PEPTIDES4ALL VILON (Lys-Glu) – Synthetic Thymic Dipeptide for Immunoregulatory & Regenerative Research

PEPTIDES4ALL VILON (Lys-Glu) is a synthetic dipeptide derived from thymic peptide research, belonging to the class of short bioregulatory peptides—also known as cytogens—that have been extensively studied in the context of immune modulation, regenerative biology, and cellular aging.
Originally developed in Russian and Eastern European biomedical research, Vilon was isolated and modeled as a functional analog of endogenous thymic regulatory factors responsible for maintaining immune system homeostasis and tissue renewal throughout life.

As a minimal sequence peptide composed of L-Lysine and L-Glutamic acid, Vilon is remarkable for its stability, small molecular size, and conformational flexibility, which allow it to interact with cellular signaling pathways at extremely low concentrations. Molecular modeling studies demonstrate that the peptide forms intramolecular salt bridges and dynamic conformations, giving it the capacity to bind selectively to regulatory receptors and influence intracellular communication in lymphoid and epithelial tissues (SpringerLink, 2021).

Functionally, Vilon has been investigated in preclinical and in vitro studies for its ability to modulate immune activity, reduce inflammation, and protect thymic and splenic tissue from degenerative changes associated with aging or radiation exposure. In cell culture experiments, particularly with THP-1 monocyte/macrophage models, Vilon altered cytokine expression and proliferative behavior, suggesting direct immunoregulatory and anti-inflammatory activity (MDPI Biomedicines, 2022).

In vivo findings further indicate that Vilon may exert radioprotective and anti-senescence effects within the thymus and spleen, partially preventing the structural and functional decline of these organs under stress or irradiation (PubMed, 2019). Comparative work with related thymic peptides, such as Thymogen (Glu-Trp) and Epitalon (Ala-Glu-Asp-Gly), has shown that Vilon demonstrates unique lymphoid organ modulation, influencing T/B cell ratios, macrophage activity, and thymic epithelial maintenance (ResearchGate, 2020).

Because of its bioregulatory origin, simplicity, and broad system-level effects, Vilon has become a central model in cytogen peptide research, providing insights into how short peptide fragments may restore homeostatic balance, slow immunosenescence, and promote coordinated regeneration in complex biological systems.

With its high purity and structural precision, PEPTIDES4ALL VILON offers a reproducible research platform for exploring peptide-mediated immune modulation, thymic rejuvenation, and tissue protection under oxidative or inflammatory stress—bridging molecular immunology with emerging peptide-based longevity science.

Scientific Evidence & Research Findings

• Molecular Structure & Dynamics — Computational molecular mechanics tracing of vilon (Lys-Glu) revealed intramolecular salt bridges and conformational flexibility, compared with Thymogen (Glu-Trp). SpringerLink+1

• Cellular / Inflammatory Models — In human monocyte/macrophage (THP-1) models, Vilon® modulated proliferative activity and expression of inflammatory markers, in a study comparing it with other cytogen peptides. MDPI

• Radiation / Thymus & Spleen Model — In rat models of low-dose ionizing radiation, vilon (Lys-Glu) partially inhibited the accelerated aging (atrophy) of thymus and spleen. PubMed

• Comparative Immuno-stimulation — In older murine studies, vilon was compared to thymogen in terms of lymphoid organ weights, redistribution of T/B lymphocytes, and activation of macrophages/neutrophils. ResearchGate

Key Research Benefits & Applications

• Immunoregulatory Activity — In several animal and cell models, vilon has shown ability to influence lymphocyte distributions and phagocytic cell activation.

• Anti-aging / Tissue Protection — In radiation-induced aging of immune organs, vilon exhibited protective effects in thymus and spleen.

• Inflammation Modulation — In THP-1 monocytic cells, vilon modulated inflammatory signals and proliferative behavior.

• Structural Basis for Binding — Models suggest that vilon’s conformation and salt-bridge interactions may influence receptor binding dynamics.

Presentation & Handling

• Form: Supplied as lyophilized peptide in sterile vial.
• Reconstitution: Use bacteriostatic water or 2% procaine; swirl gently (do not shake vigorously).
• Storage: Store at –20 °C, protected from light and moisture. After reconstitution, use according to research protocols and handle under sterile conditions.

Intended Use

For research purposes only. Must be handled in accordance with institutional protocols and ethical guidelines.