Vilon peptide (Lys-Glu): what the published papers say

What is Vilon, and how firmly is the name pinned?

Two amino acids, and four documents that agree on which two: PubChem resolves both "vilon" and "Lys-Glu" to CID 7010502, formula C₁₁H₂₁N₃O₅, IUPAC name (2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]pentanedioic acid. FDA's substance registry files VILON as a name on the record for LYSYLGLUTAMIC ACID, UNII H34V7IM5ML, CAS 45234-02-4.

The library catalog says the same: the NLM supplementary concept record for lysylglutamic acid lists Vilon, Lys-Glu, H-Lys(H-Glu-OH)-OH, AB-0 peptide and AB-17 as entry terms, with a scope note of one line, a geroprotective agent.

And the papers spell it out in their own text: the 2023 Georgian Medical News study writes the four sequences it tested as Ala-Glu-Asp-Gly for Epitalon, Lys-Glu-Asp-Ala for Livagen, Ala-Glu-Asp-Pro for Cortagen and Lys-Glu for Vilon, and the 2022 monocyte study names its second preparation as Vilon, Lys-Glu, a synthetic immunomodulatory dipeptide.

Why that is worth four documents: a two-residue molecule is cheap to make and easy to confuse with something else that also contains lysine and glutamic acid, and a chromatogram does not settle identity on its own. That gap between purity and identity is what a purity number leaves open, and it is why a certificate reports identity and purity as separate tests.

Where Vilon comes out the odd one among the peptides tested beside it

The unusual thing about this compound is not its own literature, it is the company it keeps: Vilon keeps being run as a comparator, under the same conditions and on the same day as its siblings. Six of the seven records below put it next to at least one other Khavinson peptide, and in most of them it is the one that goes a different way.

Read from another compound's page, these sentences invert: the same experiments that report a Vilon negative report an Epitalon or a Livagen positive, which is what makes this section belong to Vilon rather than to the family.

The chromatin negative, stated three times by one group

The cleanest version is the 2006 sentence: Epitalon and Livagen induce deheterochromatinization of pericentromeric structural heterochromatin of chromosomes 1 and 9, however vilon does not. The 2004 Vilon-only paper reaches the same place from the other direction, listing what Vilon did and then that it does not induce decondensation of that same structural fraction.

What that is and is not: it is a repeated, specific, negative result about one compound in one assay family, from one laboratory in Tbilisi, on cultured cells taken from donors aged 75 to 88. Nobody in these papers was given anything; the cells were.

The 2023 paper says something narrower than a Vilon-specific split: it ran Epitalon, Livagen, Cortagen and Vilon together, and its summary sentence applies the pericentromeric negative to the whole set rather than to Vilon alone, while adding that each bioregulator has a selective effect on definite regions of chromosomes. So the most recent paper in the series widens the negative instead of confirming a Vilon-specific split, and this page reports it that way.

The monocyte experiment, and the half of it that gets dropped

The quotable line is real: in a 2022 open-access paper, all the peptides except Vilon increased the phosphorylated level of ERK1/2, and Vilon showed a small modulatory capacity. Four preparations did the thing and the dipeptide did not.

The same figure says more than that: when lipopolysaccharide was added, an additive effect on ERK1/2 phosphorylation appeared only with Epitalon and Vilon, and Vilon sat with Epitalon and Chonluten among the three that activated STAT1 phosphorylation. A summary of this paper that reads "Vilon did nothing" is not a summary of this paper.

The clamp that has to travel with it: this is an immortalized human leukemia cell line in a dish, treated directly. It is not a dose, a person, or an outcome.

The fibroblast comparison, where the split runs the other way

Two peptides, one culture, different results: in human skin fibroblasts taken through replicative aging, KE reduced synthesis of IL-1, NF-κB and TGF-β and stimulated sirtuin-6, while AED activated sirtuin-1, sirtuin-6 and collagen I. The authors read KE as normalizing an immunological function and AED as the one showing a geroprotective effect.

Why it belongs here: this is the one retrieved head-to-head where Vilon is credited with something its sibling is not, and it is still a culture dish rather than skin on a person.

The fragile end of the family

Shortest is not sturdiest: in the hydrolysis work the 2022 transport review reports, the four-residue KEDW and KEDA held out against aminopeptidase cleavage for 3 to 4 hours across saline, Ringer's solution, hydrochloric acid and tissue homogenates, while KE was broken down in solution and partly in tissue, to a greater extent than the tetrapeptide AEDG.

The docking table points the same way: the review sets a score below -15.00 as the mark of a high probability of efficient LAT1 binding, says 20 of its 27 peptides clear it, and puts Vilon at -12.31 among the seven that do not, with only three rows scoring lower. Epitalon clears the cut at -20.38.

One caveat on that number, from reading the paper rather than its abstract: the sentence introducing that table names a different protein target than the table's own caption does, although its count of 27 peptides matches the table exactly, so it reads as a slip in the text rather than a different experiment. It is flagged here because a docking score is a prediction either way.

The origin story no sibling shares

Most of this family is named after an organ: Thymalin was acid-extracted from calf thymus, Glu-Trp was isolated out of Thymalin by reversed-phase HPLC and became Thymogen, and Epitalon and Chonluten trace to pineal and lung tissue in the same literature.

Vilon arrives differently: the 1997 paper describes it as a novel immunomodulatory dipeptide that was synthesized and then named, which is why the Russian literature calls it thymomimetic rather than thymic. It is the family member described in a primary source as designed.

What human evidence exists for Vilon?

Three papers, and the number is reproducible rather than asserted. On 4 August 2026 the PubMed query vilon[Title/Abstract] AND (clinical trial[pt] OR randomized controlled trial[pt] OR controlled clinical trial[pt]) returned exactly three records: PMID 17152731, PMID 18306698 and PMID 16075684.

The one tagged as randomized: a 2006 paper in Advances in Gerontology on type 1 diabetes, which names the compound in its abstract as thymomimetic Vilon (Lys-Glu) and reports that giving it significantly reduced or even totally diminished the markers of disseminated intravascular coagulation, with a less pronounced effect in elderly patients with severe disease.

The 2007 companion: in elderly patients with type I diabetes it reports raised antithrombin III and protein C, stimulated fibrinolysis, and, for most of the patients treated, a reduction in the insulin needed to stabilize carbohydrate metabolism, alongside changes in T-helper, natural-killer and B-lymphocyte counts.

The 2005 oncology paper hedges itself: it describes adding Vilon to radical treatment of stage III rectal and colon cancer in elderly patients, and its own abstract calls the work pioneer experience and preliminary results that suggest a recommendation, which is a long way from a demonstrated survival benefit. This page repeats the hedge rather than the implied number.

What none of the three gives up: a sample size, an amount, a route, a duration or a blinding method. All three are Russian-language, all three are in Advances in Gerontology, and none carries a DOI, so the PubMed identifier is the locator a reader has.

Why three still counts for something: the same publication-type filter run across sixteen synthetic short-peptide sibling names on 4 August 2026 returns nothing at all for twelve of them, and inside that set Vilon's three sits behind only Thymogen's five. Thymalin sits outside the sixteen and returns twelve, more than any name in it, and it is named here rather than left out quietly: it is the acid-extracted natural preparation the 1997 paper starts from rather than a synthesized short peptide, which is why it is counted apart. The sixteen names are listed in the sourcing note. It is also a different order of evidence from a compound that reached a label, which is the contrast worth holding: an approved peptide arrives with a prescribing document that prints its amounts and its population, and Vilon arrives with three abstracts.

What did the mice and the cell studies actually show?

The lifespan result is a mouse result: in female CBA mice given Vilon under the skin from the sixth month of life, the 2000 report describes increased physical activity and endurance, lowered body temperature, prolonged lifespan and prevention of spontaneous tumor development, with no effect on age-related changes in estrous function or free-radical processes.

That sentence does not survive translation into a person: the strain is inbred, the exposure started in young adulthood and ran for life, and nothing equivalent has been published in humans in anything we retrieved.

The most recent mechanistic figures are cell-culture figures: a 2023 Russian-language paper on human mesenchymal stem cells reports that KE raised SIRT1 gene expression and protein synthesis in young cells by 6 and 8.2 times, and during aging of those cells lowered PARP1 expression and protein by 2.1 and 5.3 times and PARP2 by 2.1 and 4.7 times.

The setting is the qualifier: cultured human cells exposed directly in a dish, with a molecular-modeling section attached, published in the same journal family as most of the rest of this record.

Is Vilon approved anywhere?

Not in any drug register we were able to read, and there is a trap in the way the records display. FDA's substance registration system returns a valid record for UNII H34V7IM5ML with a status field reading approved, and that field describes the state of the substance record itself, not a marketing authorization for a product.

Nothing hangs off that identifier: the record carries no product entry, and the openFDA label endpoint returns no match for either vilon or lysylglutamic while the same endpoint returns eighteen labels for a control term on the same day.

A second identifier exists on the EU side: the dihydrate carries its own UNII, 832IRM2G6W, with an EudraVigilance substance code and a World Health Organization drug-dictionary name tag. A substance dictionary entry records that a molecule has been named and coded, which is a different act from a regulator approving a medicine.

On Russia, the honest answer is that we do not know: the Russian State Register of Medicines serves its search results behind a CAPTCHA, which this project does not complete, so we retrieved neither a registration record nor evidence that none exists. Every web source we found asserting a Russian status was a seller, and this site does not cite sellers, so the question stays open on the page instead of being settled by a shop.

How long does Vilon last in the body?

No document we retrieved answers that. There is no human pharmacokinetic study, no bioavailability figure, no half-life and no dose-response curve anywhere in the records read for this page, so the question of how long it persists has no published answer to give.

What exists instead is a tube: the stability data is enzymatic hydrolysis in saline, buffer, acid and tissue homogenate, plus an in silico transporter docking score. Both describe how the molecule behaves in an assay, not how long it persists in a person.

The gap matters more for a dipeptide than for a longer chain: two residues is the shortest thing in this family, and in the hydrolysis comparison it was the one broken down most, so the absence of human data sits on top of the molecule that work found least resistant to cleavage.

What is documented is the container, not the compound: material of this kind ships as a freeze-dried solid, and the drying process and what sets a dry vial's shelf life are both described in regulator documents, which is more than can be said for what happens after an injection.

How big is the published record on Vilon?

The indexing term is not a species clamp: the Humans tag is applied to any record using human-derived material, so cultured donor lymphocytes and an immortalized cell line both pick it up. That is exactly why the middle number is twenty and the right-hand number is three.

One more thing the count hides: adding AND Khavinson[Author] to the first query on the same day returns thirty-nine of the sixty-two, so most of this literature carries one name, and the record count overstates how many separate groups have looked at this compound.

What is still unsettled?

Five open items, each named here rather than smoothed over:

• Whether normophthal is the same substance. The NLM record lists normophthal as an entry term for lysylglutamic acid, which makes it a Vilon synonym. The 2022 transport review's own table lists Vilon (KE) and Normoftal (H-Lys(H-Glu-OH)-OH) as separate rows, with different scores and different functional labels. Those two documents disagree and we are not going to pick a winner.
• What was given in the three human trials. No amount, route, schedule or sample size appears in any of the three abstracts, and full text was not obtained for any of them.
• Human pharmacokinetics. Absent from everything retrieved, which leaves duration of action, bioavailability and clearance all unanswered.
• Russian registration status. The state register is CAPTCHA-gated, so it was not checked, and an unchecked register is not an empty one.
• How independent the replication is. The 2022 monocyte paper is Italian-led, English-language and open access, which makes it the most externally checkable record here, but Khavinson is among its authors, so it is not an independent replication of his group's work.

One paper was deliberately left out and it is worth naming: a 2013 Bulletin of Experimental Biology and Medicine study of immunomodulating effects identifies its test articles only by the codes AB-O and R-1, and never states which of them is Vilon. The library catalog lists AB-0 peptide as a Vilon synonym, which makes the identification probable and still an inference, so the paper is not cited here.

How this page is sourced

Everything below was opened, not summarized from somewhere else: the PubMed record and English abstract for every paper cited here, pulled from the E-utilities interface on 4 August 2026, plus the full text of the two open-access papers from Europe PMC, plus the registry and database endpoints listed below, each run with a control query or a paired lookup on the same day.

A retrieval note that will save the next reader ten minutes: the human-facing PubMed pages can return an interstitial page to an automated client, so an identifier that looks broken to a script is often fine in a browser. The abstracts quoted here came from the structured interface, and the links below are for a person.

The trap in this compound's own result set: a genuine 2023 Nucleic Acids Research paper describes a data-integration method called ViLoN, which has nothing to do with the peptide and sits inside the raw search results for the name. It is listed at the bottom as an exclusion so that no later pass mistakes a high-profile item in the raw results for a relevant one.

Nineteen sources, eighteen of them load-bearing: thirteen journal papers, one chemical database record, one library catalog record, one substance registry, one label and trial-registry search entry, and one literature-count entry, plus the excluded paper described above. Every figure printed above is meant to be checkable against the document it came from.

What we could not settle: the Russian register, the normophthal identity question, and any amount used in the three human trials. Each one is named in its own section rather than smoothed over, and the rules behind that choice are on the methodology page.

Last reviewed: 4 August 2026.

1. 1

   Avolio F, Martinotti S, Khavinson VK, et al. Peptides regulating proliferative activity and inflammatory pathways in the monocyte/macrophage THP-1 cell line. Int J Mol Sci. 2022;23(7):3607. Full text retrieved from Europe PMC on 4 August 2026, HTTP 200; source for the phospho-ERK1/2 finding, the lipopolysaccharide additive effect, the STAT1 finding and the Materials and Methods identification of Vilon as Lys-Glu. doi:10.3390/ijms23073607. PMID 35408963.

2. 2

   Khavinson V, Linkova N, Kozhevnikova E, et al. Transport of biologically active ultrashort peptides using POT and LAT carriers. Int J Mol Sci. 2022;23(14):7733. Full text retrieved from Europe PMC on 4 August 2026, HTTP 200; source for the aminopeptidase hydrolysis comparison it cites and for the LAT1 docking table, whose caption reads "Binding of ultrashort peptides to LAT1" while the paragraph describing it names a different target. doi:10.3390/ijms23147733. PMID 35887081.

3. 3

   Khavinson VKh, Lezhava TA, Malinin VV. Effects of short peptides on lymphocyte chromatin in senile subjects. Bull Exp Biol Med. 2004;137(1):78-81. Source for the five-peptide comparison in leukocytes of subjects aged 75 to 88 and for which peptides decondensed chromosome 1 and chromosome 9 pericentromeric chromatin. doi:10.1023/b:bebm.0000024393.40560.05. PMID 15085253.

4. 4

   Lezhava T, Khavison V, Monaselidze J, et al. Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people. Biogerontology. 2004;5(2):73-79. The Vilon-only paper, and the source for the statement that it does not induce decondensation of pericentromeric structural heterochromatin. doi:10.1023/B:BGEN.0000025070.90330.7f. PMID 15105581.

5. 5

   Lezhava T, Monaselidze J, Kadotani T, Dvalishvili N, Buadze T. Anti-aging peptide bioregulators induce reactivation of chromatin. Georgian Med News. 2006;(133):111-115. No DOI exists for this record, so the PubMed identifier is the locator. Source for the plainest form of the negative, that epitalon and livagen induce deheterochromatinization of pericentromeric structural heterochromatin of chromosomes 1 and 9 however vilon does not. PMID 16705247.

6. 6

   Lezhava T, Jokhadze T, Monaselidze J, et al. Epigenetic modification under the influence of peptide bioregulators on the "old" chromatin. Georgian Med News. 2023;(335):79-83. No DOI. Source for the four sequences as printed, for the donor age band, for the selective-effect statement, and for the 2023 summary sentence that applies the pericentromeric negative to the whole set. PMID 37042594.

7. 7

   Fridman NV, Linkova NS, Kozhevnikova EO, Gutop EO, Khavinson VK. Comparison of the effects of KE and AED peptides on functional activity of human skin fibroblasts during their replicative aging. Bull Exp Biol Med. 2020;170(1):154-157. Source for the KE against AED split on IL-1, NF-κB, TGF-β, sirtuin-1, sirtuin-6 and collagen I. doi:10.1007/s10517-020-05022-1. PMID 33231794.

8. 8

   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. Adv Gerontol. 2006;19:107-115. The spelling fibrinolisis is the record's own and is reproduced rather than corrected, so the title still matches an exact search. Russian-language, English abstract only, no DOI. PubMed publication type Randomized Controlled Trial. The abstract reports no sample size, amount, route or blinding method. PMID 17152731.

9. 9

   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. Adv Gerontol. 2007;20(2):106-115. Russian-language, English abstract only, no DOI. PubMed publication type Clinical Trial. PMID 18306698.

10. 10

    Ias'kevich LS, Krutilina NI, Kostetskaia TV, et al. Application of peptide bioregulator in complex treatment of elderly cancer patients. Adv Gerontol. 2005;16:97-100. Russian-language, English abstract only, no DOI. PubMed publication types Clinical Trial and Controlled Clinical Trial. The abstract itself uses the words pioneer experience and preliminary results, which is the wording quoted on this page. PMID 16075684.

11. 11

    Morozov VG, Khavinson VK. Natural and synthetic thymic peptides as therapeutics for immune dysfunction. Int J Immunopharmacol. 1997;19(9-10):501-505. Source for the extraction chain from calf thymus to Thymalin to Thymogen, and for the sentence that a novel immunomodulatory dipeptide was synthesized and termed Vilon. doi:10.1016/s0192-0561(97)00058-1. PMID 9637345.

12. 12

    Khavinson VK, Anisimov VN, Zavarzina NY, et al. Effect of vilon on biological age and lifespan in mice. Bull Exp Biol Med. 2000;130(7):687-690. Animal study, female CBA mice, subcutaneous, from the sixth month of life. Source for the activity, endurance, body temperature, lifespan and spontaneous-tumor findings and for the absence of an effect on estrous function and free-radical processes. doi:10.1007/BF02682106. PMID 11140587.

13. 13

    Khavinson VK, Linkova NS, Ashapkin VV, et al. KE peptide regulates SIRT1, PARP1, PARP2 gene expression and protein synthesis in human mesenchymal stem cells aging. Adv Gerontol. 2023;36(3):302-312. Russian-language with a bilingual abstract, no DOI. In vitro, human mesenchymal stem cell culture. Source for the SIRT1, PARP1 and PARP2 fold figures and for the opening identification of the KE peptide as Lys-Glu, vilon. PMID 37782636.

14. 14

    PubChem compound record CID 7010502. Queried through the PUG REST interface twice on 4 August 2026, once by the name vilon and once by the name Lys-Glu, both resolving to the same record, HTTP 200. Source for the molecular formula, the molecular weight and the IUPAC name. pubchem.ncbi.nlm.nih.gov, CID 7010502.

15. 15

    U.S. National Library of Medicine. Medical Subject Headings supplementary concept record, lysylglutamic acid. Source for the entry terms Vilon, Lys-Glu, H-Lys(H-Glu-OH)-OH, AB-0 peptide, AB-17 and normophthal, and for the scope note describing a geroprotective agent. Retrieved 4 August 2026. ncbi.nlm.nih.gov, MeSH record.

16. 16

    U.S. Food and Drug Administration Global Substance Registration System, substance record LYSYLGLUTAMIC ACID, UNII H34V7IM5ML, CAS 45234-02-4, retrieved 4 August 2026, HTTP 200, with the names list carrying VILON, a status field reading approved that describes the substance record, and no product entry attached. The second identifier for the dihydrate, UNII 832IRM2G6W with EudraVigilance code SUB25762, was read from the openFDA substance endpoint at api.fda.gov, other/substance. gsrs.ncats.nih.gov, UNII H34V7IM5ML.

17. 17

    Label and trial-registry searches, all run 4 August 2026 with controls. openFDA drug/label search=vilon and search=lysylglutamic returned NOT_FOUND, against search=semaglutide returning 18. DailyMed v2 spls.json drug_name=vilon returned 0 elements, against semaglutide returning 9. api.fda.gov, drug/label. dailymed.nlm.nih.gov, SPL search. ClinicalTrials.gov v2 query.intr=vilon returned 0 studies, against query.term=retatrutide returning 34. clinicaltrials.gov, API v2.

18. 18

    Literature counts, PubMed E-utilities esearch, run 4 August 2026. vilon[Title/Abstract] returned 62; the same query with AND humans[MeSH] returned 20; the same query filtered to clinical trial, randomized controlled trial or controlled clinical trial publication types returned 3, being PMID 17152731, PMID 18306698 and PMID 16075684. A nonsense control term returned 0 on the same run, which is what makes a zero here a real zero. Two further queries on the same day: the same publication-type filter applied to sixteen synthetic short-peptide sibling names, being epitalon, livagen, cortagen, pinealon, prostamax, chonluten, cardiogen, vesugen, cartalax, bronchogen, testagen, pancragen, crystagen, normoftal, ovagen and thymogen, which returned 0 for twelve of them, 1 each for epitalon, pinealon and ovagen, and 5 for thymogen; and vilon[Title/Abstract] AND Khavinson[Author], which returned 39. Thymalin was run through the same filter on the same day and returned 12. It is reported apart from the sixteen, not inside them, because it is an acid-extracted natural peptide preparation rather than a synthesized short peptide, and the count is printed here so the exclusion is visible rather than assumed. eutils.ncbi.nlm.nih.gov, esearch.

19. 19

    Excluded, and recorded so it is not added back. Kańduła MM, Aldoshin AD, Singh S, et al. ViLoN-a multi-layer network approach to data integration demonstrated for patient stratification. Nucleic Acids Res. 2023;51(1):e6. The hyphen after the acronym is the record's own punctuation and is reproduced rather than smoothed, so the title still matches an exact search. A real paper in a real journal, describing a bioinformatics method whose acronym collides with this compound's name, and unrelated to the peptide. It appears in the raw search results for vilon and supports nothing on this page. doi:10.1093/nar/gkac988. PMID 36395816.

Related pages

Around this page: four neighbors on identity, paperwork and what an approved record looks like when one exists.

• What a purity number leaves open: why a high percentage says nothing about which molecule is in the vial.
• How to read a certificate of analysis: where identity, purity and peptide content sit, and what each one measures.
• A compound that did reach a label: the same questions asked of a peptide with an approved prescribing document behind it.
• KPV, another short immunomodulatory peptide: a thin human record read the same way, one paper at a time.

The compound series: each new reference page in this run goes out first in The Decadewise briefing.