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Research Guide

Vilon Peptide (Lys-Glu)
Research Guide

A Research Use Only reference to the Vilon peptide: identity data, what published studies examined, handling and storage for laboratories.

Research reference · Updated October 12, 2026 · How we check our guides

What is vilon?

Vilon is the synthetic dipeptide Lys-Glu (L-lysyl-L-glutamic acid, also written KE) (Khavinson et al., 2000). It comes from the thymus program of V. Kh. Khavinson, V. G. Morozov and colleagues at the Saint Petersburg Institute of Bioregulation and Gerontology, which made the calf thymus extract thymalin, isolated the dipeptide Glu-Trp from it, which in synthetic form became thymogen, and synthesized a new immunomodulatory dipeptide that it named vilon (Morozov and Khavinson, 1997). A 2023 paper from the institute describes KE and EW as active components of thymalin (Linkova et al., 2023).

About 60 PubMed records name vilon in the title or abstract, from 1997 to 2023; roughly two thirds list Khavinson as an author, about half are in Russian, and three quarters date from before 2010. Most of the work is in cells, organ explants and rodents, and one transgenic mouse study reported more mammary tumors with vilon, not fewer.

Vilon is not an approved drug in the United States (Drugs@FDA, via openFDA, October 2026). Disguised Alpha does not currently list vilon on its own; it appears in the catalog only as one component of a blend. This page is a literature reference for laboratory researchers. Nothing on this page is guidance for use in people.

Vilon reference data

PropertyValue
NameVilon
Also calledLys-Glu, KE, KE dipeptide, L-lysyl-L-glutamic acid, lysylglutamic acid
SequenceLys-Glu (KE), written H-Lys-Glu-OH: L-lysine linked to L-glutamic acid by one peptide bond, with free amino and carboxyl ends
Compound classSynthetic dipeptide; a thymus-series "peptide bioregulator" in its developers' terms
Molecular formulaC₁₁H₂₁N₃O₅
Molecular weight275.30 g/mol
PubChem CID7010502

All values are from PubChem CID 7010502 (lysylglutamic acid), which lists vilon, Lys-Glu and KE dipeptide among its names. Its IUPAC name, (2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]pentanedioic acid, matches the Lys-then-Glu order in the primary papers (Anisimov et al., 2001).

What the research covers

This page summarizes five areas of the published work on vilon. Each summary names the model, and nearly every study involves the originating institute or its partners.

Thymus explants and thymocytes

In the group's organotypic cultures, vilon stimulated the growth of rat thymus explants (Khavinson, 2001), although an earlier paper from the group found the direction depended on age: stimulation in thymus and spleen explants from 21-day-old rats, inhibition in thymus explants from 1-day-old rats (Chalisova et al., 1999). In mouse thymocytes, it had the strongest comitogenic effect of three peptides tested, ahead of epitalon, while cortagen had none, and it raised sphingomyelinase activity in thymocyte membranes more than the other two (Khavinson et al., 2002). Models: rat explants and mouse thymocytes.

Inflammation markers in human cells

An Italian university group, with Khavinson as a co-author, tested five of these peptides, vilon and thymogen included, in the human THP-1 monocytic cell line. In the paper's results, vilon was the one peptide that did not raise ERK1/2 phosphorylation on its own, though it added to the effect of bacterial lipopolysaccharide, and all five lowered TNF and IL-6 expression in differentiated cells stimulated with lipopolysaccharide (Avolio et al., 2022).

In LPS-stimulated blood mononuclear cells from four donors, KE at 1 mg/mL lowered TNF-α output about 6 times and IL-6 about 2.5 times but did not significantly change IL-1β, which only thymalin lowered, and docking proposed that KE prefers the sequence GCGC in nucleosomal DNA (Linkova et al., 2023). Models: a human leukemia cell line and donor blood cells.

Chromatin in cells from older donors

In cultured lymphocytes from people aged 75 to 88, vilon was one of five short peptides that activated ribosomal genes and decondensed tightly packed chromatin (Khavinson et al., 2004). A Tbilisi State University genetics group, with Khavinson as a co-author, reported that it unrolled heterochromatin and reactivated nucleolus organizer regions but did not decondense the structural heterochromatin around centromeres (Lezhava et al., 2004). These are chromosome-structure readouts, not measures of immune function. Model: human lymphocyte cultures.

Lifespan and spontaneous tumors in mice

Two of the group's reports followed female CBA mice given vilon from 6 months of age. A 2000 short report said it raised physical activity and endurance, prolonged lifespan and prevented spontaneous tumors (Khavinson et al., 2000). The fuller 2001 paper compared Lys-Glu, the pineal tetrapeptide Ala-Glu-Asp-Gly and saline, given on five consecutive days each month until natural death. It reported higher physical activity and fewer spontaneous lung adenomas with Lys-Glu, but its abstract reports a significant survival gain only for the tetrapeptide (Anisimov et al., 2001). Model: female CBA mice.

Induced and transgenic tumor models

These findings point in opposite directions. In rats given the bladder carcinogen N-butyl-N-(4-hydroxybutyl)nitrosamine, tumors developed in 56 percent of vilon-treated animals and 75.5 percent of controls, and the incidence of preneoplastic and early neoplastic changes in the bladder lining was halved (Pliss et al., 2001).

In female HER-2/neu transgenic mice, which develop mammary tumors on their own, vilon given on five consecutive days each month from 2 months of age had significant negative effects against saline controls: a higher incidence of mammary cancer, a shorter mean latent period of tumors and a higher cumulative number of tumors. Epitalon, tested alongside, reduced the cumulative number and maximum size of tumors (Anisimov et al., 2002). Both studies came from the N. N. Petrov Institute of Oncology, with Khavinson as a co-author. Models: rats and transgenic mice.

Key studies

  1. Anisimov VN, et al. "Effect of synthetic thymic and pineal peptides on biomarkers of ageing, survival and spontaneous tumour incidence in female CBA mice." Mech Ageing Dev. 2001. PMID 11163623. DOI 10.1016/s0047-6374(00)00184-6. Female CBA mice followed until natural death.
  2. Pliss GB, et al. "Inhibitory effect of peptide vilon on the development of induced rat urinary bladder tumors in rats." Bull Exp Biol Med. 2001. PMID 11586406. DOI 10.1023/a:1012354603132. Rat chemical carcinogenesis model.
  3. Anisimov VN, et al. "Inhibitory effect of the peptide epitalon on the development of spontaneous mammary tumors in HER-2/neu transgenic mice." Int J Cancer. 2002. PMID 12209581. DOI 10.1002/ijc.10570. Transgenic mice; negative effects reported for vilon.
  4. Lezhava T, 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. Human lymphocyte cultures.
  5. Avolio F, et al. "Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line." Int J Mol Sci. 2022. PMID 35408963. DOI 10.3390/ijms23073607. Human THP-1 cells.

Handling and storage of lyophilized vilon

General laboratory practice for a lyophilized dipeptide, in line with the site's peptide storage guide and reconstitution guide:

  • Keep the sealed powder at -20°C, dry and dark; let a cold vial reach room temperature before opening.
  • Lys-Glu has a basic and an acidic side chain, both charged at neutral pH, so sterile water is the usual first diluent, with any salt or buffer added after the peptide dissolves, as the reconstitution guide describes. Test a small portion and record the pH.
  • Reported cell-culture concentrations vary widely, from 100 ng/mL in THP-1 cells (Avolio et al., 2022) to 1 mg/mL in blood mononuclear cells (Linkova et al., 2023). Make fresh serial dilutions from measured content, not label mass.
  • Check whether a certificate reports the free peptide (275.30 g/mol) or a salt before calculating molarity.
  • Store solutions at 2 to 8°C in single-use aliquots; avoid repeated freeze and thaw cycles.

Frequently asked questions

What is vilon?

The synthetic dipeptide Lys-Glu, introduced by the Saint Petersburg group as an immunomodulator from its thymus program (Morozov and Khavinson, 1997) and studied in explants, immune cells, lymphocyte chromatin and rodent tumor models.

Is the vilon peptide the same as the Lys-Glu dipeptide?

Yes. Vilon is the developers' name for L-lysyl-L-glutamic acid, and PubChem files vilon, Lys-Glu and KE dipeptide under CID 7010502. "Lys-Glu" alone also pulls up unrelated protein chemistry, where it names two neighboring residues in a larger protein, so pair it with vilon or KE.

How does vilon relate to thymalin and thymogen?

They come from the same thymus program. Thymalin is a calf thymus polypeptide extract, and thymogen is based on the Glu-Trp dipeptide isolated from it and then synthesized (Morozov and Khavinson, 1997); the group later described KE and EW as active components of thymalin (Linkova et al., 2023). See our thymalin research guide.

How strong is the evidence on vilon?

Thin: mostly one group and its partners, often in Russian, and mostly cell, explant and rodent work. The tumor findings conflict: fewer induced bladder tumors in rats (Pliss et al., 2001), but more mammary tumors in HER-2/neu transgenic mice (Anisimov et al., 2002).

Has vilon been tested in people?

Only in a few clinical reports from the group's network, mostly in Russian. In one, which PubMed indexes as a randomized trial, a Chita group reported that standard care alone did little to signs of chronic intravascular coagulation in people with type 1 diabetes, while adding vilon reduced them, less so in older people with severe disease (Kuznik et al., 2006). The abstract gives no group sizes or blinding. No vilon trial is registered on ClinicalTrials.gov.

Does Disguised Alpha sell vilon?

Not as a standalone peptide. Vilon appears in the catalog only as one component of a blend. Related bioregulators listed on their own include Thymalin, Vesugen (Lys-Glu-Asp) and Epitalon.

Related compounds and guides

Literature reference for laboratory research only.