Epithalon Molecular Weight, Sequence & CAS Reference

Introduction to Epithalon (AEDG) as a Synthetic Bioregulator

Epithalon (also known as Epitalon or AEDG) is a synthetic tetrapeptide modeled after Epithalamin, a natural polypeptide extract derived from the pineal gland. Classified scientifically as a short-chain peptide bioregulator, Epithalon consists of four amino acid residues arranged in a specific sequence designed to interact with genomic DNA and transcriptional machinery in cell-free and cell-based research systems.

In preclinical settings, researchers study Epithalon primarily for its observed interactions with telomerase activity, chromatin structure, and pineal gene expression. Because small oligopeptides can exert regulatory effects at low nanomolar concentrations, maintaining exact structural fidelity and quantitative mass accuracy is essential when conducting laboratory trials. Researchers sourcing Epithalon for laboratory use must rely on precise chemical parameters to calculate stoichiometric ratios, prepare working stock solutions, and ensure reproducible experimental outcomes across diverse research projects.

As part of our commitment to transparency and chemical accuracy, PX1 Research maintains a full library of analytical metrics for our entire catalog of research peptides. This reference document outlines the physical, chemical, and structural identifiers for Epithalon, establishing the benchmark standards used in high-throughput analytical assays, mass spectrometry, and cell culture protocols.

Primary Amino Acid Sequence and Structural Representation

The primary structure of Epithalon is defined by a short linear tetrapeptide sequence. Synthesized via solid-phase peptide synthesis (SPPS), the compound features L-configuration amino acid residues connected by standard alpha-peptide bonds from the N-terminus to the C-terminus.

The standardized amino acid sequence designations for Epithalon are as follows:

• One-Letter Code: AEDG • Three-Letter Code: H-Ala-Glu-Asp-Gly-OH • Full Chemical Name: L-alanyl-L-alpha-glutamyl-L-alpha-aspartyl-glycine

The spatial arrangement of the functional side chains—specifically the carboxylic acid groups present on the glutamate (Glu) and aspartate (Asp) residues—plays a critical role in the peptide's ionic interactions and metal-cation chelating potential in aqueous solutions. During automated Edman degradation or tandem mass spectrometry (MS/MS) sequencing, the fragmentation pattern yields characteristic b- and y-ion series corresponding to sequence-specific cleavage at the peptide backbone amide bonds, confirming the exact AEDG ordering without sequence inversion or amino acid deletion contaminants.

Molecular Weight, Empirical Formula, and Mass Spectrometry

Calculating accurate working concentrations for in vitro assays requires a precise understanding of the molecular mass of the target peptide. Epithalon possesses a relatively low molecular weight compared to typical globular proteins, facilitating high solubility and straightforward mass verification via electrospray ionization mass spectrometry (ESI-MS).

Key chemical and mass metrics for the free-base form of Epithalon include:

• Empirical Formula: C14 H22 N4 O9 • Monoisotopic Mass: 390.1387 Da • Average Molecular Weight: 390.35 g/mol

When analyzing Epithalon via High-Performance Liquid Chromatography coupled with Mass Spectrometry (HPLC-MS), the primary molecular ion peak observed under positive ionization mode corresponds to the protonated species [M+H]+ at m/z 391.15. Secondary adducts, such as sodium [M+Na]+ at m/z 413.13 or potassium [M+K]+ at m/z 429.10, may appear depending on the mobile phase modifiers and salt content of the sample matrix. Laboratory investigators must distinguish between the free-base theoretical mass ($390.35\text{ g/mol}$) and the gross formula weight, which incorporates variable amounts of associated water (hydration state) and non-covalent counterions.

CAS Registry Number and Chemical Identifiers

To ensure precise tracking across chemical databases, electronic laboratory notebooks, and procurement registries, Epithalon is indexed under several internationally recognized chemical identification systems.

Standard identifiers for Epithalon include:

• CAS Registry Number: 307297-39-8 • PubChem CID: 219462 • ChemSpider ID: 190186 • IUPAC Name: (2S)-2-[[(2S)-2-[[(2S)-2-aminopropanoyl]amino]-4-carboxybutanoyl]amino]-4-[[(2-hydroxy-2-oxoethyl)amino]-4-oxobutanoic acid

In commercial and academic registries, the CAS number 307297-39-8 specifically designates the L-stereoisomeric form of the AEDG tetrapeptide. Analytical validation requires matching the CAS-indexed structure against nuclear magnetic resonance (1H-NMR and 13C-NMR) spectra to verify stereochemical purity, ensuring that no D-amino acid racemization occurred during solid-phase chain elongation.

Salt Counterions, TFA Content, and Net Peptide Quantification

Synthetic peptides generated via solid-phase synthesis undergo cleavage from the solid resin support using trifluoroacetic acid (TFA). Consequently, raw peptide preparations typically exist as trifluoroacetate salts, where basic amino groups (such as the N-terminal amine) carry a positive charge balanced by TFA counterions (CF3COO-).

The presence of salt counterions and residual moisture impacts the total mass of the lyophilized powder. When weighing a dry peptide sample, the total gross mass consists of three components:

1. Net Peptide Weight: The actual weight of the AEDG peptide molecules. 2. Counterion Mass: Trifluoroacetate (TFA, MW ~114 g/mol) or Acetate (MW ~59 g/mol) counterions. 3. Residual Water: Bound moisture retained following the freeze-drying process (typically 2–8%).

The 'Net Peptide Content' (or Net Peptide Purity) represents the percentage of the gross lyophilized mass composed solely of the peptide sequence. For standard research-grade Epithalon, net peptide content typically ranges from 80% to 90%. For example, if a vial contains 10.0 mg of gross lyophilized powder with an 85% net peptide content, the actual amount of active AEDG peptide is 8.5 mg. Researchers preparing precise molarity standards for quantitative bioassays must adjust their reconstitution volumes based on the net peptide content reported on the lot-specific Certificate of Analysis (COA) rather than relying on gross powder weight alone.

Preclinical Research Focus: Telomerase Maintenance and Circadian Models

In academic literature, Epithalon is studied primarily as an epigenetic modulator and pineal-stage bioregulator. Preclinical investigation centers on several key biochemical axes:

• Telomerase Activation: In vitro assays utilizing human somatic cell cultures and senescence models demonstrate that exposure to Epithalon induces telomerase catalytic subunit (TERT) expression. Preclinical studies suggest this upregulation promotes telomere elongation and delays morphological signs of cellular senescence.

• Chromatin Remodeling: Nuclear binding assays indicate that short peptides like AEDG can interact directly with the promoter regions of specific genes, facilitating histone modifications and altering local chromatin accessibility.

• Melatonin Regulation and Circadian Rhythm: In animal models involving aging rodents and non-human primates, administration of pineal-derived short peptides was observed to restore night-time melatonin secretion patterns, suggesting a regulatory role in pineal gland homeostasis and circadian transcriptomics.

All investigations involving Epithalon are conducted strictly in cell culture (in vitro) or rodent/preclinical models. The compound is made available strictly to advance foundational biochemical research regarding telomere dynamics, genomic stability, and age-associated gene expression changes.

Comparative Structural Analysis: Epithalon vs. Related Bioregulators

Epithalon belongs to a broader family of short-chain peptide bioregulators developed to target specific tissue pathways. Comparing the molecular weights, sequences, and charge profiles of these compounds illustrates the structural specificity inherent in bioregulatory peptide design.

When evaluating structural parameters across this class, scientists frequently compare Epithalon with other tissue-specific short peptides:

• Epithalon (AEDG): Molecular weight of $390.35\text{ g/mol}$, featuring two acidic residues (Glu, Asp) that confer a net negative charge at physiological pH (pH 7.4). Studied primarily in pineal and telomerase models.

• Pinealon: A tripeptide with the sequence Glu-Asp-Arg (EDR) and a molecular weight of $432.43\text{ g/mol}$. Unlike Epithalon, Pinealon incorporates a basic arginine residue, altering its overall charge profile and target interaction kinetics in central nervous system cellular models.

• Thymogen: A synthetic dipeptide with the sequence Glu-Trp (EW) and a molecular weight of $333.34\text{ g/mol}$. Studied predominantly in immunomodulatory and thymic cell line assays.

These structural variations emphasize how single amino acid substitutions or deletions drastically alter molecular weight, iso-electric point (pI), and functional specificity across preclinical peptide research.

Solubility Profile and Laboratory Reconstitution Guidance

Epithalon contains hydrophilic amino acid side chains (glutamic acid, aspartic acid, and glycine), granting it high solubility in polar aqueous solvents. Lyophilized Epithalon readily dissolves in standard laboratory buffers without requiring organic co-solvents such as dimethyl sulfoxide (DMSO) or ethanol.

Standard solubilization practices for analytical experiments involve:

• Reconstitution Media: Sterile Deionized Water ($ddH_2O$) or Phosphate-Buffered Saline (PBS, pH 7.4) are optimal for preparing stock solutions.

• Concentration Range: Typical stock concentrations range from $1.0\text{ mg/mL}$ to $10.0\text{ mg/mL}$. Violent agitation or excessive vortexing should be avoided; gentle manual swirling or short low-speed shaking prevents foam formation and potential peptide aggregation.

• Molar Calculations: To calculate accurate concentration metrics accounting for salt weight and net peptide percentage, researchers should utilize our interactive peptide reconstitution calculator.

Once reconstituted in aqueous media, aliquots should be prepared immediately to avoid repeated freeze-thaw cycles, which can induce physical degradation or adsorption to standard glass or plastic container surfaces.

Storage Conditions and Lyophilized Stability

Maintaining structural integrity over extended periods requires proper physical storage conditions to prevent hydrolytic degradation, oxidation, or beta-elimination reactions.

Recommended handling and storage protocols for research-grade Epithalon include:

• Lyophilized Powder Storage: Store at $-20^\circ\text{C}$ for short-to-medium term storage (up to 12 months) or at $-80^\circ\text{C}$ for long-term preservation. Protect vials from light and atmospheric moisture.

• Handling Desiccated Vials: Prior to opening, allow the lyophilized vial to equilibrate to room temperature inside a desiccator cabinet. This prevents room moisture from condensing onto the cold peptide powder, which can accelerate hydrolytic cleavage.

• Reconstituted Solution Stability: Liquid stock solutions dissolved in sterile PBS or $ddH_2O$ should be stored at $-20^\circ\text{C}$ or $-80^\circ\text{C}$ in single-use polypropylene micro-centrifuge tubes. Liquid aliquots maintained at $2^\circ\text{C}$ to $8^\circ\text{C}$ should be utilized within 7 to 14 days.

PX1 Research Quality Assurance, HPLC Verification, and Endotoxin Standards

To supply the scientific community with reliable research materials, PX1 Research applies rigid analytical verification to every lot of Epithalon synthesized. All products are manufactured in state-of-the-art, GMP-compliant facilities within the USA and dispatched directly from our CA and AZ facilities.

Every batch undergoes independent validation in an ISO 17025 accredited laboratory, featuring:

• HPLC Purity Determination: Reverse-phase HPLC (RP-HPLC) analysis ensuring chemical purity equal to or exceeding 98.0%.

• Mass Spectrometry Identity: Electrospray ionization mass spectrometry (ESI-MS) to verify molecular weight ($390.35\text{ g/mol}$) and confirm the absence of truncated peptide impurities.

• Endotoxin Quantitation: Limulus Amebocyte Lysate (LAL) testing to confirm endotoxin levels remain strictly below $0.1\text{ EU/mg}$, making the compound suitable for sensitive cell culture and in vitro biochemical models.

Institutional laboratories requiring bulk quantities for extended experimental series can establish dedicated research supply arrangements through our wholesale peptide portal.