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Vilon

Tier 3 · Reported use
Also known as KE peptide · Lys-Glu dipeptide

The strongest evidence present is Tier 2 (animal, in-vitro, and mechanistic studies). Nearly all data derive from a single research program (Khavinson's St. Petersburg Institute of Bioregulation and Gerontology), predominantly in Russian-language literature, with little independent Western replication. Efficacy data are dominated by cell-culture and rodent studies plus ex vivo work on aged human lymphocyte chromatin; the only human data are one group's 12-year observational cohort follow-up. There are no randomized controlled human trials and no approved indications.

Half-life
~1.2 h
Routes
Subcutaneous injection · Intramuscular injection · Intravenous (used in PK reporting) · Oral / sublingual (Russian retail; intact-peptide oral bioavailability not demonstrated)
Goals
Immune support / immunomodulation · Longevity / geroprotection · Cancer/tumor prevention research (preclinical) · Anti-inflammatory research
Cost / mg
Not recorded

How it works

Vilon is one of the simplest possible bioregulators — a two-amino-acid peptide (lysine plus glutamic acid) developed within the Soviet-era Khavinson peptide bioregulator program. Its developers propose that, because it is so small, it can slip into the cell nucleus and bind specific DNA sequences to gently switch certain genes on or off, particularly genes involved in immunity and cell growth. In laboratory studies it appears to 'unwind' certain compacted regions of chromatin in cells from elderly people, reawakening some silenced genes, while leaving other regions untouched. In animals it has been reported to stimulate immune tissue, tune inflammatory signaling, prolong lifespan, and reduce the development of tumors. Importantly, the DNA-binding/epigenetic story is based mostly on computer modeling and cell-culture work, not confirmed in humans, and almost all of the evidence comes from a single research group.

Overview

Overview

Vilon (also called the KE peptide or Lys-Glu dipeptide) is a synthetic dipeptide composed of L-lysine and L-glutamic acid (Lys-Glu, abbreviated KE). It has a molecular weight of approximately 275.30 g/mol, the molecular formula C11H21N3O5, and CAS number 45234-02-4. It is described as among the shortest known biologically active peptides — the shortest bioactive peptide in the Khavinson bioregulator program.

Origin

Vilon was developed by Professor Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology, first synthesized in the 1970s as part of a Soviet-era peptide bioregulator program. It was originally identified as one of three principal active components of Thymalin, the bovine thymic extract that became the first peptide bioregulator preparation approved in the USSR (1982).

Proposed Mechanism

According to its developers, Vilon's small size allows it to enter cell nuclei, bind sequence-specific sites in gene-promoter DNA, and remodel chromatin to selectively modulate expression of immune- and proliferation-related genes. This proposed DNA-binding/epigenetic mechanism is model-based (molecular docking) and not clinically confirmed. Molecular docking identified GCGC as the preferred double-stranded DNA sequence (in the curved nucleosomal form), and cluster analysis nominated genes encoding AKT1/AKT2 — proteins implicated in cytokine-storm development — as potential targets.

In cultured lymphocytes from elderly donors (age 75–88), Vilon induced deheterochromatinization (decondensation) of total facultative heterochromatin, reactivated ribosomal genes, and released age-silenced genes — an effect that increased progressively with donor age. Notably, it did not decondense pericentromeric structural heterochromatin, indicating selective, region-specific effects. In mesenchymal stem cells it regulated IGF1, FOXO1, TERT, and NFkB; in the THP-1 monocyte/macrophage line it produced modest, receptor-independent shifts in proliferative and inflammatory gene programs. A bioinformatic analysis of 20,417 UniProt proteins found KE motifs enriched in cytoplasmic and nuclear proteins and minimal in membrane proteins, supporting a model in which KE released during proteolysis binds DNA to regulate transcription.

Preclinical Findings

Decades of predominantly preclinical (largely Russian-language) research have investigated Vilon's effects on immune function, lifespan, tumor prevention, and cardiovascular gene expression:

  • Immune: KE stimulates cellular immunity and nonspecific resistance, activating macrophages, blood lymphocytes, thymocytes, and neutrophils. It stimulated thymus explant growth in organotypic culture and promoted immune-cell differentiation. Rodent studies reported improved CD4/CD8 ratios and innate immune markers.
  • Anti-inflammatory: In an in vitro inflammatory model, Thymalin and its EW and KE dipeptides reduced synthesis of IL-1β, IL-6, and TNF-α in human peripheral blood mononuclear cells by 1.4–6.0 times.
  • Geroprotection: In female CBA mice, subcutaneous Vilon from the 6th month of life increased physical activity and endurance, decreased body temperature, prolonged lifespan, and prevented spontaneous neoplasms — but had no effect on age-related estrous changes or free-radical processes.
  • Oncostatic: At 10 µg/kg, Vilon reduced tumor development in a 1,2-dimethylhydrazine model to 14.3% vs 60% in controls and inhibited preneoplastic kidney changes; it decreased urinary bladder tumor incidence in a nitrosamine rat model (56% vs 75.5%); and at 1 mg/kg increased survival of mice with transplanted Lewis lung carcinoma.
  • Other: Oral administration for 1 month improved small-intestine glucose transport in aged rats. In mouse heart, Vilon altered expression of a small fraction of a cDNA library, with broader changes when combined with Epithalon.

Human Data & Positioning

Human data are limited to ex vivo studies of aged lymphocyte chromatin and one group's cohort follow-up. Khavinson's group has published 12-year follow-up cohort data reporting reduced mortality in elderly subjects taking annual Vilon + Thymalin cycles, and has claimed telomerase upregulation in immune cell lines — both from a single group without independent replication. Vilon is studied and positioned as an immune modulator, claimed geroprotector, and immune-targeted short bioregulator, sometimes paired with Thymalin for claimed synergistic effects on T-cell maturation and innate immunity. Thymalin itself (whose active substances include KE and EW) has reported efficacy in acute respiratory distress syndrome, COPD, and complex therapy of severe COVID-19 in middle-aged and elderly patients.

Important Limitations

Nearly all Vilon evidence comes from one research program with little independent replication, predominantly in Russian-language literature. There are no human randomized controlled trials and no approved indications. The DNA-binding/chromatin mechanism is model-based, not clinically confirmed. Oral bioavailability of the intact dipeptide is proposed on the basis of its small size but has not been demonstrated in formal pharmacokinetic studies.

What the research shows

195 findings extracted from the 30 sources cited below, strongest evidence first within each group. Every one links to the source it came from.

What human studies found

Based on 4 human study findings, 22 animal findings, 1 in vitro finding, 14 expert opinion findings and 2 theoretical findings.

  • human studyThymalin is an immunomodulatory drug containing a polypeptide extract of thymus that has demonstrated efficacy in the therapy of acute respiratory distress syndrome and chronic obstructive pulmonary disease, as well as in complex therapy related to severe COVID-19 in middle-aged and elderly patients8

  • human studyKhavinson's group has published 12-year follow-up cohort data showing reduced mortality in elderly subjects taking annual Vilon + Thymalin cycles22

  • human studyPersistence and adherence in anti-obesity drug use are low26

  • human studyPersistence and compliance in anti-obesity drug use can be significantly increased by reducing the dosing frequency26

  • animalVilon (L-Lys-L-Glu) inhibits growth of spontaneous tumors in mice2

  • animalVilon increases life span of mice2

  • animalExtended lifespan and inhibited spontaneous tumor growth in CBA mice with chronic subcutaneous administration5

  • animalEffect shown mainly in rodent and cell-culture models6

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  • animalMouse studies report inhibition of spontaneous tumors and increased mean life span6

  • animalAfter vilon treatment at 10 microg/kg, tumors developed in 14.3% of mice that survived until first tumor detection at 46 weeks11

  • animalIn control group, tumors occurred in 60%11

  • animalVilon-related inhibition of preneoplastic alterations in the kidneys was reported11

  • animalInjections of synthetic peptide vilon at the doses 1 mg/kg significantly increased the survival of mice with transplanted Lewis lung carcinoma13

  • animalVilon (Lys-Glu) decreased the incidence of urinary bladder tumors in rats treated with N-butyl-N-(4-hydroxybutyl)nitrosamine carcinogen16

  • animalVilon significantly inhibited carcinogenesis in urinary bladder16

  • animalSubcutaneous administration of vilon (Lys-Glu) to female CBA mice starting from the 6th month of life increased physical activity and endurance18

  • animalVilon decreased body temperature in female CBA mice18

  • animalVilon prolonged the lifespan in female CBA mice18

  • animalVilon prevented the development of spontaneous neoplasms in female CBA mice18

  • animalVilon had no effect on age-related changes of estrous function in female CBA mice18

  • animalVilon had no effect on free radical processes in female CBA mice18

  • animalKhavinson-group studies span animal models, cell-culture work, and gene-expression profiling21

  • animalVilon has demonstrated measurable effects in animal models of aging, carcinogenesis, and immune function, and in ex vivo studies of aged human lymphocyte chromatin24

  • animalIn mouse studies, Vilon extended lifespan and reduced tumor growth28

  • animalMouse lifespan studies show extension and tumor inhibition28

  • animalVilon extended lifespan and inhibited spontaneous tumors in CBA mice28

  • in vitroAn in vitro model of an inflammatory reaction demonstrated that Thymalin and EW and KE dipeptides reduced the synthesis of IL-1β, IL-6, and TNF-α cytokines in human peripheral blood mononuclear cells by 1.4-6.0 times8

  • expert opinionPeptides demonstrate effective target engagement and clinically meaningful efficacy3

  • expert opinionDisease-specific therapeutic applications including tumor regression, metabolic regulation, neuroprotection, and immune modulation have demonstrated beneficial effect3

  • expert opinionNo large controlled human trials, no approved indication, and limited independent replication6

  • expert opinionEvidence dominated by a single research program with little independent replication and essentially no robust human RCTs6

  • expert opinionVilon is showing remarkable promise in experimental biology and longevity research19

  • expert opinionDecades of preclinical research, predominantly from Russian-language literature, have investigated Vilon's effects on immune function, lifespan, tumor prevention, and cardiovascular gene expression20

  • expert opinionOver four decades of published research, predominantly preclinical; human data limited to in vitro studies on elderly donor cells20

  • expert opinionHundreds of publications, primarily in Russian-language journals; limited English-language peer-reviewed literature20

  • expert opinionNo registered human clinical trials identified; human cell studies conducted in vitro20

  • expert opinionPublished Vilon record is thin and preclinical21

  • expert opinionThere are no Western randomized controlled trials22

  • expert opinionDecades of preclinical research have investigated Vilon's effects on immune function, lifespan, tumor prevention, and cardiovascular gene expression23

  • expert opinionNo human clinical trials have been registered or published23

  • expert opinionHuman data consists primarily of in vitro experiments on cultured lymphocytes taken from elderly donors23

  • theoreticalPeptide KE exhibits immunoprotective, geroprotective, and oncostatic activities9

  • theoreticalNo controlled human trial has ever been published for Vilon28

How it works

Based on 3 human study findings, 14 animal findings, 30 in vitro findings, 22 expert opinion findings and 19 theoretical findings.

  • human studyPeptide bioregulator Lys-Glu (Vilon) induces deheterochromatinization (decondensation) of total heterochromatin in lymphocytes from 75-88-year-old individuals7

  • human studyVilon activates synthetic processes of ribosomal genes without causing deheterochromatinization of pericentromeric structural heterochromatin7

  • human studyVilon has selective effects on definite regions of chromosomes, inducing selective remodeling of facultative heterochromatin7

  • animalVilon has antineoplastic (anti-tumor) pharmacology2

  • animalKE stimulates cellular immunity and nonspecific resistance in organisms, exerting an activating effect on macrophages, blood lymphocytes, thymocytes, and neutrophils8

  • animalVilon possesses oncomodulating action on transplanted carcinoma13

  • animalVilon enhanced passive glucose accumulation in the serous fluid in inverted sac made from the distal region of the small intestine14

  • animalVilon stimulated active glucose accumulation in the serous sac of the medial small intestine14

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  • animalVilon changed expression of 36 clones out of 15,247 total clones from a cDNA library in mouse heart15

  • animalVilon alone or in combination with Epithalon activated expression of 157 clones (maximally by 6.13 times)15

  • animalVilon alone or in combination with Epithalon inhibited expression of 23 clones (maximally by 2.79 times)15

  • animalCombined treatment with Vilon and Epithalon changed expression of 144 clones15

  • animalVilon has specific effects on gene expression15

  • animalVilon 2-fold decreased the incidence of preneoplastic and early neoplastic changes in urinary bladder mucosa16

  • animalVilon stimulated the growth of explants from thymus in organotypic cultures17

  • animalVilon produced tissue-specific effects, stimulating growth of explants from tissues whose cytomedins (peptide complexes) were used for chemical synthesis17

  • animalRodent studies showing improved CD4/CD8 ratios and innate immune markers22

  • in vitroNew strategy for enhancing the in vivo half-life of peptides without compromising their potency1

  • in vitroInduced deheterochromatinization (chromatin unrolling) in aged lymphocytes, potentially reactivating silenced genes5

  • in vitroImmunomodulatory effects on thymus cell cultures, promoting immune cell differentiation5

  • in vitroRegulated expression of IGF1, FOXO1, TERT, and NFkB genes in mesenchymal stem cells in vitro5

  • in vitroCell-culture work shows chromatin deheterochromatinization in elderly-donor lymphocytes6

  • in vitroModest, receptor-independent immune signaling effects in THP-1 macrophages6

  • in vitroUsing molecular docking, GGAG was found to be the best dsDNA sequence in the classical B-form for binding the EW dipeptide, while GCGC is the preferred dsDNA sequence in the curved nucleosomal form for the KE dipeptide8

  • in vitroCluster analysis revealed that potential target genes for the EW and KE peptides encode the AKT1 and AKT2 proteins involved in the development of the cytokine storm8

  • in vitroThe levels of KE motifs were maximum in cytoplasmic and nuclear proteins9

  • in vitroThe presence of KE in the membrane and all other proteins was the minimum9

  • in vitroVilon activates synthetic processes, caused by reactivation of ribosomal genes as a result of deheterochromatinization (decondensation) of nucleolus organizer regions10

  • in vitroVilon induces unrolling (deheterochromatinization) of total heterochromatin10

  • in vitroVilon releases genes repressed by heterochromatinization (condensation) of euchromatic regions forming facultative heterochromatin10

  • in vitroVilon does not induce deheterochromatinization of pericentromeric structural heterochromatin10

  • in vitroVilon causes activation (deheterochromatinization) of chromatin in lymphocytes of old individuals10

  • in vitroVilon induces unrolling (deheterochromatinization) of total heterochromatin12

  • in vitroVilon activates synthetic processes caused by the reactivation of ribosomal genes as a result of deheterochromatinization of nucleolus organizer regions12

  • in vitroVilon releases genes repressed due to the condensation of euchromatic regions forming facultative heterochromatin12

  • in vitroVilon does not induce decondensation of pericentromeric structural heterochromatin12

  • in vitroVilon stimulated apoptosis in spleen organotypic tissue culture in both young and old rats13

  • in vitroThe inhibitory effect of cyclophosphan was abolished in the presence of vilon in culture media at the dose 5 ng/ml13

  • in vitroKhavinson's group has published cell-culture studies showing increased telomerase activity in human immune cell lines exposed to KE22

  • in vitroThe KE dipeptide shows energetically favorable binding to specific DNA motifs, potentially modulating transcription of downstream genes involved in immune cell proliferation, differentiation, and cytokine production24

  • in vitroIn cultured lymphocytes from elderly subjects (age 75-88), Vilon induced activation of ribosome genes, decondensation of densely packed heterochromatin fibrils, and release of genes that had been repressed through age-specific chromatin condensation24

  • in vitroIn the THP-1 monocyte/macrophage cell line, Vilon modulated expression of genes associated with proliferative activity and inflammatory pathways, including effects on cytokine balance and apoptosis regulation24

  • in vitroIn lab dishes, Vilon appears to open up tightly packed DNA in aging immune cells28

  • in vitroEx vivo studies show chromatin remodeling in aged human lymphocytes28

  • in vitroIn vitro work shows cytokine modulation28

  • in vitroVilon reported to decondense heterochromatin and reactivate ribosomal genes in aged human lymphocytes (ex vivo)28

  • in vitroVilon modulated proliferative activity and inflammatory pathways in THP-1 monocyte/macrophage cell line28

  • expert opinionVilon is a tiny dipeptide (Lys-Glu)19

  • expert opinionVilon is a synthetic dipeptide consisting of just two amino acids, lysine and glutamic acid20

  • expert opinionVilon studied primarily for its ability to remodel chromatin structure and reactivate genes silenced by aging20

  • expert opinionKey mechanisms: Chromatin deheterochromatinization, ribosomal gene reactivation, interleukin-2 upregulation, tyrosine kinase signaling modulation20

  • expert opinionVilon is a short-peptide analog associated with the Thymalin thymus extract21

  • expert opinionVilon is a dipeptide of Lys-Glu (KE)22

  • expert opinionKhavinson's group positions it as the immune-targeted short bioregulator, paired with Thymalin for synergistic effects on T-cell maturation and innate immunity22

  • expert opinionCell- and nucleus-permeable, binds DNA promoter regions, modulates immune-cell gene expression in a tissue-specific manner22

  • expert opinionVilon is sometimes claimed to upregulate telomerase activity in immune cells22

  • expert opinionVilon is a synthetic dipeptide consisting of lysine and glutamic acid23

  • expert opinionVilon holds the distinction of being among the shortest known biologically active peptides23

  • expert opinionVilon's primary mechanism appears to operate at the level of chromatin, the complex of DNA and proteins that controls which genes are accessible for transcription23

  • expert opinionAs organisms age, certain genes become progressively silenced through tightening of chromatin structure23

  • expert opinionPeptides exhibit unique and powerful pharmacology that has not been possible to effectively mimic with either small molecules or antibodies25

  • expert opinionPEGylation was one of the first chemical modification techniques shown to increase peptide half-life by decreasing the rate of renal filtration25

  • expert opinionLipidation has been utilised to extend peptide half-life25

  • expert opinionClassical genetic fusions offer advantages in terms of half-life but also their own severe constraints in terms of drug design25

  • expert opinionPEGylation can make proteins or peptides more water-soluble and protect them from degradation by proteolytic enzymes25

  • expert opinionPEGylation can reduce the affinity of therapeutic proteins to their cognate cellular receptors25

  • expert opinionPEG is attached to the -amino groups of lysine on the surface of proteins or peptides25

  • expert opinionAt high pH (8.0 or higher), lysine side chain amino groups are covalently attached to PEG through N-hydroxy succinimides25

  • expert opinionThe most common half-life extension technologies used for peptides include lipidation, PEGylation, and Fc fusions, all of which allow only weekly administration26

  • theoreticalVilon is a synthetic dipeptide2

  • theoreticalPeptides interact with specific receptors to elicit highly selective biological responses3

  • theoreticalPeptides often demonstrate higher specific activity per unit mass, approximately 15-60 times that of antibodies, due to their lower molecular weight and more efficient receptor engagement3

  • theoreticalVilon is a synthetic Lys-Glu dipeptide proposed to enter cells, bind sequence-specific sites in gene-promoter DNA and remodel chromatin, thereby modulating expression of immune- and proliferation-related genes6

  • theoreticalProposed DNA-binding/epigenetic mechanism is model-based (molecular docking), not clinically confirmed6

  • theoreticalKE and EW dipeptides are active substances of Thymalin8

  • theoreticalEW reduces angiotensin-induced vasoconstriction and preserves endothelium-dependent vascular relaxation by inhibiting ACE2, the target protein of SARS-CoV-28

  • theoreticalPeptide KE stimulates functional activity of fibroblasts9

  • theoreticalThe KE motif is present in amino acid sequences of some cytokines and peptide hormones functionally similar to KE peptide9

  • theoreticalKE peptide molecules released from nuclear proteins during limited proteolysis can bind to DNA and regulate gene expression9

  • theoreticalMolecular weight: 275.30 g/mol20

  • theoreticalVilon is a synthetic dipeptide with the amino acid sequence Lys-Glu (KE), consisting of L-lysine linked to L-glutamic acid by a peptide bond, with a molecular weight of 275.30 g/mol24

  • theoreticalThe optimal half-life is about equal to the dosing interval26

  • theoreticalAccording to its developers, this two-amino-acid molecule can enter cell nuclei, interact with DNA, and selectively modulate immune gene expression28

  • theoreticalThe assembly of peptides is generally mediated by liquid-liquid phase separation, which enables control over assembly kinetics, final structure, and functions of peptide-based supramolecular materials.29

  • theoreticalModulating phase separation can alter the assembly kinetics of peptides by changing solvents or introducing external fields.29

  • theoreticalThe assembly of peptides can be effectively catalyzed by complex coacervates.29

  • theoreticalNegatively charged sodium alginate (SA) can form complex coacervates with the positively charged KLVFFAE (Aβ, abbreviated as KE) peptide, thereby lowering the nucleation barrier and promoting the assembly of the peptide.29

  • theoreticalAs the binding affinity of SA-KE and the dosage of SA decrease, the system shifts from a relatively inefficient template-induced assembly to a highly efficient catalytic assembly before ultimately reverting to slow spontaneous assembly.29

Dosing

Based on 1 animal finding and 4 expert opinion findings.

  • animalRussian experimental/clinical work used short intramuscular injection courses and rodent studies used microgram-to-milligram parenteral doses6

  • expert opinionNo validated human dosing protocols exist; all research is from a single research group (Khavinson) without independent replication5

  • expert opinionStandard biohacker / research dosing is 100–200 mcg subcutaneously daily for 10–14 days, repeated 2–3 times per year22

  • expert opinionRussian clinical dose for immunodeficiency, post-infection recovery is 0.5–2 mg IM for 10 days22

  • expert opinionRussian retail sublingual / oral dosing is drops or caps 3–4×/day for 30 days, 3×/year22

How the body handles it

Based on 1 animal finding, 5 expert opinion findings and 5 theoretical findings.

  • animalElimination half-life averages 1.2 ± 0.4 hours following intravenous dosing4

  • expert opinionChallenges remain in improving peptide stability and delivery3

  • expert opinionShort half-lives resulting from sensitivity to proteases and rapid renal clearance mean that peptide drugs tend to require frequent doses25

  • expert opinionPEGylation improved the pharmacokinetics of proteins even in the absence of anti-drug antibodies25

  • expert opinionIncreasing size or hydrodynamic radius led to reduced renal clearance and increased half-life25

  • expert opinionAMG133 – a GLP-1 agonist/GIP antagonist mAb – has a half-life of 14 days yet is dosed every month26

  • theoreticalExtremely small molecular size (275 Da dipeptide) enabling potential oral bioavailability5

  • theoreticalOral bioavailability of intact vilon dipeptide has not been demonstrated in formal pharmacokinetic studies5

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  • theoreticalPlasma half-life is expected to be very short (on the order of minutes)6

  • theoreticalAll peptides have short in vivo half-lives of minutes to hours and require some form of half-life extension to make them practical for use as therapeutics26

  • theoreticalVilon weighs approximately 275 daltons, making it one of the smallest bioactive peptides on record28

Safety and side effects

Based on 3 human study findings, 7 animal findings, 10 expert opinion findings and 1 anecdotal finding.

  • human studyRussian clinical literature reports rare local injection-site reactions22

  • human studyThe GI toxicity of GLP-1 agonists is related to dosing frequencies in the order twice daily (BID) > daily (QD) > weekly (QWk)26

  • human studyGI effects are less common with long-acting than short-acting compounds26

  • animalThe longest published safety study for Vilon spans 12 months in rat models4

  • animalChronic vilon administration in mouse studies was associated with increased lifespan, reduced spontaneous tumor incidence, and improved physical parameters without adverse effects on development or estrous function5

  • animalSynchronous injection of both vilon and cyclophosphan at the doses 100 mg/kg decreases the survival of mice13

  • animalLong-term administration of vilon caused no unfavourable effects on animal development18

  • animalResults show safety of chronic vilon administration18

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  • animalThat claim rests on a small body of preclinical animal and cell-culture work from a single Russian research lineage21

  • animalAdverse events were not a documented finding in Khavinson-group studies21

  • expert opinionPeptides generally demonstrate favorable safety profiles with minimal adverse events3

  • expert opinionResearch use only; not approved for human therapeutic application in any major jurisdiction20

  • expert opinionThe originators describe the whole bioregulator family as producing practically no side effects21

  • expert opinionNear-zero third-party Western replication exists for Vilon safety data21

  • expert opinionVilon is not FDA-approved for any indication21

  • expert opinionVilon is not FDA-approved22

  • expert opinionNo serious AEs documented at standard doses22

  • expert opinionUse during active autoimmune flare is not well-characterized – Vilon modulates T-cell function and the direction of effect in active autoimmunity is unknown22

  • expert opinionVilon is classified as research use only; not approved for human therapeutic application in any major jurisdiction23

  • expert opinionVilon is not registered as a pharmaceutical in any country and is marketed as a peptide dietary supplement and has not been evaluated by the FDA, EMA, or other Western regulatory agencies24

  • anecdotalThe most consistent community feedback for subcutaneous bioregulator use is mild redness, itching, or tenderness at the injection site, typically short-lived21

What people use it for

Based on 3 animal findings, 1 in vitro finding, 9 expert opinion findings and 1 theoretical finding.

  • animalVilon (Lys-Glu) influences 1.2-dimethylhydrazine-induced neoplasia in mice11

  • animalVilon and cytostatic drugs must not be used synchronously in cancer therapy13

  • animalVilon (Lys-Glu) administered orally for 1 month improved transport characteristics of the small intestine in aged rats14

  • in vitroVilon causes progressive activation (deheterochromatinization) of the facultative heterochromatin with increased aging12

  • expert opinionShort peptide bioregulators like Vilon open up new opportunities in the treatment of aging diseases through chromosome region remodeling7

  • expert opinionVilon could help regulate immunity19

  • expert opinionVilon could help regulate gene expression19

  • expert opinionVilon could help regulate cellular aging19

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  • expert opinionVilon could help with tissue regeneration19

  • expert opinionVilon is studied as an immune modulator and claimed geroprotector21

  • expert opinionVilon is studied for its ability to remodel chromatin structure and reactivate genes silenced by aging23

  • expert opinionVilon research investigates whether the peptide can reverse this silencing in a selective and controlled way23

  • expert opinionPeptides suffer from drawbacks, in particular, the lack of oral bioavailability which necessitates injections25

  • theoreticalProdrugs of low-clearance GLP-1 agonists could produce ultralong-acting agonists with dosing intervals reaching 3 to even 6 months26

Other findings

Based on 1 animal finding, 9 expert opinion findings and 3 theoretical findings.

  • animalVilon composition is Lys-Glu14

  • expert opinionVilon (L-lysyl-L-glutamic acid, abbreviated KE) is a synthetic dipeptide consisting of lysine and glutamic acid developed by Professor Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology5

  • expert opinionFirst synthesized in 1970s as part of Professor Vladimir Khavinson's Soviet-era peptide bioregulator program20

  • expert opinionVilon is a synthetic dipeptide from the Khavinson peptide-bioregulator family21

  • expert opinionVilon was first synthesized in the 1970s as part of Professor Vladimir Khavinson's Soviet-era peptide bioregulator program23

  • expert opinionThe overwhelming majority of publications originate from Russian-language literature and from Khavinson's own research group23

  • expert opinionVilon was developed by Vladimir Khavinson at the Saint Petersburg Institute of Bioregulation and Gerontology as the shortest bioactive peptide in the peptide bioregulator program24

  • expert opinionVilon was originally identified as one of three principal active components of Thymalin, the bovine thymic extract that was the first peptide bioregulator preparation approved in the USSR (1982)24

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  • expert opinionNearly all the data comes from one lab28

  • expert opinionAll published data from Vilon comes from Khavinson's institutional network with no independent replication28

  • theoreticalVilon is mentioned in a reference list or header structure for a peptide half-life chart27

  • theoreticalVilon is a synthetic peptide made of two amino acids—lysine and glutamic acid28

  • theoreticalVilon was developed by Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology as part of a family of bioregulator peptides designed to restore organ function by switching genes back on28

Points of contention

Where the evidence is unsettled, thin, or says less than the popular claim — worth knowing before you draw conclusions.

Single source

Nearly all Vilon evidence comes from one research program with little independent replication.

Multiple sources note the evidence is dominated by Khavinson's institutional network, predominantly in Russian-language literature, with essentially no independent Western replication of efficacy or safety data.

Limited evidence

No human randomized controlled trials or approved indications exist for Vilon.

Sources agree there are no large controlled human trials, no registered/published human clinical trials, and no approved indication; human data is limited to in vitro studies on cells from elderly donors and one group's cohort follow-up. The bulk of efficacy data is animal and cell-culture.

Contested

Reported half-life estimates conflict (minutes vs ~1.2 hours).

One source states the plasma half-life is expected to be very short, on the order of minutes (theoretical), while another reports an elimination half-life of 1.2 ± 0.4 hours after IV dosing. No robust human PK data reconciles these.

Limited evidence

Oral bioavailability is proposed but not demonstrated.

Sources note the small ~275 Da size is claimed to enable potential oral bioavailability, but also explicitly state oral bioavailability of intact vilon has not been demonstrated in formal pharmacokinetic studies.

Limited evidence

The DNA-binding/chromatin mechanism is model-based, not clinically confirmed.

The proposed nuclear entry, sequence-specific DNA binding, and epigenetic gene modulation rest largely on molecular docking and cell-culture/ex vivo work, and are described as not clinically confirmed.

Single source

Claims of telomerase upregulation and reduced-mortality cohort data come from a single group.

The telomerase upregulation claim and the 12-year follow-up cohort reporting reduced mortality with Vilon+Thymalin derive from Khavinson's group only, without independent replication.

Using it with other compounds

Check a stack
  • SelankComplementary

    No documented conflict

    Selank (a tuftsin-derived peptide) carries immunomodulatory and Th1/Th2-balancing activity alongside its main anxiolytic/nootropic role. That immune-modulating side overlaps with Vilon's T-cell and cytokine effects, so the two can complement each other where both immune support and CNS/stress effects are desired.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms clearly establish the claimed shared dimensions. Vilon demonstrates T_cell_regulation (stimulation of thymus tissue growth, immune cell differentiation, improved CD4/CD8 ratio, reactivation of age-silenced genes in aged lymphocytes) and anti_inflammatory effects (IL-1β/IL-6/TNF-α cytokine suppression, IL-2 upregulation). Selank demonstrates T_cell_regulation (Th1-Th2 balancing via cytokine/interferon signaling) and anti_inflammatory activity (approved tags include both). The proposed complementary relationship is justified: Vilon operates primarily through gene-promoter DNA binding and chromatin remodeling to modulate immune function, while Selank operates through receptor-mediated pathways (GABA-A, serotonin, enkephalinase) with immune modulation as a secondary effect. Their distinct mechanisms of action supporting overlapping immune outcomes (T-cell regulation and anti-inflammatory effects) logically support a complementary rather than redundant relationship.

    Shares anti inflammatory · T cell regulation

  • LL-37Complementary

    Worth caution

    LL-37 is a human cathelicidin providing frontline antimicrobial and innate-immune signaling; Vilon supports adaptive/T-cell immunity via gene reactivation. They cover different arms of immunity, so they are complementary rather than redundant, though LL-37's context-dependent pro-inflammatory effects warrant monitoring.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    The mechanisms clearly establish complementary roles in immunity. Vilon targets adaptive immunity (T-cell regulation, CD4/CD8 ratio improvement, thymus stimulation, age-silenced gene reactivation in lymphocytes) via receptor-independent chromatin remodeling and gene expression modulation. LL-37 targets innate immunity (antimicrobial activity, TLR/FPR2 signaling, neutrophil chemotaxis, NET promotion) via multiple cell-surface receptors. Both peptides modulate anti-inflammatory pathways (Vilon: IL-1β/IL-6/TNF-α suppression; LL-37: NF-κB and TLR signaling with documented anti-inflammatory effects), but through distinct mechanisms and immune arms. The shared tags (innate_immune, anti_inflammatory) are justified by their respective mechanisms, and the explanation accurately captures their non-redundant, complementary positioning—Vilon reactivates adaptive immunity while LL-37 provides frontline innate defense. The caveat about LL-37's context-dependent pro-inflammatory effects is supported by the mechanism description noting 'both anti- and pro-inflammatory' immunomodulation.

    Shares innate immune · anti inflammatory

  • HumaninComplementary

    No documented conflict

    Humanin is a mitochondrial-derived cytoprotective 'mitokine' with anti-inflammatory and IGF-1-related signaling; Vilon is a gene-regulatory geroprotector supporting immune and metabolic function in aged tissue. They target aging through distinct mechanisms (mitochondrial stress signaling vs. chromatin/gene reactivation) that can complement each other in a longevity-oriented approach.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms clearly establish the two claimed shared dimensions: (1) Anti-inflammatory: Vilon suppresses IL-1β/IL-6/TNF-α cytokines in vitro and is tagged anti_inflammatory; Humanin reduces pro-inflammatory cytokines and is tagged anti_inflammatory. (2) IGF1_signaling: Vilon modulates IGF1/FOXO1 gene expression and is tagged IGF1_signaling; Humanin engages IGF-I signaling and is tagged IGF1_signaling. The proposed relationship type (complementary) is justified: the mechanisms describe distinct pathways—Vilon acts via chromatin remodeling and gene reactivation (receptor-independent, DNA-binding), while Humanin acts via cell-surface receptors (FPR2/FPR3, gp130) and intracellular anti-apoptotic targets (Bax, Bid/Bim)—that converge on shared anti-inflammatory and IGF1 outcomes relevant to aging. The explanation accurately reflects both mechanisms' descriptions and their potential synergy in addressing age-related dysfunction.

    Shares anti inflammatory · IGF1 signaling

  • PidotimodSame downstream effect

    Worth caution

    Vilon is a Khavinson-school bioregulator reported to stimulate cellular immunity, improve CD4/CD8 ratio and enhance innate-immune markers — the same immune-enhancing goals as pidotimod but through a proposed gene/chromatin mechanism rather than TLR/dendritic-cell signaling. They overlap heavily on outcome, so combining them is more redundant than synergistic; choose based on evidence quality rather than stacking.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms clearly support the three shared dimensions. Pidotimod targets TLR2/TLR7 and dendritic cells to drive Th1 differentiation, T-lymphocyte proliferation, NK cell activity, and immunoglobulin production (innate_immune, T_cell_regulation, anti_inflammatory via Th1 balance). Vilon's proposed chromatin/gene-expression mechanism similarly produces improved CD4/CD8 ratio, thymus stimulation, cellular immunity enhancement, and IL-1β/IL-6/TNF-α suppression (innate_immune, T_cell_regulation, anti_inflammatory). Both mechanisms converge on downstream immune activation and inflammatory modulation despite different entry points (receptor-mediated vs. gene-regulatory). The 'same_downstream' relationship is justified: they pursue overlapping immunological outcomes through mechanistically distinct pathways, making the redundancy concern valid.

    Shares innate immune · anti inflammatory · T cell regulation

  • ThymulinComplementary

    May be complementary

    Both are thymus-linked immune bioregulators that push the immune system toward balance rather than pure stimulation. Vilon is reported to stimulate thymus tissue growth and improve CD4/CD8 ratios, while thymulin drives T-lymphocyte maturation and normalizes CD4/CD8 balance from the endocrine side. They approach the same immune-normalizing endpoint by different routes, which makes them reasonably complementary for restoring aged/depleted immunity.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    The mechanisms clearly establish both peptides as immune modulators with overlapping functional outcomes. Both target thymic function (Vilon stimulates thymus tissue growth and differentiation; thymulin promotes T-lymphocyte maturation in thymic tissue), both modulate CD4/CD8 ratios (explicitly stated for both), both suppress excessive proinflammatory cytokines (IL-1β, IL-6, TNF-α suppression documented for both), and both engage NF-kB modulation (Vilon via gene expression modulation, thymulin via NF-kB inhibition). The four shared dimensions are directly supported by the provided mechanisms. The 'complementary' relationship type is justified: Vilon acts via receptor-independent chromatin remodeling and gene reactivation, while thymulin acts via cell-surface receptor binding and endocrine signaling—distinct mechanistic routes converging on immune normalization (T-cell balance, cytokine suppression, thymic function). This represents genuine complementarity rather than redundancy.

    Shares innate immune · anti inflammatory · T cell regulation · NF kB modulation

  • ImunofanSame downstream effect

    Worth caution

    Vilon is a Khavinson bioregulator that improves CD4/CD8 ratio, stimulates thymic/immune cell differentiation and suppresses TNF/IL-6, reaching the same immune-normalizing endpoint as imunofan but via a proposed gene/chromatin route rather than thymopoietin receptors. Overlapping goals mean modest additive value at best and heavy redundancy in immune correction.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms clearly establish the three shared dimensions. Imunofan targets thymopoietin receptors and normalizes CD4/CD8 ratios, enhances immune cell differentiation, and modulates TNF/IL-6 downward. Vilon improves CD4/CD8 ratio, stimulates thymic/immune cell differentiation, and suppresses IL-1β/IL-6/TNF-α. Both are tagged innate_immune, anti_inflammatory, and T_cell_regulation. The proposed relationship correctly identifies that despite different upstream mechanisms (receptor-mediated vs. proposed gene/chromatin), both converge on similar downstream immune-normalizing endpoints (CD4/CD8 correction, thymic stimulation, cytokine suppression). The 'same_downstream' classification is justified by the mechanism descriptions showing parallel functional outcomes in immune correction, even though the pathways diverge upstream.

    Shares innate immune · anti inflammatory · T cell regulation

  • LactoferrinComplementary

    No documented conflict

    Lactoferrin adds direct antimicrobial and innate-immune defense plus anti-inflammatory activity, while Vilon works at the gene-expression level to support T-cell/thymic immunity. Different mechanisms both reinforcing host defense, making them a reasonable complementary immune pairing.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms clearly establish the claimed shared dimensions. Vilon demonstrates innate_immune activity through stimulation of cellular immunity, improved innate immune markers, and thymus tissue growth; anti_inflammatory activity through IL-1β/IL-6/TNF-α suppression and cytokine modulation. Lactoferrin demonstrates innate_immune activity through broad-spectrum antimicrobial effects and modulation of cellular immune responses; anti_inflammatory activity through reported anti-inflammatory immunomodulatory effects. The proposed relationship as 'complementary' is well-justified: the mechanisms show Vilon operates via gene-expression/chromatin remodeling to enhance adaptive immunity (T-cell/thymic), while Lactoferrin operates via direct antimicrobial binding and receptor-mediated pathways affecting innate immunity and inflammation. These represent distinct mechanistic approaches (transcriptional vs. direct protein-based) that both target immune/inflammatory pathways, supporting the characterization of complementary action reinforcing host defense.

    Shares innate immune · anti inflammatory

  • ElafinComplementary

    No documented conflict

    Vilon is an immunomodulatory bioregulator that suppresses inflammatory cytokines and normalizes immune ratios, overlapping with elafin's anti-inflammatory NF-κB modulation but acting through different (gene-regulatory) mechanisms.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms establish the three claimed shared dimensions: (1) innate_immune—Elafin inhibits neutrophil serine proteases and modulates immune responses; Vilon stimulates cellular immunity and improves innate immune markers. (2) anti_inflammatory—Elafin is explicitly tagged anti_inflammatory with NF-κB pathway modulation; Vilon suppresses IL-1β/IL-6/TNF-α cytokines in inflammatory models. (3) NF_kB_modulation—Both peptides' mechanisms explicitly reference NF-κB pathway modulation (Elafin: src-17, src-23; Vilon: IGF1/FOXO1/TERT/NFkB gene expression modulation). The explanation correctly identifies that they share these functional dimensions but operate through distinct mechanisms: Elafin via protease inhibition and direct signaling modulation, Vilon via gene-promoter DNA binding and chromatin remodeling. This constitutes a valid complementary relationship—overlapping functional outcomes achieved through mechanistically different pathways.

    Shares innate immune · anti inflammatory · NF kB modulation

  • KlothoComplementary

    No documented conflict

    Both are framed as geroprotective agents that lower inflammatory cytokines and modulate NF-κB, with Vilon additionally influencing IGF1/FOXO/TERT gene expression and Klotho acting as a longevity-associated, anti-senescence protein. They converge on healthy-aging endpoints through largely different mechanisms (chromatin/gene regulation vs. FGF23/antioxidant/anti-fibrotic signaling).

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    Both peptides' mechanisms clearly establish the three claimed shared dimensions: (1) Anti-inflammatory activity is documented for both (Klotho via NF-κB/NLRP3/antioxidant pathways; Vilon via IL-1β/IL-6/TNF-α suppression); (2) NF-κB modulation is explicitly listed in approved tags for both; (3) IGF1_signaling is explicitly approved for both (Klotho via IGF-1/insulin receptor axis; Vilon via IGF1/FOXO1 gene expression modulation). The explanation correctly characterizes them as converging on geroprotective/longevity endpoints through distinct mechanistic pathways—Klotho via FGF23/TGF-β/Wnt/antioxidant signaling, Vilon via chromatin remodeling and gene expression. The 'complementary' relationship type is justified: they share three functional dimensions but operate through largely non-overlapping upstream mechanisms, making them potentially synergistic rather than redundant. No contradictions are present in the mechanism descriptions.

    Shares anti inflammatory · NF kB modulation · IGF1 signaling

  • PinealonSame mechanism

    Worth caution

    Vilon is another ultra-short Khavinson bioregulator that, like Pinealon, is proposed to act without a membrane receptor by binding gene-promoter DNA and remodeling chromatin. They target different systems on paper (Vilon skews immune/geroprotective, Pinealon neuroprotective), but the entire underlying 'peptide binds DNA to reactivate genes' mechanism is shared and rests on modeling/in-vitro claims. Understand that combining them does not give you two independent, well-validated tools — it gives you two peptides resting on the same unproven premise.

    Tier 4Theoretical — not established

    What the research doesn't fully establish

    The mechanisms of both peptides share a core proposed action: receptor-independent, sequence-specific DNA binding to gene-promoter regions followed by chromatin/gene remodeling. Pinealon is described as binding CNG/CAG sequences in the major groove (src-27, src-19, src-2, src-31), while Vilon is proposed to bind GCGC motifs (model-based). Both are credited with modulating gene expression via direct DNA interaction rather than cell-surface receptor engagement. Both show pathway involvement in transcription factor modulation (Pinealon: PPARA/PPARG, src-18; Vilon: IGF1/FOXO1/TERT/NFkB, in vitro). The explanation correctly identifies that despite different downstream phenotypes (neuroprotection vs. immunomodulation), the underlying mechanistic premise—ultra-short peptide binding promoter DNA to alter gene expression—is identical. The caveat that both rest on modeling/in-vitro claims without strong validation is accurate but does not negate the mechanistic similarity. The relationship is 'same_mechanism' because the proposed molecular action (DNA-binding-driven gene reactivation) is shared, even though tissue specificity and downstream effects diverge.

Safety and side effects

Safety Profile

Regulatory status: Vilon is not registered or approved as a pharmaceutical in any country. It is classified as research-use-only or marketed as a dietary supplement and has not been evaluated by the FDA, EMA, or other Western regulatory agencies.

Reported Tolerability

  • In long-term/chronic mouse studies, Vilon caused no unfavourable effects on animal development or estrous function and was associated with increased lifespan, reduced spontaneous tumor incidence, and improved physical parameters.
  • Adverse events were not a documented finding in Khavinson-group studies; the originators describe the entire bioregulator family as producing practically no side effects — a claim resting on a small body of preclinical work from a single Russian research lineage.
  • The most consistent community/anecdotal feedback for subcutaneous bioregulator use is mild, typically short-lived redness, itching, or tenderness at the injection site. Russian clinical literature reports rare local injection-site reactions with no serious adverse events documented at standard doses.
  • The longest published safety study for Vilon spans 12 months in rat models.

Cautions & Interactions

  • Cytostatic drug interaction: Vilon and cytostatic drugs should not be used synchronously. Synchronous injection of Vilon and cyclophosphan at 100 mg/kg decreased mouse survival. (Note that in cell culture, Vilon at 5 ng/ml abolished cyclophosphan's inhibitory effect — the interaction direction is context-dependent.)
  • Active autoimmune disease: Use during an active autoimmune flare is not well-characterized, because Vilon modulates T-cell function and the direction of effect in active autoimmunity is unknown.

Bottom Line

The absence of documented adverse events reflects a small, single-lineage evidence base rather than large, independently replicated safety trials. There are no controlled human safety data and no regulatory review to support clinical use.

Reconstitution and handling

Preparation & Dosing

No dose has been established for this compound. No regulatory label exists for it, so the figures below are what sources report — not guidance.

Important: No validated human dosing protocols exist for Vilon. All research derives from a single research group without independent replication, and Vilon is not an approved pharmaceutical anywhere. The figures below simply report what has been described in the literature and community.

Reported Routes & Doses

  • Historical Russian experimental/clinical work used short intramuscular injection courses; rodent studies used microgram-to-milligram parenteral doses.
  • Russian clinical dosing reported for immunodeficiency and post-infection recovery: 0.5–2 mg intramuscularly for 10 days.
  • Russian retail sublingual/oral dosing: drops or capsules 3–4×/day for 30 days, 3×/year.
  • Reported research/biohacker dosing: 100–200 mcg subcutaneously daily for 10–14 days, repeated 2–3 times per year.

Pharmacokinetic Considerations

  • Vilon's plasma/in vivo half-life is expected to be very short, on the order of minutes (theoretical), while one source reports an elimination half-life of ~1.2 ± 0.4 hours after IV dosing — these estimates conflict and are not reconciled by robust human PK data.
  • Peptides generally have short in vivo half-lives (minutes to hours) owing to protease sensitivity and rapid renal clearance, often prompting frequent dosing.
  • Vilon's very small size (~275 Da dipeptide) is proposed to enable potential oral bioavailability, but oral bioavailability of the intact dipeptide has not been demonstrated in formal pharmacokinetic studies — a key caveat for the sublingual/oral retail forms.

Practical Notes

As a lyophilized research peptide, injectable preparations are typically reconstituted with bacteriostatic or sterile water; however, no standardized, validated reconstitution or dosing protocol has been published. Given the single-source evidence base and lack of regulatory oversight, any use falls outside established clinical guidance.

Sources

Ordered by evidence quality — the strongest first.

  1. A biomimetic approach for enhancing the in vivo half-life of peptides - PMC(opens in a new tab)
    Tier 2Web · pmc.ncbi.nlm.nih.gov
  2. A synthetic dipeptide vilon (L-Lys-L-Glu) inhibits growth of spontaneous ...(opens in a new tab)
    Tier 2Web · pubmed.ncbi.nlm.nih.gov
  3. Safety and Efficacy of Peptide-Based Therapeutics in Health Sciences(opens in a new tab)
    Tier 2Web · biomedgrid.com
  4. Vilon Side Effects: What to Know Before Starting Treatment(opens in a new tab)
    Tier 2Web · mypeptidematch.com
  5. Vilon: Complete Overview and Research Guide | Peptide Protocol Wiki(opens in a new tab)
    Tier 2Web · peptideprotocolwiki.com
  6. Vilon: Mechanism, Status, Dose Reference & Half-Life | PeptideStat(opens in a new tab)
    Tier 2Web · peptidestat.com
  7. EPIGENETIC MODIFICATION UNDER THE INFLUENCE OF PEPTIDE BIOREGULATORS ON THE "OLD" CHROMATIN.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2023
  8. 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.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2023
  9. Peptide KE in Human Proteome.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2020
  10. Anti-aging peptide bioregulators induce reactivation of chromatin.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2006
  11. [The effect of vilon (Lys-Glu) on 1.2-dimethylhydrazine-induced neoplasia].(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2005
  12. Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2004
  13. [Combined effect of vilon and cyclophosphane on tumor transplants and lymphoid tissue explants in mice and rats of various age].(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2003
  14. Effect of Vilon and Epithalon on glucose and glycine absorption in various regions of small intestine in aged rats.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2002
  15. Studies of the effects of Vilon and Epithalon on gene expression in mouse heart using DNA-microarray technology.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2002
  16. Inhibitory effect of peptide vilon on the development of induced rat urinary bladder tumors in rats.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2001
  17. Tissue-specific effects of peptides.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2001
  18. Effect of vilon on biological age and lifespan in mice.(opens in a new tab)
    Tier 2PubMed · pubmed.ncbi.nlm.nih.gov · 2000
  19. Healthtimes - 🧬 Vilon Peptide: The Minimalist Bioregulator...(opens in a new tab)
    Tier 3Web · facebook.com
  20. Vilon Peptide Research: Complete Guide | Cenexa Labs(opens in a new tab)
    Tier 3Web · cenexalabs.com
  21. Vilon Side Effects: What the Evidence Shows (2026)(opens in a new tab)
    Tier 3Web · thepeptidecatalog.com · 2026
  22. Vilon: KE Immune Bioregulator Guide 2026(opens in a new tab)
    Tier 3Web · thepeptidetoolkit.com · 2026
  23. Vilon Peptide Research: Complete Guide(opens in a new tab)
    Tier 3Web · cenexalabs.com · 2026
  24. Vilon: Research Evidence & Safety Profile | PeptideInsight(opens in a new tab)
    Tier 3Web · peptideinsight.com · 2026
  25. Long Live Peptides - Evolution of peptide half-life extension technologies and emerging hybrid approaches - Drug Discovery World (DDW)(opens in a new tab)
    Tier 4Web · ddw-online.com
  26. Long-Acting, Longer-Acting and Ultralong-Acting Peptides(opens in a new tab)
    Tier 4Web · preprints.org
  27. Peptide Half-Life Chart: Quick Reference | PeptideJournal(opens in a new tab)
    Tier 4Web · peptidejournal.org
  28. Vilon: Research, Evidence, Dosing & Safety | Peptidings(opens in a new tab)
    Tier 4Web · peptidings.com · 2026
  29. Catalytic Assembly of Peptides Mediated by Complex Coacervates.(opens in a new tab)
    Tier 4PubMed · pubmed.ncbi.nlm.nih.gov · 2025
  30. ViLoN-a multi-layer network approach to data integration demonstrated for patient stratification.(opens in a new tab)
    Tier 4PubMed · pubmed.ncbi.nlm.nih.gov · 2023