Vilon Research, Specifications & Scientific Information

Introduction

Vilon is two amino acids long — lysine joined to glutamic acid, 275 daltons — which makes it the smallest molecule in this library with a research literature attached to its own name.

It is also the member of the Khavinson bioregulator series with the clearest origin account. A 1997 paper from the originating group sets out the sequence: a peptide complex acid-extracted from calf thymus became the preparation Thymalin; one immunomodulatory molecule was isolated from that complex by reversed-phase chromatography and became Thymogen; and a further dipeptide was then synthesised and named Vilon ^[1]. The first two were found. This one was designed.

Five limitations run through the whole of this compound's literature and are stated once, here, rather than repeated under every heading. Nearly all primary work originates with the St Petersburg Institute of Bioregulation and Gerontology and its collaborators. A large share is published in Russian, in journals with limited circulation elsewhere. Group sizes are small and frequently unstated in the indexed abstracts. The emphasis falls on organotypic and dissociated cell culture rather than on intact organisms. And independent replication by unrelated groups has not been published for the central findings. None of that makes the work wrong; all of it changes how much weight a single result can carry.

What Is Vilon?

A synthetic dipeptide with free termini: L-lysyl-L-glutamic acid, KE in single-letter code. In the originating group's own papers it also appears under the laboratory code AB-0, which is worth knowing because some of the cell-culture literature identifies it that way rather than by name ^[6].

The design premise behind the series is that a short sequence can reproduce the activity of the tissue extract whose amino acid composition it was drawn from. For this dipeptide the parent material is thymic, and the group's early characterisation places it alongside the natural extract rather than in place of it: both natural and synthetic preparations were reported to activate T-cell differentiation and to alter cytokine output from blood lymphocytes, while the synthetic dipeptides — unlike the natural peptides — had no effect on antioxidant response in thymocytes ^[1]. A reported difference between an extract and a designed dipeptide is the kind of detail that usually drops out of summaries.

Vilon has not been approved by the U.S. Food and Drug Administration for any indication. No marketing application is on record in the United States, and no study of it appears on ClinicalTrials.gov. Its availability elsewhere is under national registrations that confer nothing here.

Vilon Specifications

The formula and mass above are PubChem's record for compound identifier 7010502, the free dipeptide with a free N-terminal amine and a free C-terminal carboxyl. CAS registry number 45234-02-4 and FDA/NCATS unique ingredient identifier H34V7IM5ML are recorded against the same substance, which makes this one of the few compounds in the bioregulator series carrying a full set of register identifiers. Reagent material is frequently supplied as an acetate or trifluoroacetate salt, and a salt-form mass will not equal the 275.30 g/mol figure above. Two residues is short enough that the name, the sequence and the constitution are effectively the same statement; what a register number cannot settle is counter-ion, water content, or whether the material has partly cyclised in storage, and those are questions for the certificate of analysis of a given lot.

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 Vilon Work?

Not established, and the honest form of that answer has three parts.

There is no receptor and no search for one that has succeeded. A 275-dalton molecule with two residues presents very little surface, and the programme that produced it has never proposed receptor pharmacology for it. The specification table above shows primary target, receptor family and agonist status as not publicly characterised, and those entries are accurate rather than unfinished.

The proposed mechanism is chromatin. The hypothesis advanced across the series is that these peptides act on gene expression directly. For this dipeptide the supporting observation is cytogenetic rather than biochemical: chromatin in cultured lymphocytes from elderly donors is reported to decondense in a specific pattern, which is described below under the in vitro heading. What is absent is a structural determination of any peptide–DNA or peptide–protein complex involving this sequence.

Two signalling observations exist and neither closes the gap. Exposure of murine splenocytes was reported to activate interleukin-2 messenger RNA synthesis without any specific inducer present ^[4], and exposure of mouse thymocyte membranes was reported to stimulate sphingomyelinase activity more than the related tetrapeptides tested beside it ^[5]. Both are downstream measurements. Neither identifies what the peptide binds first.

A fourth point is rarely made and matters: no pharmacokinetic dataset for this dipeptide is published in any species. Nothing is known about what fraction of an administered amount survives circulating peptidases, or reaches a cell nucleus, where the proposed mechanism would have to operate.

Vilon Mechanism of Action

In vitro research

Chromatin in lymphocytes from elderly donors. The most-cited result for this compound comes from a cytogenetics group in Tbilisi working with the originating group. Lymphocytes cultured from old donors were exposed to the dipeptide, and four effects were reported: unrolling of total heterochromatin; reactivation of ribosomal genes through decondensation of nucleolus organiser regions; release of genes repressed by age-related condensation of euchromatic regions; and — the negative result, which is the most informative of the four — no decondensation of pericentromeric structural heterochromatin ^[2]. A compound that moves one chromatin compartment and leaves another alone is behaving selectively, which is a stronger claim than a general activation and a more testable one.

A companion study in donors aged 75 to 88 placed the dipeptide beside four other peptides of the series and reported that all of them activated ribosomal genes and decondensed facultative chromatin, while only some acted on pericentromeric heterochromatin of chromosomes 1 and 9 ^[3]. Read together, the two papers describe a graded pattern across the series rather than a single on-switch.

Thymic cell culture. In cultured human and rat thymic cells the dipeptide, identified there by its laboratory code, increased expression of the lymphocyte differentiation marker CD5 and pushed T-cell precursors towards CD4-positive helper cells — and the report is explicit that its effect was weaker than that of the comparator dipeptide tested alongside it ^[6].

Macrophage output, in both directions. Peritoneal macrophages from young and old mice produced less lymphocyte-activating factor with age. Short peptides including this one modulated that production, and the authors describe the effects as opposite in resting and lipopolysaccharide-stimulated macrophages ^[7]. A bidirectional effect is harder to interpret than a monotonic one.

Ageing fibroblast cultures. In human skin fibroblasts aged by serial passage, this dipeptide and three others reduced synthesis of matrix metalloproteinase 9 and raised Ki-67 and CD98hc ^[13].

Everything in this section was observed in cultured cells. None of it establishes anything about an intact animal, and none of it about a person.

What Is Vilon Being Researched For?

• Chromatin state in cells from elderly donors — the decondensation work, which is the compound's signature result ^{[2, 3]}.
• Thymic and splenic cell differentiation — marker expression and cytokine transcription in culture ^{[6, 4]}.
• Renal microvascular physiology — transforming growth factor beta and microvessel permeability in a rat model of chronic renal failure ^[8].
• Chemically induced carcinogenesis — tumour incidence in mice given a colon carcinogen ^[10].
• Digestive enzyme activity in aged animals — membrane and cytosolic enzymes of the small intestine ^[9].
• Peptide transport modelling — docking of the dipeptide, among twenty-five others, at amino acid and peptide transporters ^[14].

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

Human Research on Vilon

Human clinical research

Results from pharmaceutical clinical trials describe the investigational material and populations used in those studies and should not be interpreted as establishing the effects of research-grade materials offered for laboratory use.

Two indexed human reports have been identified. Both concern type 1 diabetes mellitus, both come from the same author group, both are in Russian, and both appeared in Advances in Gerontology.

Coagulation and fibrinolysis, 2006

As reported. People with type 1 diabetes mellitus in a destabilisation phase were described as showing accelerated coagulation, reduced antithrombin III and protein C, raised fibrinogen and soluble fibrin-monomer complexes, and depressed fibrinolysis — a picture the authors interpret as chronic disseminated intravascular coagulation. Conventional treatment was reported to leave those indices largely unchanged, while administration of the dipeptide was reported to reduce or abolish the picture, with a smaller effect in older participants with severe disease ^[11].

Limitations. The indexed abstract gives no participant count, no randomisation, no blinding, no control arm and no effect estimate. The claim that standard treatment did nothing while the study compound did a great deal is exactly the comparison an uncontrolled design cannot support.

Immune status and coagulation, 2007

As reported. In a second report from the same group, adding the dipeptide to combination treatment in elderly participants with type 1 diabetes mellitus was described as raising antithrombin III and protein C, stimulating fibrinolysis, lowering T-helper and natural killer cell counts, normalising active T-lymphocyte, B-lymphocyte and IgA levels, and in most cases permitting a reduction in the insulin amount needed to stabilise carbohydrate metabolism ^[12].

Limitations. The same structural gaps apply, and one more is worth naming. Directionally mixed immunological findings — some counts down, others described as normalised — are presented as a single coherent stabilising effect. Without a control group and a pre-specified endpoint there is no way to distinguish that reading from ordinary variation in a small sample.

Together these two reports are the entire identified human literature on this dipeptide. Neither was registered as a trial.

Preclinical Research on Vilon

Animal research

Chronic renal failure in rats

Rats were studied 2, 4 and 6 months after the onset of experimental chronic renal failure. Subcutaneous administration of the dipeptide significantly reduced serum transforming growth factor beta-1 and the permeability of mesenteric microvessels at the two-month point; the authors describe the result as a homeostatic effect confined to the early period of the disease ^[8]. The confinement is the point. An effect present at two months and not reported at six is a narrower finding than "protects the kidney", and the paper does not claim otherwise.

Chemically induced tumours in mice

Mice given 1,2-dimethylhydrazine, a colon carcinogen, received 10 µg/kg of the dipeptide. Among animals surviving to the first tumour detection at 46 weeks, tumours developed in 14.3% of the treated group against 60% of controls, and preneoplastic change in the kidneys was reported to be inhibited ^[10]. The indexed abstract gives no group sizes and no statistical test, and the denominator is survivors rather than all animals enrolled — a conditioning that can move a proportion substantially on its own.

Intestinal enzymes in aged rats

Oral administration to aged Wistar rats for one month raised the activity of the membrane enzymes maltase and alkaline phosphatase in the epithelial layer of the small intestine, and raised cytosolic glycyl-L-leucine dipeptidase activity in the stromal and seromuscular layers ^[9]. The second observation is the more interesting one: it places an effect in a layer beneath the epithelium, which is the hypothesis the paper was testing.

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

Current Research Status

Status as of September 22, 2026. This block is rendered from maintained fields, not from prose, so it cannot go stale in one place and stay current in another.

Vilon vs Related Compounds

Thymogen :: The other thymic dipeptide, Glu-Trp. It was isolated from the Thymalin extract before being synthesised, whereas this one was synthesised outright ^[1]. Thymogen carries an International Nonproprietary Name and has been studied in registered trials under a separate development code; this dipeptide has neither. Thymalin :: The calf thymus extract that the programme began from — a mixture, not a defined molecule. Findings about the extract are not findings about either dipeptide, and the 1997 paper is explicit that natural and synthetic preparations behaved differently in at least one assay ^[1]. Epitalon and Cortagen :: Tetrapeptides from the same programme, tested beside this one in the splenocyte, thymocyte and chromatin experiments. In those direct comparisons the dipeptide was sometimes the more active of the set and sometimes not, which is the only kind of ranking this literature supports ^{[4, 5, 3]}. Cartalax and Vesugen :: The peptides most often placed beside this one in the recent fibroblast and stem-cell work, where the three are compared as a set ^[13].

Evidentiary position

Not approved by the U.S. Food and Drug Administration, no registered trial, two uncontrolled human reports, and no independent replication of the chromatin work.

No comparison of effect between these compounds is made on this page.

Chemical & Molecular Characteristics

A dipeptide is a demanding analytical object precisely because it is so small, and four properties of this one follow directly from its two residues.

It is unusually well registered for this series. PubChem carries it as compound identifier 7010502 with CAS registry number 45234-02-4 and FDA/NCATS unique ingredient identifier H34V7IM5ML, formula C11H21N3O5 and an average mass of 275.30 g/mol. Most of the bioregulator series has no unique ingredient identifier at all, so a complete set here is worth noting rather than assuming.

Charge is balanced and polarity is extreme. The lysine side-chain amine is basic; the glutamate side chain and the C-terminal carboxyl are acidic. At physiological pH the molecule carries both charges and very little hydrophobic surface — nothing aliphatic or aromatic sits anywhere in it. The practical consequence is poor retention on conventional C18 columns, where a species this polar can elute near the void volume alongside salts and synthesis by-products. A purity figure "by HPLC" is only as good as the method behind it, and for a compound of this polarity the method is most of the claim.

There is no aromatic residue, so there is no useful absorbance at 280 nm. Quantification by ultraviolet absorbance has to rely on the peptide bond near 214 nm, where solvents and buffer components also absorb. This is a genuine constraint on every lot of this material and it is one of the sharpest differences between this dipeptide and Glu-Trp, whose tryptophan makes it straightforward to quantify.

Dipeptides cyclise. Linear dipeptides are prone to intramolecular cyclisation to the corresponding 2,5-diketopiperazine, which is a distinct compound of lower mass formed by loss of water. It is favoured by heat, by moisture and by time in solution. Mass spectrometry distinguishes the cyclic species from the linear one because their masses differ, but only if the analysis is asked to look; a certificate reporting a single expected mass says nothing about a degradation product nobody searched for.

A fifth point belongs here rather than in the mechanism section. A 2022 modelling study docked this dipeptide, with twenty-five other ultrashort peptides, at the LAT1, LAT2 and PEPT1 transporters and reported that the biologically active set bound more efficiently than randomly chosen di- and tripeptides ^[14]. That is a computational result about a transport route, offered as a hypothesis for how such peptides might enter a cell at all. It is not a measurement of transport, and the paper does not present it as one.

Frequently Asked Questions

Scientific References

1. Morozov VG, Khavinson VK. Natural and synthetic thymic peptides as therapeutics for immune dysfunction International journal of immunopharmacology; 1997. PMID 9637345 doi:10.1016/s0192-0561(97)00058-1
2. Lezhava T, Khavison V, Monaselidze J, et al.. Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people Biogerontology; 2004. PMID 15105581 doi:10.1023/B:BGEN.0000025070.90330.7f
3. Khavinson VKh, Lezhava TA, Malinin VV. Effects of short peptides on lymphocyte chromatin in senile subjects Bulletin of experimental biology and medicine; 2004. PMID 15085253 doi:10.1023/b:bebm.0000024393.40560.05
4. Kazakova TB, Barabanova SV, Khavinson VKh, et al.. In vitro effect of short peptides on expression of interleukin-2 gene in splenocytes Bulletin of experimental biology and medicine; 2002. PMID 12447482 doi:10.1023/a:1020210615148
5. Khavinson VKh, Rybakina EG, Malinin VV, et al.. Effects of short peptides on thymocyte blast transformation and signal transduction along the sphingomyelin pathway Bulletin of experimental biology and medicine; 2002. PMID 12420072 doi:10.1023/a:1019830308824
6. Sevostianova NN, Linkova NS, Polyakova VO, et al.. Immunomodulating effects of Vilon and its analogue in the culture of human and animal thymus cells Bulletin of experimental biology and medicine; 2013. PMID 23486604 doi:10.1007/s10517-013-2000-0
7. Gumen AV, Kozinets IA, Shanin SN, et al.. Production of lymphocyte-activating factors by mouse macrophages during aging and under the effect of short peptides Bulletin of experimental biology and medicine; 2006. PMID 17426849 doi:10.1007/s10517-006-0366-y
8. Gavrisheva NA, Malinin VV, Ses TP, et al.. Effect of peptide Vilon on the content of transforming growth factor-beta and permeability of microvessels during experimental chronic renal failure Bulletin of experimental biology and medicine; 2005. PMID 16142267 doi:10.1007/s10517-005-0202-9
9. Khavinson VKh, Timofeeva NM, Malinin VV, et al.. Effect of vilon and epithalon on activity of enzymes in epithelial and subepithelial layers in small intestine of old rats Bulletin of experimental biology and medicine; 2002. PMID 12660839 doi:10.1023/a:1022913228900
10. Pliss GB, Mel'nikov AS, Malinin VV, et al.. [The effect of vilon (Lys-Glu) on 1.2-dimethylhydrazine-induced neoplasia] Voprosy onkologii; 2005. PMID 16308980
11. 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] Advances in gerontology = Uspekhi gerontologii; 2006. PMID 17152731
12. 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] Advances in gerontology = Uspekhi gerontologii; 2007. PMID 18306698
13. Lin'kova NS, Drobintseva AO, Orlova OA, et al.. Peptide Regulation of Skin Fibroblast Functions during Their Aging In Vitro Bulletin of experimental biology and medicine; 2016. PMID 27259496 doi:10.1007/s10517-016-3370-x
14. 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

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Research-Use Information

For in vitro research use only. This material is a laboratory reagent. It is not a drug, food, dietary supplement, or cosmetic and is not for human or veterinary use, including ingestion, injection, or any other administration. No information on this page describes or implies any effect in humans or animals. Sold only to researchers under our Terms of Sale.