. PubMed.
  27. Pliss GB, Mel’nikov AS, Malinin VV, et al. Inhibitory effect of peptide vilon on the development of induced rat urinary bladder tumors in rats. Bull Exp Biol Med. 2001;131(6):558–560. PubMed.
  28. Pliss GB, Mel’nikov AS, Malinin VV, et al. The effect of vilon (Lys-Glu) on 1.2-dimethylhydrazine-induced neoplasia. In Russian. Vopr Onkol. 2005;51(4):466–469. PubMed.
  29. Barykina OP, Iuzhakov VV, Chalisova NI, et al. Combined effect of vilon and cyclophosphane on tumor transplants and lymphoid tissue explants in mice and rats of various age. In Russian. Adv Gerontol. 2003;12:128–131. PubMed.
  30. Khavinson VK, Yuzhakov VV, Kvetnoi IM, et al. Immunohistochemical and morphometric analysis of effects of vilon and epithalon on functional morphology of radiosensitive organs. Bull Exp Biol Med. 2001;131(3):285–292. PubMed.
  31. Kudriavtseva TA, Zaĭchenko IN, Efremov OM, et al. Effect of vilon on neuroendocrine status and sexual function of old male rats. In Russian. Adv Gerontol. 2006;19:97–101. PubMed.
  32. Khavinson VK, Timofeeva NM, Malinin VV, et al. Effect of the dipeptide vilon on activity of digestive enzyme in rats of various ages. Bull Exp Biol Med. 2001;131(6):583–585. PubMed.