High-purity Vilon (Lys-Glu) dipeptide is a critical reference standard for investigating short-chain peptide interaction with lipid membranes, nuclear envelopes, and chromatin structures. Laboratories seeking to buy Vilon membrane binding research compounds require analytical-grade purity (>98%), validated sequence identity via mass spectrometry, and verified endotoxin control to ensure reproducible data in cell-free and cell-based biophysical assays.
High-purity Vilon (Lys-Glu) dipeptide is a critical reference standard for investigating short-chain peptide interaction with lipid membranes, nuclear envelopes, and chromatin structures. Laboratories seeking to buy Vilon membrane binding research compounds require analytical-grade purity (>98%), validated sequence identity via mass spectrometry, and verified endotoxin control to ensure reproducible data in cell-free and cell-based biophysical assays.
Vilon is a synthetic ultra-short bioregulatory dipeptide composed of L-lysine and L-glutamic acid (H-Lys-Glu-OH). Originally derived from computational and structural analysis of thymic peptide fractions, Vilon has become a primary target of investigation in cellular biophysics, epigenetics, and membrane transport dynamics. Researchers studying membrane binding phenomena examine how the specific zwitterionic charge distribution of Lys-Glu interacts with eukaryotic cell membrane microdomains, phospholipid bilayers, and nuclear envelopes.
When purchasing compounds to study membrane binding, investigators must ensure that the peptide standard is free from residual synthetic scavengers, counter-ions, or bacterial endotoxins that can artificially disrupt lipid bilayers or alter surface charge kinetics. PX1 Research supplies high-purity Vilon research peptide specifically synthesized for high-throughput in vitro binding assays, fluorescence polarization studies, and nuclear translocation assays.
Understanding the specific interactions between short peptide chains and biological membranes is essential for mapping non-receptor-mediated cellular entry mechanisms. Because Vilon lacks a extended hydrophobic core, its capacity to associate with cell membranes relies heavily on electrostatic interactions with polar headgroups, followed by targeted penetration into the nuclear matrix where it binds directly to histone proteins and DNA promoter regions.
Vilon possesses a molecular formula of C11H21N3O5 and a molecular weight of approximately 275.3 g/mol. At physiological pH (7.4), the N-terminal amino acid (L-lysine) carries a positively charged alpha-amino group and an epsilon-amino side chain, while the C-terminal amino acid (L-glutamic acid) presents a negatively charged carboxyl group and a gamma-carboxyl side chain. This unique balance of basic and acidic moieties within a two-amino-acid motif yields a distinct dipolar moment that facilitates electrostatic docking with cell membrane components.
Biophysical characterization indicates that Vilon does not disrupt lipid bilayer integrity via pore formation or detergent-like lysis. Instead, in vitro fluorescence spectroscopic models demonstrate that Vilon partitions near the interfacial region of phosphatidylcholine and phosphatidylserine membranes. The basic lysine residue anchors to negatively charged phospholipid headgroups, permitting the dipeptide to adopt a conformation that facilitates crossing of biological barriers without requiring energy-dependent active transport systems.
To explore comprehensive data on peptide structural dynamics and bioregulatory pathways, researchers can consult the PX1 Research Hub, which catalogues comparative literature on short-chain peptide-membrane interactions.
Preclinical studies evaluating Vilon have demonstrated a two-stage mechanism of cellular interaction: outer membrane association followed by rapid intranuclear localization. In vitro models using fluorophore-labeled Lys-Glu show that upon crossing the plasma membrane, the dipeptide preferentially migrates to the nucleus. Inside the nuclear matrix, Vilon binds to specific DNA sequences and histone tails, inducing local chromatin decondensation.
Research in cell culture models indicates that Vilon selectively binds to double-stranded DNA motifs containing specific nucleotide sequences (such as CATTG and CTTG). By interacting with the major and minor grooves of DNA, as well as binding to histone H1 and H3 proteins, Vilon modulates the accessibility of RNA polymerase complexes to promoter regions of genes involved in cellular senescence, antioxidant defense, and cell proliferation.
These nuclear interactions highlight why researchers investigating epigenetic peptide bioregulators focus on Vilon as a key model molecule. Unlike larger proteins that require receptor-mediated endocytosis, short dipeptides like Lys-Glu bypass classical surface receptors, providing a unique model for direct nuclear signaling.
When evaluating candidates for membrane binding and gene regulation studies, investigators frequently compare Vilon against other short-chain thymic and bioregulatory peptides. The structural variations between di-, tri-, and tetrapeptides significantly alter their membrane partition coefficients, binding affinities, and nuclear access times.
For example, Vilon (Lys-Glu) exhibits rapid nuclear entry and high affinity for histone structures due to its concentrated charge density. In contrast, Epitalon (Ala-Glu-Asp-Gly), a synthetic tetrapeptide modeled after pineal gland secretions, exhibits distinct binding kinetics focused on telomerase modulation and heterochromatin remodeling. Similarly, Thymogen (Glu-Trp), another short thymic dipeptide, incorporates a bulky hydrophobic tryptophan residue that alters its membrane insertion depth compared to the highly hydrophilic Lys-Glu backbone.
The following matrix outlines the key structural and biophysical differences across these comparative compounds used in laboratory assays:
In vitro membrane binding assays—such as isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), and liposome leakage assays—are highly sensitive to chemical impurities. The presence of residual trifluoroacetic acid (TFA) salts, uncoupled amino acids, or synthesis side-products can skew binding affinity constants ($K_d$) and generate false-positive membrane disruption signals.
To maintain assay precision, laboratories must procure Vilon synthesized to strict analytical specifications. Mass spectrometry (ESI-MS) must confirm the exact molecular ion peak at 276.15 m/z ([M+H]+), validating the absence of deletion sequences or truncated peptide fragments. High-Performance Liquid Chromatography (RP-HPLC) analysis must confirm chemical purity of >98.0%, ensuring that chromatographic peaks reflect only pure Lys-Glu dipeptide.
For laboratories scaling up their screening protocols, sourcing verified standards through an institutional wholesale portal ensures batch-to-batch consistency across extended experimental series.
Bacterial endotoxins (lipopolysaccharides, LPS) are potent biological contaminants that avidly bind to cell membranes and activate Toll-like receptors (TLR4) in cell culture models. If a peptide sample contains elevated endotoxin levels, observed cellular responses—such as membrane depolarization, cytokine release, or altered gene expression—may result from endotoxin contamination rather than the research peptide itself.
PX1 Research subjects every production lot of Vilon to rigorous Limulus Amebocyte Lysate (LAL) testing, guaranteeing endotoxin levels below 0.01 EU/mg. This low endotoxin threshold is essential for studies evaluating cellular senescence, immune cell modulation, or membrane permeability, preventing confounding signaling artifacts during live-cell imaging or transcriptomic analysis.
Researchers can browse our full catalog of research peptides to review detailed purity specifications and analytical metrics for all available bioregulatory research standards.
Vilon is supplied as a lyophilized white powder to maximize chemical stability during transport and storage. Proper laboratory reconstitution protocols must be followed to maintain peptide integrity and prevent premature hydrolysis or aggregation prior to binding assays.
For optimal solubility, lyophilized Vilon should be reconstituted in sterile, deionized water or phosphate-buffered saline (PBS, pH 7.4). Because Lys-Glu is highly soluble in aqueous media due to its hydrophilic and zwitterionic structure, gentleness during reconstitution is sufficient; avoid vigorous vortexing or sonication, which can introduce shear forces or induce air-water interface denaturation.
Reconstituted stock solutions should be aliquoted into polypropylene microcentrifuge tubes to prevent adsorption loss to glass surfaces and avoid repeated freeze-thaw cycles. Stored at -20°C or -80°C, reconstituted aliquots maintain structural stability for extended research use. Lyophilized vials should be stored at -20°C in a desiccated environment upon arrival.
PX1 Research is committed to supplying the scientific community with analytical-grade compounds that strictly adhere to research standards. Every batch of Vilon synthesized in our USA-based GMP-compliant facilities undergoes independent, third-party testing at ISO 17025 accredited laboratories.
Each shipment includes a lot-specific Certificate of Analysis (COA) detailing RP-HPLC purity traces, mass spectra verification, water content, residual solvent analysis, and endotoxin quantitation. By providing total lot traceability and transparent analytical data, PX1 Research enables investigators to publish reproducible, high-impact data.
To support rigorous project timelines, PX1 Research operates domestic fulfillment centers in California and Arizona, offering same-day shipping for orders placed Monday through Friday before 12:00 PM PST.
What is the targeted primary research use of Vilon?
Vilon (Lys-Glu) is supplied strictly as a research-grade compound for in vitro laboratory investigation. It is primarily studied for its interactions with lipid membranes, nuclear envelopes, histone proteins, chromatin decondensation, and epigenetic gene regulation.
How does Vilon interact with cell membranes in preclinical models?
Preclinical biophysical studies indicate that Vilon's zwitterionic structure allows it to bind electrostatically to polar heads of membrane phospholipids. It translocates across bilayers without causing mechanical pore formation or lysis, allowing it to reach the cell nucleus.
What purity level is required for Vilon membrane binding research?
Membrane binding assays require Vilon with >98.0% purity confirmed by RP-HPLC and ESI-MS. Impurities or residual synthesis reagents can disrupt lipid bilayers, generating false positives in binding kinetics or membrane permeability assays.
What are the endotoxin limits for PX1 Research Vilon?
PX1 Research verifies that all Vilon lots contain endotoxin levels under 0.01 EU/mg using standard LAL assays, preventing LPS-induced membrane signaling artifacts in cell culture experiments.
How should lyophilized Vilon be stored upon receipt?
Lyophilized Vilon should be stored at -20°C or -80°C in a desiccated storage container. Under these conditions, the un-reconstituted peptide remains stable for extended laboratory storage.
What solvent is recommended for reconstituting Vilon for biophysical assays?
Vilon is highly soluble in aqueous media. Sterile double-distilled water or phosphate-buffered saline (PBS, pH 7.4) is recommended for reconstitution prior to dilution into cell culture or binding assay buffers.
How does Vilon differ structurally from Thymogen?
Vilon consists of Lysine and Glutamic Acid (Lys-Glu), making it highly hydrophilic and charged. Thymogen consists of Glutamic Acid and Tryptophan (Glu-Trp), featuring a hydrophobic aromatic side chain that alters membrane insertion depth.
Does PX1 Research provide lot-specific COAs with Vilon purchases?
Yes. Every order of Vilon from PX1 Research includes a third-party, ISO 17025 accredited Certificate of Analysis with raw RP-HPLC chromatograms, ESI-MS data, and endotoxin test results.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.