Overview
Vilon is a synthetic dipeptide composed of lysine and glutamic acid (Lys-Glu, commonly abbreviated KE). It is the shortest of the Khavinson "bioregulator" peptides, a family of di-, tri- and tetrapeptides originally isolated from animal tissue extracts at the St Petersburg Institute of Bioregulation and Gerontology from the 1970s onward and later reproduced by synthesis.
The published research programme treats Vilon as an epigenetic signalling molecule rather than a receptor ligand. Fluorescence-labelling work reported that short peptides of this class enter the cytoplasm, nucleus and nucleolus of cultured human cells and bind sequence-selectively to deoxyribooligonucleotides and DNA, discriminating between nucleotide sequences and even between cytosine methylation states. In aged-donor lymphocytes, Vilon has been reported to decondense heterochromatin and reactivate ribosomal genes silenced by age-related chromatin condensation.
In immune tissue, Vilon has been reported to activate T-helper cells in ageing spleen, an effect attributed to reduced apoptosis rather than increased proliferation, and to reduce LPS-stimulated TNF and IL-6 expression in differentiated THP-1 monocytes.
Nearly all of this evidence is in vitro or ex vivo, and nearly all of it comes from one research network. There are no controlled clinical trials establishing any health outcome in humans.
What the evidence shows
Separated by study type- HumanClinical trials and human studies
- No controlled clinical trials. The only human-derived data are ex vivo experiments on lymphocytes taken from donors aged 75–88, in which Vilon altered chromatin condensation state. That is a cell-level observation, not a clinical outcome.
- AnimalRodent and other animal models
- Rodent work on this peptide family is reported almost exclusively by the originating laboratory and has not been independently replicated at scale.
- In vitroCell and tissue studies
- Reported to penetrate nucleus and nucleolus of HeLa cells and bind DNA sequence-selectively; reported to decondense heterochromatin and activate ribosomal genes in aged-donor lymphocytes; reported to suppress LPS-induced TNF and IL-6 in differentiated THP-1 monocytes.
Key studies & findings
4 studies- 1
Fluorescein-labelled short peptides including Vilon-class dipeptides penetrated cytoplasm, nucleus and nucleolus of HeLa cells and showed sequence-specific interaction with deoxyribooligonucleotides and DNA, discriminating cytosine methylation status.
- 2
In lymphocytes from 75–88-year-old donors, Lys-Glu (Vilon) induced deheterochromatinisation of total heterochromatin and activated ribosomal gene synthesis, with a selective effect on specific chromosome regions.
- 3
Vilon activated T-helper cells in ageing spleen tissue, an effect attributed to decreased apoptosis.
- 4
Vilon inhibited LPS-stimulated TNF and IL-6 expression in terminally differentiated THP-1 monocytes and reduced their adhesion to activated endothelium.
Benefits & effects
5 documentedChromatin decondensation in aged lymphocytes
Ribosomal gene reactivation in aged cells
T-helper cell activation in ageing spleen tissue
Suppression of LPS-induced TNF and IL-6 in monocytes
Reduced monocyte adhesion to activated endothelium
Side effects & safety
1 reportedSafety noteResearch compound for laboratory use only. No regulatory safety review, no established human safety database, and no controlled toxicology data in the public literature.
Recorded in the cited literature No controlled human safety data exist for this compound.
Purity and identity of research-grade material are unverified
Limitations & open questions
Nearly all published work on this compound originates from a single research programme (the St Petersburg Institute of Bioregulation and Gerontology, Khavinson group) and its collaborators. Independent replication outside that network is sparse to non-existent, sample sizes are small, and much of the source literature is published in Russian-language journals with limited peer-review transparency. Effects reported in cell culture and in aged-donor lymphocytes have not been shown to produce clinical outcomes in controlled human trials.
Pharmacology
Vilon is a synthetic dipeptide (C11H21N3O5, MW 275.30, CAS 45234-02-4, PubChem CID 7010502). No published pharmacokinetic study characterises its absorption, distribution, metabolism or elimination in humans. As an unprotected dipeptide it would be expected to be rapidly hydrolysed by plasma and tissue peptidases; the source literature does not reconcile this with the durable gene-expression effects it reports.
Frequently asked questions
What is Vilon's amino acid sequence?
Lys-Glu (KE), a dipeptide. This is confirmed both by PubChem (CID 7010502, lysylglutamic acid, CAS 45234-02-4) and by the Khavinson-group literature, which names Vilon as Lys-Glu directly.
Is there any human clinical trial evidence for Vilon?
No. There are no controlled clinical trials. The human-derived evidence is limited to ex vivo chromatin experiments on lymphocytes from elderly donors.
How does a two-amino-acid peptide affect gene expression?
The proposed mechanism is direct: the peptide is reported to enter the nucleus and bind DNA sequence-selectively, changing how tightly chromatin is packed. This is a hypothesis supported by in vitro binding data, not an established pharmacological mechanism.
Why is the evidence base considered weak?
Almost every study originates from one research group and its collaborators, sample sizes are small, and independent replication is largely absent. Treat reported effects as preliminary.
Citations
5 sources- 1
- 2Epigenetic modification under the influence of peptide bioregulators on the "old" chromatin
- 3Molecular aspects of immunoprotective activity of peptides in spleen during the ageing process
- 4
- 5