Vilon: what the studies show, status and safety

Summary

Vilon is a synthetic peptide of two amino acids, lysine and glutamic acid, from a St Petersburg institute that calls such molecules bioregulators. The same compound is catalogued as an ordinary human metabolite. No measurement of what happens to it in a body exists in any species. Its developers report that it breaks down faster than the three peptides they compared it against. It is approved as a medicine nowhere, and no trial in people has been registered.

Key findings at a glance

• It is the smallest molecule a peptide can be, and the body already makes it. Two amino acids, one bond, 275.30 g/mol, both building blocks ordinary constituents of food protein. Lys-Glu also has an entry in the Human Metabolome Database, because that pair is released as proteins are broken down ^[1], ^[2].
• Its own developers report that it is the least stable of their peptides. In a 2022 review they write that KE was hydrolysed in solutions and partly in tissues, more than the three peptides tested alongside it. Nothing that happens to it in a body has ever been measured: no half-life, no blood level, no bioavailability, in any species ^[3], ^[4].
• Their own transport calculation misses their own threshold. At the carrier LAT1 Vilon scores −12.31, where a more negative number means a better computed fit. The same paper names −15 as the value a peptide must beat before efficient binding becomes likely ^[3].
• An independent study of 228 dipeptides predicts instability for this one. Neither lysine at the front nor glutamic acid at the end is among the residues that protect a dipeptide from breakdown ^[4].
• In 2003 the developers reported activity at about six thousand molecules per millilitre, explained as signalling without any ligand-receptor complex, mediated by the dynamics of the water ^[5].
• No registered trial exists. Four database queries on 17 September 2026 returned nothing relevant, while a control query returned 782 studies ^[6].
• It is a medicine in no country, Russia included. The institute's own head wrote in 2020 that Vilon had been submitted for registration, 22 years after the patent priority. Its only market entry is a Russian food supplement taken by mouth, and it is banned in sport at all times ^[7], ^[8], ^[9].
• What the page does not say. None of this shows that Vilon does nothing; it shows that the case for a specific signalling effect is weak and unmeasured, which is a different statement ^[3], ^[4].

What it is

Vilon is a dipeptide: lysine joined to glutamic acid by one ordinary peptide bond, and the shortest molecule of the series developed at the St Petersburg Institute of Bioregulation and Gerontology. The group around Vladimir Khavinson calls such compounds peptide bioregulators ^[7], ^[12].

According to that group the pair was detected by mass spectrometry inside Thymalin, a peptide preparation made from calf thymus, and then reproduced synthetically ^[7]. The first English-language description, in 1997, calls it a novel immunomodulatory dipeptide ^[12], and a United States patent was filed in 1998 and granted in 2003 ^[11].

Quick facts

One thing this page can confirm rather than correct: the sequence and the common synonyms are right, with four independent sources giving Lys-Glu, the patent and the database structure record among them ^[1], ^[11].

How it works

Nobody knows, and the proposals are unusually far-reaching for a molecule of two amino acids. Every mechanism below is a hypothesis resting on modelling, cell-free experiments or cell culture, never on measurement in a living body ^[3].

• It is said to bind DNA in gene promoters and so change how certain genes are read. The group proposes that KE recognises the four-letter stretches TCGA, GCAG, GCGG and GGGC ^[13], ^[15].
• That binding is described as running along the minor groove, the shallower of the two spiral channels of DNA, which lacks the hydrogen-bonding pattern that tells the four bases apart. Recognition there is generally considered non-specific ^[14].
• The proposed target is extremely common. A stretch such as TCGA occurs every few hundred base pairs, millions of times across the human genome, so binding it is not a way of selecting a handful of genes ^[13].
• Downstream effects are listed without a route to them. The group's own overview assigns each peptide an organ and an effect category, raised interleukin-2 messenger RNA among them, without a measured step in between ^[46].
• Tissue specificity is argued from origin, not from measurement. The claim that it acts preferentially on the thymus rests on its having been found in a thymus preparation ^[26].

The group's own work contains the awkward part. They report that the effect depends on the peptide bond, because a plain mixture of free lysine and glutamic acid slowed the same cultures down instead of speeding them up ^[14]. Yet they also write that KE is hydrolysed in solution and partly in tissue, and hydrolysis produces exactly that mixture ^[3].

What the studies found

There is a large amount of literature and almost no evidence in the usual sense: around 60 indexed papers from a single network of authors, mostly without case numbers or statistics, each load-bearing claim resting on one unreplicated study ^[34].

Whether it survives long enough to act

Review of the developers' own work This is the finding that carries the page. In a 2022 transport review the group reports that KE was hydrolysed in solutions and partly in tissues, while two other peptides of the series resisted hydrolysis for three to four hours. Of the four, theirs falls apart fastest ^[3].

Independent modelling A study outside this network synthesised 228 dipeptides and measured how well they survive digestion. Protection comes from specific end residues: aspartate, glycine or proline at the front, proline, serine, threonine or aspartate at the end. Vilon carries neither, having lysine at the front and glutamic acid at the end. The same authors conclude that effects of dipeptides in a living body are most likely limited by their very low gut permeability, for which their modelling produced no reliable correlation at all ^[4].

Calculation only The group's proposed way in is the carrier LAT1, and the evidence is a docking score rather than a measurement. Vilon scores −12.31, while the same table states that scores more negative than −15 may indicate a high probability of efficient binding. Their own number for their own peptide falls short of their own mark ^[3].

The passage describing that hydrolysis experiment carries a single reference, and it is a general review of small peptide absorption that does not examine these four peptides at all. The experiment itself could not be found ^[45].

Activity reported at six thousand molecules per millilitre

In vitro In 2003 the developing group, with the institute's director as co-author, reported a two-humped dose-response curve for thymus cells, the second hump sitting between 10⁻¹⁷ and 10⁻¹⁵ moles per litre. At the lower figure a millilitre holds roughly six thousand molecules. The authors did not treat that as a problem: they proposed that a signal forms and reaches the target cell without any ligand-receptor complex, with the water medium taking an active role ^[5].

A signal without a ligand-receptor complex is not compatible with receptor pharmacology, the framework in which statements about how a substance acts on a cell are normally made. This is not a critic's characterisation but what the developers published, and it sets the standard by which their other dose-response claims should be read, including a second paper from the same laboratory reporting effects between 10⁻⁹ and 10⁻¹³ moles per litre ^[30].

Lifespan in mice

Animal data Female CBA mice were given the peptide under the skin from six months of age. The authors report greater physical activity and endurance, a lower body temperature and a longer lifespan, while two measures explicitly did not move: age-related changes in oestrous function, and free-radical processes. No animal numbers, no dose, no survival curves and no p-values appear ^[19]. The widely quoted figure of 20 to 40 per cent longer life comes not from this paper but from a later review by the same authors, where it refers to "some peptide preparations" as a group ^[20].

Chromatin in donated human cells

Cell culture White blood cells from people aged 75 to 88 were cultured with the peptide. The reports describe loosened overall heterochromatin, reactivation of ribosome genes and release of genes from facultative packing, with no measured values and no p-values. This is the best-supported finding on Vilon, because two of the three papers appeared without the institute's director as a co-author, and it has a clear negative half: the pericentromeric heterochromatin of chromosomes 1 and 9 did not loosen, an effect the same group saw with two other peptides ^[17].

Gene expression

Animal data The most-cited mechanistic paper put 15,247 gene clones from mouse heart on a microarray. 300 of them, 1.94 per cent, changed by more than twofold, and Vilon alone accounted for 36. With no correction for multiple testing, that count cannot be separated from noise ^[16].

Cell culture In human stem cells the reported changes are large but bare. IGF1 output rose 3.5- to 5.6-fold with the peptides tested, while KE roughly doubled FOXO1 in one ageing model and did nothing in the other ^[18]. In a second study KE raised SIRT1 gene expression 6-fold and protein output 8.2-fold in young cells, and lowered PARP1 by 2.1- and 5.3-fold and PARP2 by 2.1- and 4.7-fold, with no p-values, spread or replicate counts ^[15].

Organ models in animals

Animal data In rats with scarred livers, 1.7 µg/kg daily for five days raised total protein by 4.7 per cent and cell ploidy by 11.5 per cent over untreated animals. The authors themselves call that a weak stimulating effect, and two of the enzymes measured did not differ at all ^[22].

Animal data In rats with chronic kidney failure, serum TGF-beta1 and the leakiness of small mesenteric vessels were significantly lower two months in, with no such effect at four and six months ^[24]. In old, half-castrated male rats given 50 µg per animal, the authors report changed luteinising hormone, prolactin and ACTH, with a marked fall in prolactin, but no figures, animal numbers or statistics ^[25].

Findings that point both ways

Animal data In fruit flies, Vilon suppressed reactive oxygen species in mitochondria and stimulated them in the cytosol within the same experiment, so the blanket label "antioxidant effect" in the group's summary tables is not supported ^[23]. In organ explants the direction likewise depended on the donor's age: tissue from 21-day-old rats grew faster at 2 to 20 ng/ml, while thymus tissue from one-day-old rats was suppressed ^[26].

Cell culture In a human monocyte line, all five peptides tested raised the phosphorylation of certain cytoplasmic kinases; the reduction in TNF reported there belongs to another peptide of the series ^[28].

What people were given, outside any trial

Unregistered clinical report Two reports from a hospital group in Chita describe the peptide added to standard treatment in type 1 diabetes, reporting higher antithrombin III and protein C, stimulated fibrinolysis, fewer helper T cells and natural killer cells, and in most cases a lower insulin requirement. Those are indications in the legal sense, and this page reproduces them only as unverified source statements: neither abstract gives case numbers, spread, p-values or a defined endpoint, there was no placebo and no blinding, and the two papers share several authors and may describe one cohort ^[21].

Animal data An independent group in Ivanovo tested the peptide in rats with experimental endometriosis, alone and with surgery, and called the combination promising, without figures, dose or animal numbers ^[27].

What is still unknown

• Whether intact Vilon ever reaches a target, and what the body does with it. No experiment here was designed to answer the first question, and there is no half-life, bioavailability, blood level, distribution or excretion data in any species ^[3], ^[4].
• Whether the DNA binding happens in a living cell. What exists is docking, a gel experiment whose raw data are not accessible, and no independent replication ^[13], ^[14].
• Whether any human effect is real, and what is actually in the traded material. Neither the lifespan claim nor any clinical report has been replicated outside the post-Soviet publishing world, and no independent analysis of identity, purity, endotoxin content or sterility has been published ^[34], ^[41].

Side effects and safety

There is no safety record, because no study anywhere took tolerability or toxicity as its subject ^[3].

• The single safety sentence is an aside. In the mouse lifespan experiment the developers write that long-term administration caused no unfavourable effects and conclude that chronic use is safe, with no animal numbers, dose, measured parameters or statistics ^[19].
• The human reports mention no adverse events, and also no search for them. None contains a section on tolerability, dropouts or adverse events, and absence of records is not absence of harm ^[21].
• The developers report that it suppresses cell suicide. Vilon is described as inhibiting programmed cell death in irradiated spleen lymphocytes, more strongly than a sibling peptide. Suppressing that process is not automatically good, since it is how damaged cells are cleared ^[31].
• Nothing is known about pregnancy, breastfeeding, children, or impaired kidney or liver function. The longest documented human exposure of any Lys-Glu preparation is a 20- to 30-day course of capsules by mouth ^[8].

The gaps are near-total: no toxicology, no dose-finding, no NOAEL, no reproductive or genetic toxicity, no immunogenicity testing, and for the injected form the Western trade actually sells, no safety data at all ^[3], ^[41].

Doses used in studies

The doses below are simply what the cited studies gave, listed so that the results can be understood. They are not advice on how to use anything. The one line describing people comes from a Russian food supplement label, not from a trial.

Every line comes from an animal experiment, cell culture, a patent claim or that label, and no conversion from animal to human is covered. The only documented human amount is thousands of times smaller than the quantities circulating for injection, for which no human safety data exist at all ^[8], ^[41]. Four lines come from tumour studies; German medicines advertising law does not permit this page to reproduce what those studies found, in either direction, so only the amounts appear ^[32].

A concentration in a dish cannot be converted into an amount for a body, and neither can an amount given to an animal; the patent range spans four orders of magnitude, which is legal breadth rather than dose-finding ^[11]. The last line needs its own caution: that product declares a peptide complex rather than the pure dipeptide and is taken by mouth, so neither figure transfers to the injected material sold in the West ^[8]. Schedules for injection do circulate on trade-adjacent pages, above every documented human amount; they cite nothing, several of those pages state within the same text that no measured data exist, and none is reproduced here ^[42].

Development and approval status

There is no development programme: no sponsor, no registered study, no ongoing procedure, and an application that has visibly gone nowhere for more than two decades ^[6], ^[7].

Several rows need care. The European, British, Australian and Swiss findings rest on absence everywhere else, because those registers could not be read on the day of checking, and the American substance identifier is a catalogue number that says nothing about approval ^[10], ^[38]. The Russian row is most often misread: a food supplement passes no test of whether a product works, its own label states that it is not a medicine, and it is not even sold under the name Vilon. The only Russian product with a Vilon-derived name is a cosmetic cream ^[8], ^[43].

All registers were checked on 17 September 2026. The wider legal picture is under are peptides legal and FDA-approved peptides.

Anti-doping

Vilon is prohibited at all times, in and out of competition. It is not named on the 2026 list. It falls inside class S0, which covers any pharmacological substance with no current approval by a government health authority for human therapeutic use ^[9].

Nothing about that needs interpretation, because there is no approval anywhere to argue about. A food supplement registration is not an approval for therapeutic use, and it makes no difference that the molecule is built from two ordinary food amino acids ^[8], ^[9]. The German anti-doping statute's annex does not list it, and that list has no catch-all position for unapproved peptides ^[40]. No validated detection method has been published, which would be hard in any case: the molecule is a normal metabolite and its breakdown products are common amino acids ^[2]. The full picture is at peptides banned in sport.

Compared with related peptides

No head-to-head measure of effect exists, so the table is about place rather than strength: the shortest of the family, with the weakest computed transport and the frankest admission of instability from its own makers. Epitalon and Livagen behave differently in the very experiments they share with Vilon, so borrowing their findings inflates the apparent record ^[3], ^[17].

Common misconceptions

• "Vilon and Epitalon carry the same findings." They do not. In shared experiments they diverge and sometimes point in opposite directions ^[17].
• "It is approved in Russia, and the Russian supplement is Vilon." Neither. The institute's own head wrote in 2020 that it had been submitted for registration, and the Russian medicines database held no product of that name in September 2026. The supplement is not sold under that name, declares a peptide complex rather than the pure dipeptide, is taken by mouth, and states on its own label that it is not a medicine ^[7], ^[8], ^[39].
• "It is a fragment of many cytokines, so it must be active." The pair lysine-glutamic acid occurs in almost any sizeable protein by simple statistics, which is why it is catalogued as a human metabolite. That argues against a special signalling role, not for one ^[2], ^[7].
• "There are no studies on Vilon." Wrong in the other direction: around 60 indexed papers exist, and what is missing is a registered trial, which is a different statement. Not every hit belongs to the peptide either — a bioinformatics method shares the name, a drug-delivery copolymer shares part of the sequence, and several papers test peptides under laboratory codes alone, without sequences ^[6], ^[33], ^[34], ^[44].

Frequently asked questions

What is Vilon?

It is a synthetic peptide of two amino acids, lysine and glutamic acid, written Lys-Glu or KE. At 275.30 g/mol it is the smallest molecule a peptide can be. It came from the St Petersburg Institute of Bioregulation and Gerontology.

Does Vilon survive in the body long enough to do anything?

Nobody has measured it: no half-life, no blood level and no bioavailability figure in any species. Its own developers wrote in 2022 that it breaks down in solution and partly in tissue, more so than the three others they tested alongside it.

Is Vilon approved as a medicine anywhere?

No, and that includes Russia. The head of the developing institute wrote in 2020 that Vilon had been submitted for registration, which is an application rather than an approval, 22 years after the patent filing. The Russian medicines database returned no product of that name on 17 September 2026.

Have there been clinical trials of Vilon?

No registered trial was found in any database checked on 17 September 2026, while a control query returned 782 studies. Unregistered reports from Russian hospitals exist, but none was pre-registered, blinded or published with case numbers.

Can a peptide as small as Vilon really control genes?

That is the central open question. Its developers propose that it binds four-letter stretches of DNA in gene promoters. Those stretches occur millions of times across the human genome, the evidence is mostly computer modelling by the same group, and no independent laboratory has repeated it.

What did the ultra-low-dose paper on Vilon claim?

In 2003 the developing group, with the institute's director as a co-author, reported a second peak of activity between 10 to the minus 17 and 10 to the minus 15 moles per litre. At the lower figure a millilitre holds roughly six thousand molecules, and they explained it as signalling without any ligand-receptor complex, carried by the dynamics of the water.

Is Vilon safe?

Nobody knows. There is no toxicology study, no dose-finding, no immunogenicity testing and no safety data at all for the injected form sold in the West. The one safety sentence in the literature is an aside in a mouse experiment by the developers.

Cite this page

The facts on this page were checked on 17 September 2026, and every register behind the status table was queried that day. Three things could still move: a Russian-language report outside the international databases could surface, a pharmacokinetic measurement could finally be published, and five register entries rest on inference because those registers could not be read.

myPeptides Research & Editing. (2026). Vilon: what the studies show, status and safety. Version 1.0, 17 September 2026. myPeptides Peptide Register. Retrieved from https://mypep.app/peptides/vilon

How pages in this register are compiled and graded is described under methodology; the full register is at peptides.

Last verified: 17 September 2026. Next review: on any registered trial, on any published pharmacokinetic measurement, or on any change to the anti-doping classification.