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Vilon
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Vilon is a two-amino-acid peptide studied for immune system regulation and aging research through its unique gene reactivation mechanism.
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Vilon Peptide
The Epigenetic Gene Reactivation Peptide
Also known as: Lysylglutamic Acid, Lysylglutamate, KE
Why Researchers Choose Vilon
Vilon stands apart as the shortest peptide known to possess biological activity—just two amino acids—yet it works through one of the most sophisticated mechanisms in peptide research: epigenetic chromatin remodeling. Unlike peptides that simply activate receptors, Vilon selectively reactivates genes that have been silenced by aging without affecting genes that should naturally remain inactive, making it uniquely valuable for studying age-related gene suppression and immune senescence.
What It Is
Vilon is a synthetic dipeptide composed of lysine and glutamic acid, originally developed by Russian researchers at the Institute of Immunology in Moscow during the 1990s as part of a broader thymic peptide research program. The combination of positively charged lysine and negatively charged glutamate allows it to interact fluidly with cellular structures and penetrate both cell and nuclear membranes.
Researchers became interested when early studies showed that despite its minimal size (just 257 Da molecular weight), Vilon peptide could access the cell nucleus and directly influence chromatin structure—the tightly wound DNA-protein complexes that regulate which genes are available for transcription. This epigenetic mechanism made it a compelling model for understanding how peptides might reverse age-related changes in gene expression.
How It Works (What Makes It Interesting)
Studies suggest Vilon influences cellular function through several interconnected mechanisms:
- Chromatin Deheterochromatinization – Induces unrolling of tightly packed heterochromatin (the “wound” state of DNA), making previously silenced genes accessible for transcription again without affecting pericentromeric structural chromatin
- Ribosomal Gene Reactivation – Activates synthetic processes by reactivating ribosomal genes in nucleolar organizer regions, supporting protein production in aging cells
- Interleukin-2 Signaling – Activates IL-2 pathways in spleen cells, a cytokine critical for coordinating immune responses to microbial infection and preventing autoimmune reactions
- CD5 T-Cell Proliferation – Enhances expression of CD5 markers in thymus cells (78% increase observed in thymic cells), promoting differentiation of T-cell precursors toward CD4+ T-helper cells that regulate immune function
- Multi-Gene Expression Modulation – Alters expression of 36+ genes in cardiac tissue (144+ when combined with Epithalon), demonstrating broad but selective influence on tissue-specific gene patterns
- Selective Gene Activation – Uniquely appears to only reactivate genes that have been inappropriately silenced by chromatin changes, not genes that should naturally be inactive in those cell types
Common Research Applications
Immunosenescence & Immune Regulation: Thymus aging models, lymphopenia (low lymphocyte count), T-cell differentiation studies, immune suppression recovery, autoimmune disease prevention mechanisms
Gerontology & Longevity Studies: Cellular aging mechanisms, lifespan extension models, epigenetic aging clocks, bioregulatory peptide research, geroprotective compound screening
Oncology Research: Spontaneous tumor incidence studies, cancer prevention mechanisms, tumor growth inhibition models, apoptosis regulation in aging cells
Tissue Regeneration & Repair: Liver regeneration after damage, thymus restoration post-irradiation, spleen function recovery, intestinal stem cell activation, wound healing acceleration
Radiation Biology: γ-irradiation damage recovery, thymic lobule enlargement post-exposure, lymphocyte normalization after repeated irradiation
Cardiovascular Research: Cardiac gene expression patterns, vascular function regulation, heart-specific bioregulatory mechanisms
Stress & Neuroendocrine Research: Emotional stress resistance, hypothalamic c-Fos expression, adrenal hypertrophy prevention, cortisol response modulation
What You’re Getting
Every batch of our Vilon meets rigorous research standards:
- Exceeds 99% Purity – Verified by HPLC analysis
- Certificate of Analysis (COA) – Included with every order, showing purity and identity confirmation
- Endotoxin-Free – Tested to ensure <1 EU/mg for cell culture applications
- Manufactured in USA – GMP-certified facilities with full traceability
- Sterile & Lyophilized – Stable for long-term storage, easy reconstitution
- Fast Shipping – Most orders ship same day. We offer flat rate shipping and 2-3 day delivery in the USA
Click the “Add To Cart” button to grab your Vilon peptide today!
Vilon Peptide Research & Scientific Overview
Jump to: Structure | Mechanism | Studies | Pharmacokinetics | Protocols | Limitations | Lead Researcher | References
Vilon Molecular Structure & Chemical Properties
Vilon represents one of the shortest biologically active peptides ever characterized, consisting of only two amino acids yet demonstrating remarkably diverse biological effects across multiple organ systems. Originally synthesized in the 1970s as part of Professor Vladimir Khavinson’s pioneering work on peptide bioregulators, this dipeptide was developed through systematic analysis of thymus peptide extracts to identify minimal functional sequences. Unlike longer peptides that face significant stability challenges, Vilon’s compact structure provides exceptional resistance to degradation, allowing it to maintain activity across various physiological conditions. The peptide has been the subject of over four decades of research investigating its effects on immune function, chromatin remodeling, and cellular aging processes, with particular emphasis on its unique ability to modulate gene expression through epigenetic mechanisms.
Chemical Structure
 |
2D molecular structure (Source: PubChem)
Technical Specifications
| Property | Value |
|---|---|
| CAS Number | 45234-02-4 |
| Molecular Formula | C11H21N3O5 (subscripted) |
| Molecular Weight | 275.30 g/mol |
| Amino Acid Sequence | Lys-Glu (KE) |
| Half-Life (Plasma) | Not extensively characterized; presumed short based on dipeptide structure |
| Stability | Stable in aqueous solutions; resistant to gastric acid degradation |
| Solubility | Water soluble; soluble in saline and buffered solutions |
| Storage | Lyophilized: -20 degrees C; Reconstituted: 2-8 degrees C (stability varies by protocol) |
The dipeptide structure features both a positively charged lysine residue and a negatively charged glutamic acid residue, creating an amphipathic molecule that can interact with both hydrophilic and hydrophobic cellular components, potentially contributing to its cell membrane permeability and nuclear localization properties.
Vilon Mechanism of Action
Vilon peptide exerts its biological effects primarily through epigenetic modulation of chromatin structure rather than through conventional receptor-mediated signaling pathways. Current evidence suggests that chromatin remodeling and selective gene activation serve as the primary mechanisms driving Vilon’s diverse biological activities, with documented effects spanning immune function, cellular aging, and tissue regeneration across multiple organ systems.
Primary Cellular Mechanisms
Chromatin Deheterochromatinization – Gene Reactivation
Research has demonstrated that Vilon induces structural changes in chromatin, specifically targeting facultative heterochromatin that accumulates with cellular aging[1]. This mechanism involves:
- Decondensation of tightly packed chromatin allowing previously silenced genes to become transcriptionally accessible
- Reactivation of ribosomal genes through deheterochromatinization of nucleolus organizer regions
- Release of genes repressed by age-related condensation of euchromatic regions
- Selective action on facultative heterochromatin without affecting pericentromeric structural heterochromatin
Studies using differential scanning microcalorimetry revealed that Vilon treatment of lymphocytes from elderly donors resulted in chromatin heat absorption patterns resembling those of younger donors, indicating restoration of more youthful chromatin architecture[2].
Immune Cell Regulation – Thymic and Lymphocyte Modulation
Vilon peptide demonstrates potent effects on immune cell function, particularly targeting thymus-dependent processes[3]:
- Enhancement of interleukin-2 gene expression in splenocytes
- Increased thymocyte proliferation and activation following stress or radiation exposure
- Upregulation of activation markers including HLA-DR and CD54 on thymic cells
- Normalization of lymphocyte blast-transformation responses critical for immune function
- Stimulation of both T-cell and B-cell differentiation pathways
The peptide appears to selectively reactivate immune-related genes that have been silenced rather than inducing inappropriate gene expression, suggesting tissue-specific regulatory mechanisms[4].
Cell Proliferation and Differentiation Signaling
Investigations indicate Vilon influences multiple proliferative pathways[5]:
- Increased tyrosine phosphorylation of mitogen-activated cytoplasmic kinases
- Modulation of ERK1/2 phosphorylation levels in certain cell types
- Enhancement of calcium signaling in thymocytes and macrophages, a key activation mechanism
- Promotion of cellular proliferation while maintaining appropriate apoptotic balance
Antioxidant and Cytoprotective Mechanisms
Research suggests Vilon peptide may exert protective effects through oxidative stress modulation:
- Reduction of lipid peroxidation markers in aging cells
- Protection of cellular integrity under stress conditions
- Support of mitochondrial function in aged tissues
- Maintenance of cellular redox balance
Vilon Research Applications & Key Findings
Aging and Longevity Research
Lifespan Extension Studies
Extensive research in mouse models has examined Vilon’s effects on aging biomarkers and lifespan, with studies demonstrating significant longevity benefits[6]. Key findings include:
- Increased mean lifespan in female CBA mice treated from 6 months of age
- Enhanced physical activity and endurance compared to age-matched controls
- Decreased body temperature, associated with reduced metabolic rate and extended lifespan
- Prevention of spontaneous neoplasm development in aging animals
- No adverse effects observed with long-term chronic administration
Subcutaneous administration at 10 mcg/kg resulted in measurable improvements in biological age markers without affecting estrous function or baseline free radical processes[7].
Chromatin Aging and Gene Expression
Studies in cultured lymphocytes from elderly human donors showed remarkable chromatin restoration effects[8]:
- Progressive activation of facultative heterochromatin that increases with donor age
- Reactivation of ribosomal genes silenced by age-related chromatin condensation
- Restoration of lymphocyte chromatin structure toward more youthful patterns
- Enhanced synthetic processes in aged immune cells
These findings suggest potential for reversing age-related epigenetic changes contributing to immunosenescence.
Oncology Research
Tumor Prevention Studies
Multiple investigations examined Vilon’s effects on spontaneous and chemically-induced tumor development[9,10]:
- Reduced spontaneous tumor incidence in aging mice (total tumor formation decreased significantly)
- Lower occurrence of pulmonary adenomas and mammary adenocarcinomas in treated animals
- Decreased incidence of chemically-induced bladder tumors (14.3% in treated vs 60% in controls)
- Twofold reduction in preneoplastic changes in urinary bladder mucosa
- Inhibition of 1,2-dimethylhydrazine-induced kidney neoplasia
The mechanisms appear related to immune system enhancement and maintenance of cellular integrity rather than direct cytotoxic effects.
Combination Therapy Considerations
Research indicates complex interactions with chemotherapeutic agents:
- Enhancement of survival in mice with transplanted Lewis lung carcinoma when given alone
- Potential antagonism when combined simultaneously with cyclophosphamide chemotherapy
- Stimulation of apoptosis in both young and old tissue cultures
- Results suggest timing and sequencing critical for combination approaches[11]
Immunology Research
Immune System Restoration
Studies in radiation-exposed and aging models demonstrated immune-restorative effects[12]:
- Accelerated recovery of thymus structure following gamma-irradiation
- Restoration of thymic lobules through expansion of cortical layers
- Enhanced thymocyte proliferation and differentiation post-irradiation
- Improved B-cell and T-cell maturation in immunocompromised models
- Normalized immune parameters in stress-induced immune suppression
Immune Cell Activation
In vitro investigations revealed specific cellular activation patterns:
- Increased intracellular calcium concentrations in thymocytes and macrophages
- Enhanced expression of CD5 markers on mature T-helper cells
- Activation of both neutrophils and macrophages at specific concentrations
- Lymphocyte redistribution in lymphoid organs following treatment
Cardiovascular and Renal Research
Gene Expression Modulation
Microarray analysis revealed Vilon’s effects on cardiac tissue gene expression[13]:
- Alteration of expression patterns in 36 different cardiac genes
- Effects on genes involved in vascular regulation and hemodynamic function
- Potential modulation of coagulation pathways and fibrinolysis
- Increased concentrations of natural anticoagulants (antithrombin III, protein C)
Renal Protection Studies
Research in chronic renal failure models demonstrated protective effects[14]:
- Decreased serum transforming growth factor-beta-1 concentrations
- Reduced microvessel permeability in mesenteric circulation
- Protective effects observed 2 months after onset of experimental renal failure
- Potential modulation of fibrotic processes in kidney disease
Vilon Pharmacokinetics & Metabolism
Absorption & Distribution
Vilon peptide exhibits pharmacokinetic properties consistent with small dipeptides, though comprehensive characterization remains limited. Based on available research:
- Subcutaneous bioavailability confirmed in multiple rodent studies
- Presumed rapid absorption given small molecular size and hydrophilic nature
- Tissue distribution studies demonstrate accumulation in lymphoid organs (thymus, spleen)
- Nuclear localization observed in chromatin interaction studies
- Oral activity has been suggested but not extensively characterized
The dipeptide’s amphipathic structure (positive lysine, negative glutamate) may facilitate membrane permeability and intracellular uptake compared to larger peptides.
Metabolism & Elimination
Detailed metabolic studies of Vilon are notably absent from published literature, but general dipeptide characteristics suggest:
- Rapid degradation by plasma and tissue peptidases expected
- Presumed plasma half-life measured in minutes to hours
- Cleavage into constituent amino acids (lysine and glutamate) by peptidases
- No evidence of accumulation with repeated dosing in animal studies
- Metabolic stability may be enhanced compared to longer peptides
A significant knowledge gap exists regarding the relationship between presumed rapid clearance and the prolonged biological effects (days to weeks) observed in aging and immune function studies, suggesting either: tissue retention, generation of active metabolites, or initiation of persistent epigenetic changes.
Excretion Pathways
Limited data on excretion mechanisms indicate:
- Likely renal elimination of dipeptide and constituent amino acids
- No evidence of biliary or hepatic excretion pathways
- Lysine and glutamate incorporation into normal amino acid pools expected
- No reports of accumulation toxicity in chronic administration studies
The absence of comprehensive pharmacokinetic studies represents a major translational gap requiring systematic investigation before human applications could be considered.
Vilon Research Protocols & Administration
Dosing in Published Research
Research investigations have employed Vilon doses varying by species, experimental model, and route of administration:
- Mouse studies: 10 mcg/kg most commonly used for longevity and tumor studies (range: 1-1000 mcg/kg)
- Rat studies: 1-10 mcg/kg typical for immune function and organ protection research
- In vitro studies: 0.01-10 mcg/mL in cell culture media for chromatin and immune cell experiments
- Chronic administration: Long-term dosing studies extended over months to years in aging research
Important: These are experimental doses used in animal studies and cannot be extrapolated to other species due to fundamental differences in peptidase activity, tissue distribution, receptor expression density, metabolic rate, and pharmacokinetic parameters. Species-specific factors profoundly influence both efficacy and safety profiles, making direct dose translation inappropriate and potentially hazardous.
Administration Routes in Research
Multiple delivery methods have been investigated:
- Subcutaneous injection – Most common route in aging, longevity, and tumor prevention studies
- Intraperitoneal injection – Used in acute immune modulation and radiation protection research
- Cell culture application – Direct medium supplementation for in vitro chromatin and lymphocyte studies
- Oral administration – Suggested in some gastrointestinal research but not systematically characterized
Common Model Organisms
Vilon has been studied across multiple experimental systems:
- Mice – Primary model for aging, tumor prevention, and lifespan studies (CBA, C57BL/6 strains)
- Rats – Used for immune function, radiation protection, and organ-specific studies (Wistar strain common)
- Cell culture systems – Human lymphocytes from elderly donors, thymocytes, splenocytes, various tissue explants
- Tissue explants – Organotypic cultures of thymus, spleen, and other tissues from animals of varying ages
Research Limitations & Regulatory Status
Critical Gaps in Current Evidence
Despite over 40 years of preclinical research spanning hundreds of publications, Vilon faces substantial evidence gaps that limit its translational potential and prevent clinical applications.
Lack of Human Clinical Data
The most significant limitation is the complete absence of controlled human studies:
- No Phase I, II, or III clinical trials published in peer-reviewed literature
- No registered clinical trials in major international databases (ClinicalTrials.gov, EudraCT)
- Human safety profile completely unestablished – no systematic toxicology data
- Optimal human dosing unknown and cannot be reliably predicted from animal data
- Long-term effects in humans unstudied across any age group or condition
- No pharmacokinetic data in human subjects
The extensive Russian-language literature has not been translated or validated through international peer-review standards common in Western pharmaceutical development.
Mechanistic Understanding Gaps
Fundamental aspects of Vilon’s mechanism remain poorly characterized:
- Precise molecular targets for chromatin interaction not identified at atomic resolution
- Whether effects result from direct DNA binding versus indirect signaling mechanisms unclear
- Relationship between rapid presumed clearance and prolonged biological effects unexplained
- Tissue-specific selectivity mechanisms not elucidated
- Active metabolite contribution to effects versus parent peptide actions unknown
- Dose-response relationships incompletely characterized across different endpoints
Long-Term Safety Considerations
Critical safety questions remain unanswered even in animal models:
- Chronic use effects beyond one year inadequately studied
- Potential for dysregulation of gene expression with extended use unknown
- Effects on cancer cell growth in individuals with existing tumors understudied
- Interaction potential with medications uncharacterized
- Reproductive and developmental toxicity not systematically evaluated
- Effects across diverse genetic backgrounds and disease states unknown
The observation of reduced tumor incidence in some studies combined with potential interference with chemotherapy in others highlights unresolved safety considerations.
Regulatory & Competitive Sport Status
FDA and Regulatory Position
Vilon has not received approval from major regulatory authorities:
- Not approved by FDA for any indication (human or veterinary use)
- Not recognized as Generally Recognized as Safe (GRAS)
- Not approved for medical compounding in the United States
- No established therapeutic use basis from any major health authority worldwide
- Classified as unapproved new drug substance by regulatory agencies
No applications for regulatory approval appear to have been submitted to FDA, EMA, or other major agencies.
WADA Status
Currently, Vilon’s status under World Anti-Doping Agency regulations is not explicitly defined:
- Not specifically listed by name in WADA prohibited substance lists
- May fall under Section S0 (Non-Approved Substances) due to lack of regulatory approval
- Classification as peptide hormone and growth factor requires case-by-case evaluation
- No published guidance on detection methods or testing protocols
Athletes should consult with anti-doping authorities before considering any experimental peptides.
Research Classification: Vilon is available only for laboratory research use. It is not intended for human consumption, medical use, or veterinary applications. All research must be conducted under appropriate ethical oversight and regulatory compliance with institutional review board approval where applicable.
Lead Researcher Spotlight
Professor Vladimir Khatskelevich Khavinson, MD, PhD
Former Director
Saint Petersburg Institute of Bioregulation and Gerontology, Saint Petersburg, Russia
Professor Vladimir Khavinson (1946-2024) pioneered the field of peptide bioregulators through four decades of systematic research beginning in the 1970s. His work originated from Soviet military research aimed at protecting personnel from environmental stresses, eventually evolving into comprehensive investigations of tissue-specific peptides and their effects on aging, immunity, and gene expression. Khavinson developed a systematic methodology for identifying biologically active short peptides through amino acid composition analysis of tissue extracts, leading to the synthesis of over 20 distinct peptide bioregulators including Vilon.
Professor Khavinson’s research contributions to Vilon include:
- Original synthesis and characterization of Vilon (Lys-Glu) from thymus peptide extract analysis in the 1970s
- Extensive investigations of immunomodulatory effects and thymus function restoration
- Pioneering studies on chromatin remodeling and epigenetic mechanisms of peptide action
- Longevity and tumor prevention research establishing geroprotective potential
- Gene expression studies using microarray technology to characterize molecular targets
His laboratory published over 775 scientific papers and obtained 196 patents across multiple countries. Khavinson served as President of the European Region of the International Association of Gerontology and Geriatrics (2011-2015) and founded the Saint Petersburg Institute of Bioregulation and Gerontology in 1992, which became the primary center for peptide bioregulator research worldwide.
Disclaimer: This spotlight is provided for educational purposes to acknowledge scientific contributions to Vilon research. Cenexa Labs has no affiliation with Professor Khavinson, his estate, or the Saint Petersburg Institute of Bioregulation and Gerontology, and this information does not constitute an endorsement of any products or services.
References
- Lezhava, T., Khavinson, V., Monaselidze, J., Jokhadze, T., Dvalishvili, N., Bablishvili, N., & Barbakadze, S. (2004). Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people. Biogerontology, 5(2), 73-79. PubMed
- Khavinson, V.K., Lezhava, T.A., Monaselidze, J.G., Dzhokhadze, T.A., Dvalishvili, N.A., Bablishvili, N.K., & Ryadnova, I.Y. (2004). Effects of short peptides on lymphocyte chromatin in senile subjects. Bulletin of Experimental Biology and Medicine, 137(1), 78-81. PubMed
- Kazakova, T.B., Barabanova, S.V., Khavinson, V.K., Glushikhina, M.S., Parkhomenko, E.P., Malinin, V.V., & Korneva, E.A. (2002). In vitro effect of short peptides on expression of interleukin-2 gene in splenocytes. Bulletin of Experimental Biology and Medicine, 133(6), 614-616. PubMed
- Sevostianova, N.N., Kuznik, B.I., Khavinson, V.K., Malinin, V.V., Ryzhak, G.A., & Mikhaleva, I.V. (2013). Immunomodulating effects of Vilon and its analogue in the culture of human and animal thymus cells. Bulletin of Experimental Biology and Medicine, 154(4), 562-565. PubMed
- Ticinesi, A., Nouvenne, A., Tana, C., Prati, B., & Meschi, T. (2022). Peptides regulating proliferative activity and inflammatory pathways in the monocyte/macrophage THP-1 cell line. International Journal of Molecular Sciences, 23(7), 3607. PubMed
- Khavinson, V.K., Anisimov, V.N., Zavarzina, N.Y., Zabezhinskii, M.A., Zimina, O.A., Popovich, I.G., Shtylik, A.V., Malinin, V.V., & Morozov, V.G. (2000). Effect of vilon on biological age and lifespan in mice. Bulletin of Experimental Biology and Medicine, 130(7), 687-690. PubMed
- Khavinson, V.K., & Anisimov, V.N. (2000). A synthetic dipeptide vilon (L-Lys-L-Glu) inhibits growth of spontaneous tumors and increases life span of mice. Doklady Biological Sciences, 372, 261-263. PubMed
- Lezhava, T., Monaselidze, J., Kadotani, T., Dvalishvili, N., & Buadze, T. (2006). Anti-aging peptide bioregulators induce reactivation of chromatin. Georgian Medical News, 133, 111-115. PubMed
- Anisimov, V.N., Loktionov, A.S., Khavinson, V.K., & Morozov, V.G. (1989). Effect of low-molecular-weight factors of thymus and pineal gland on life span and spontaneous tumour development in female mice of different age. Mechanisms of Ageing and Development, 49(3), 245-257. PubMed
- Pliss, G.B., Mel’nikov, A.S., Malinin, V.V., & Khavinson, V.K. (2001). Inhibitory effect of peptide vilon on the development of induced rat urinary bladder tumors in rats. Bulletin of Experimental Biology and Medicine, 131(6), 558-560. PubMed
- Bykov, N.M., Chalisova, N.I., & Zeziulin, P.N. (2004). Combined effect of vilon and cyclophosphane on tumor transplants and lymphoid tissue explants in mice and rats of various age. Advances in Gerontology, 13, 122-129. PubMed
- Khavinson, V.K., Izmailov, D.M., Obukhova, L.K., Malinin, V.V., & Rybakina, E.G. (2002). Effect of Vilon on recovery of immune homeostasis in gamma-irradiated rats. Bulletin of Experimental Biology and Medicine, 134(2), 179-182.
- Anisimov, S.V., Boheler, K.R., Khavinson, V.K., & Anisimov, V.N. (2002). Studies of the effects of Vilon and Epithalon on gene expression in mouse heart using DNA-microarray technology. Bulletin of Experimental Biology and Medicine, 133(3), 293-299.
- Khavinson, V.K., Malinin, V.V., & Fedulov, A.V. (2005). Effect of peptide Vilon on the content of transforming growth factor-beta and permeability of microvessels during experimental chronic renal failure. Bulletin of Experimental Biology and Medicine, 140(3), 315-317. PubMed
All references open in new window. These citations are provided for educational and research purposes only. This information is not intended to diagnose, treat, cure, or prevent any disease. Vilon is intended for laboratory research use only.
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Why Researchers Choose Cenexa Labs
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