Vilon 20mg (Lys-Glu)

Description

Disclaimer: This compound is provided strictly for laboratory and scientific research purposes only. It is not approved by the U.S. Food and Drug Administration (FDA) for human or veterinary use, including ingestion, injection, or any form of administration.

Chemical Properties of Vilon

Overview

Vilon is a synthetic dipeptide composed of lysine (Lys) and glutamic acid (Glu). Its single-letter sequence designation is KE. Based on articles retrieved from PubMed, it belongs to the class of tissue-specific short bioregulator peptides developed at the St. Petersburg Institute of Bioregulation and Gerontology. It is classified in research literature as a thymus-derived dipeptide bioregulator. Short peptides of this class are designed based on the amino acid composition analysis of tissue extracts. They are proposed to exert organotropic regulatory activity in target tissue cell preparations in experimental models. [Khavinson, 2002]

The FDA has not approved Vilon for human or veterinary use, including ingestion, injection, or any form of administration. It is not a dietary supplement or consumer product. Availability is restricted to qualified researchers at licensed institutions. Clinical research initiatives require guidance from the relevant Institutional Review Board (IRB). Preclinical animal studies must comply with IACUC directives under the Animal Welfare Act (AWA).

Working Mechanism of Vilon

Vilon (Lys-Glu) belongs to the class of short bioregulator peptides proposed to exert tissue-specific regulatory activity through interactions with chromatin structures in experimental models. Short peptides of 2–7 amino acid residues are proposed to penetrate cell nuclei and nucleoli and interact with nucleosomes, histone proteins, and both single- and double-stranded DNA in experimental systems. [Khavinson et al., 2021]

Based on articles retrieved from PubMed, Vilon (Lys-Glu) has been specifically studied for its influence on condensed chromatin in lymphocytes from aged individuals. Heterochromatinization is the progressive condensation of chromatin regions in aging cells. This process is associated with gene silencing and aging pathologies. Short peptide bioregulators, including Vilon, were observed to induce selective deheterochromatinization of chromatin regions in experimental lymphocyte culture models. All mechanistic findings are from in vitro and cell-based experimental models only. Human pharmacology data are absent. Findings are not generalizable to human therapeutic outcomes. [Lezhava et al., 2023]

Research Findings / Research Applications

Preclinical investigations have examined Vilon (Lys-Glu) and related thymus-derived short peptide bioregulators in relation to:

Vilon-Specific Chromatin Remodeling in Aged Lymphocyte Models

Based on articles retrieved from PubMed, Vilon (Lys-Glu) was studied alongside other short peptide bioregulators for its influence on condensed chromatin in lymphocyte cell cultures derived from aged donors (75–88 years). Molecular-cytogenetic methods, including differential scanning calorimetry, ribosomal gene activity analysis, C-heterochromatin polymorphism, and sister chromatid exchange assessment, were employed. Progressive heterochromatinization of chromosomes was observed in aged cell preparations, associated with the deactivation of previously active genes. Vilon (Lys-Glu) was observed to induce selective deheterochromatinization of total heterochromatin and satellite stalks of acrocentric chromosomes in the cell culture model. Each peptide bioregulator studied, including Lys-Glu, demonstrated a selective effect on definite chromosome regions. Findings are from in vitro cell culture models only and do not constitute clinical evidence.

[Lezhava et al., 2023 — https://pubmed.ncbi.nlm.nih.gov/37042594/]

Tissue-Specific Thymus Dipeptide Bioregulator Activity in Explant Models

Based on articles retrieved from PubMed, dipeptides specific for the thymus, derived from amino acid analysis of thymic tissue extracts, were investigated for their proposed tissue-specific regulatory activity. In vitro explant outgrowth models demonstrated that thymus-specific dipeptides stimulate outgrowth of thymic tissue explants but not explants from other tissues, suggesting organotropic specificity. This tissue selectivity was studied as a foundational research observation in the broader investigation of short peptide bioregulator organ-specificity. Changes in gene expression were observed to be associated with short peptide preparations in these experimental systems. Findings are from in vitro explant models only and require compound-specific validation.

[Khavinson, 2002 — https://pubmed.ncbi.nlm.nih.gov/12374906/]

Short Peptide Gene Expression Regulation — Class-Level Research Framework

Based on articles retrieved from PubMed, short peptides consisting of 2–7 amino acid residues, including dipeptides of the KE-sequence class, are proposed to penetrate cell nuclei and interact with nucleosomes, histone proteins, and both single- and double-stranded DNA. DNA-peptide interactions in gene promoter regions have been studied in relation to transcription, replication, and DNA methylation regulation. Short peptides have been proposed to regulate the status of DNA methylation as an epigenetic mechanism for gene activation or repression in normal conditions and in senescence. These findings are from a systematic review of preclinical literature and do not constitute clinical evidence. Vilon is not specifically named in this source. These findings apply to the broader class of short bioregulator dipeptides.

[Khavinson et al., 2021 — https://pubmed.ncbi.nlm.nih.gov/34834147/]

Note: All findings above are from preclinical, in vitro, or cell-based experimental models only. Results are not consistent across all experimental models, and data remain limited without validation in human clinical settings.

Risks & Handling Information

Risk Tier: LOW-MODERATE. Vilon is a synthetic dipeptide composed of two endogenous amino acids (lysine and glutamic acid). Its biological activity profile in experimental systems remains incompletely characterized. The full toxicological profile in human biological systems has not been established. Any unintentional exposure should be treated as requiring immediate decontamination and medical consultation.

PPE Requirement: Nitrile gloves, lab coat, and eye protection are required at all times during all handling and reconstitution procedures involving this compound.

Controlled Environment: Handling must occur exclusively within controlled laboratory environments with adequate ventilation, appropriate containment, and institutional biosafety oversight. This compound must not be handled in non-laboratory settings under any circumstances.

Exposure Prohibition: Do not inhale, ingest, or make direct skin contact with this compound. This material is not intended for any form of self-administration or non-laboratory exposure under any circumstances.

Toxicological Status: The full toxicological profile of Vilon in human biological systems is not established. As a short bioregulator dipeptide proposed to interact with chromatin structures and gene expression regulatory pathways, researchers must adhere to institutional biosafety protocols applicable to nucleic acid-interacting research compounds.

Storage and Degradation Risk: Maintain lyophilized vials at −20°C until use. Following reconstitution, store at 2–8°C and use within 30 days. Avoid repeated freeze-thaw cycles and exposure to heat, light, or moisture to preserve research-grade peptide integrity.

FAQs

Q: What is the regulatory status of Vilon in the United States?

Vilon (H-Lys-Glu-OH) has not been approved by the FDA for human or veterinary use, including ingestion, injection, or any form of administration. It is available exclusively for qualified laboratory and scientific research purposes at licensed institutions operating under applicable institutional oversight frameworks.

Q: What is the amino acid composition of Vilon?

Vilon is a dipeptide composed of two amino acid residues: L-lysine (Lys, K) and L-glutamic acid (Glu, E). Its single-letter sequence designation is KE. It is identified by CAS number 45234-02-4 and molecular formula C₁₁H₂₁N₃O₅.

Q: What tissue class is Vilon derived from in the research classification?

Based on articles retrieved from PubMed, Vilon is classified as a thymus-derived short bioregulator dipeptide. It was developed based on amino acid analysis of thymic tissue extracts at the St. Petersburg Institute of Bioregulation and Gerontology. Short thymus-specific dipeptides of this class are proposed to exert organotropic regulatory activity in thymic tissue experimental models. [Khavinson, 2002]

Q: What chromatin effects has Vilon specifically been studied for in experimental models?

Based on articles retrieved from PubMed, Vilon (Lys-Glu) was studied in lymphocyte cell cultures derived from aged donors and was observed to induce selective deheterochromatinization of total heterochromatin and satellite stalks of acrocentric chromosomes. Each peptide bioregulator studied demonstrated a selective effect on definite chromosome regions. Findings are from in vitro aged human lymphocyte culture models only. [Lezhava et al., 2023]

Q: What storage conditions are required to maintain Vilon integrity for research use?

Lyophilized Vilon should be stored at −20°C, protected from light, heat, and moisture. Following reconstitution in an appropriate aqueous buffer, store at 2–8°C and use within 30 days. Avoid repeated freeze-thaw cycles to preserve peptide integrity.

Q: What distinguishes Vilon from other short bioregulator peptides in the same class?

Vilon carries the KE (Lys-Glu) dipeptide sequence, distinguishing it from related bioregulator peptides Vesilute (Glu-Asp, ED) and from tetrapeptides such as Epitalon (Ala-Glu-Asp-Gly) and Livagen (Lys-Glu-Asp-Ala). Based on articles retrieved from PubMed, each short peptide bioregulator has been proposed to exert selective effects on definite chromosome regions in experimental models. [Lezhava et al., 2023]

References

Khavinson, V. Kh. (2002). Peptides and Ageing. Neuro Endocrinology Letters, 23(Suppl 3), 11–144. https://pubmed.ncbi.nlm.nih.gov/12374906/

Khavinson, V. K., Popovich, I. G., Linkova, N. S., Mironova, E. S., & Ilina, A. R. (2021). Peptide Regulation of Gene Expression: A Systematic Review. Molecules, 26(22), 7053. https://pubmed.ncbi.nlm.nih.gov/34834147/

Lezhava, T., Jokhadze, T., Monaselidze, J., Buadze, T., Gaiozishvili, M., Sigua, T., Khujadze, I., Gogidze, K., Mikaia, N., & Chigvinadze, N. (2023). Epigenetic Modification Under the Influence of Peptide Bioregulators on the “Old” Chromatin. Georgian Medical News, 335, 79–83. https://pubmed.ncbi.nlm.nih.gov/37042594/

BC9 Disclaimer

This content is presented exclusively for educational purposes and should not be construed as medical advice. THE MATERIALS REFERENCED HEREIN ARE EXCLUSIVELY INTENDED FOR LABORATORY AND RESEARCH USE.

Any clinical research initiatives must be conducted under the guidance of the relevant Institutional Review Board (IRB). Similarly, preclinical research involving animals must comply with the directives of the Institutional Animal Care and Use Committee (IACUC), adhering to the standards delineated by the Animal Welfare Act (AWA).

Our informational content is meticulously designed for research-oriented insights and is not a substitute for individual analysis and verification from credible sources before any purchasing decisions are made.Upon finalizing your order and payment, you explicitly acknowledge and agree to adhere to our Terms and Conditions. Customer satisfaction stands as our paramount concern. If you are dissatisfied with the product received, kindly contact us at 419-707-5450 or email our support team at support@bc9.co.

IMPORTANT NOTICE: All products showcased on our platform are EXCLUSIVELY INTENDED FOR LABORATORY AND RESEARCH APPLICATIONS. They are expressly not intended for veterinary or human utilization.