DSIP Molecular Weight, Sequence & CAS Reference

Chemical Profile & Primary Identifiers

Delta Sleep-Inducing Peptide (DSIP) is a non-apeptide originally isolated from the cerebral venous blood of rabbits induced into delta-wave sleep. As an endogenous regulatory peptide, it plays a key role in central nervous system research, particularly regarding neuroendocrine equilibrium, stress modulation, and slow-wave sleep architecture.

When sourcing DSIP 5mg vials for analytical or cell-culture assays, verified chemical identification is vital to ensure experimental reproducibility. The table below outlines the established chemical parameters for reference-grade DSIP.

Primary chemical specifications for synthesized DSIP: - Chemical Name: Delta Sleep-Inducing Peptide - CAS Registry Number: 62568-57-4 - IUPAC Name: L-tryptophyl-L-alanylglycylglycyl-L-aspartyl-L-alanyl-L-seryl-glycyl-L-glutamic acid - Molecular Formula: C35H48N10O15 - Monoisotopic Mass: 848.3202 Da - Average Molecular Weight: 848.81 g/mol - Counterion Options: Trifluoroacetate (TFA) or Acetate - Physical Appearance: White to off-white lyophilized powder

Amino Acid Sequence & Structural Architecture

The primary sequence of DSIP consists of nine amino acid residues: H-Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu-OH (single-letter code: WAGGDASGE). The structure features N-terminal tryptophan and C-terminal glutamic acid, producing an amphipathic peptide chain with distinct polar and hydrophobic domains.

The primary sequence lacks disulfide bridges, rendering its tertiary structure flexible in aqueous solution. Preclinical structural studies demonstrate that the N-terminal tryptophan (Trp1) is crucial for biological activity, while the central flexible motif (Gly3-Gly4) facilitates necessary conformational transitions when interacting with putative central nervous system binding sites.

Salt Form Impact on Net Peptide Content

Like most synthetic peptides produced via solid-phase peptide synthesis (SPPS), DSIP is purified using reverse-phase high-performance liquid chromatography (RP-HPLC) utilizing mobile phases containing trifluoroacetic acid (TFA). Consequently, the raw peptide material exists as a TFA salt, where basic nitrogen groups (such as the N-terminal amine) form ion pairs with TFA counterions.

Because TFA counterions and residual moisture contribute to total gross mass, the net peptide content (NPC) typically ranges between 75% and 85% of total dry mass. For precise quantitative in vitro assays, researchers must account for NPC to calculate accurate molar concentrations. Quantitative assays should refer to the batch-specific certificate of analysis (COA) to review elemental microanalysis (CHN) or quantitative amino acid analysis (AAA) data.

Preclinical Mechanisms & Research Applications

Preclinical investigations indicate that DSIP modulates central neuroendocrine axes and central EEG patterns. Early animal studies demonstrated that central administration of DSIP induces elevated electroencephalographic delta-wave activity, characteristic of deep, slow-wave sleep stages in mammalian models.

Beyond sleep architecture, preclinical models show that DSIP interacts with the hypothalamic-pituitary-adrenal (HPA) axis. In vitro and animal studies suggest that DSIP can attenuate acute stress-induced release of adrenocorticotropic hormone (ACTH) and corticosterone, indicating potential regulatory pathways in cellular stress responses and metabolic homeostasis during rest.

Comparative Analysis: Central Regulatory Peptides

Within neurochemical research, DSIP is evaluated alongside other synthetic and endogenous regulatory peptides targeting circadian rhythms, stress responses, and cognitive parameters. To review additional candidate compounds for your laboratory protocol, consult our complete catalog of research peptides.

When comparing neuroendocrine research compounds, DSIP (MW: 848.81 g/mol; sequence WAGGDASGE) functions via central delta-wave induction and stress-axis stabilization. In contrast, Epitalon 10mg (MW: 390.35 g/mol; sequence AEDG) is primary investigated for pineal gland regulation and telomerase activity, while Selank 5mg (MW: 751.9 g/mol; sequence TKPRPGP) acts as a heptapeptide analog of tuftsin evaluated for anxiolytic and neuroprotective mechanisms. Understanding these molecular mass and sequence distinctions is essential when designing comparative binding assays.

Solubility, Handling, and Reconstitution Guidelines

DSIP exhibits favorable solubility in aqueous buffers due to the presence of multiple hydrophilic residues (Asp5, Ser7, Glu9). For standard laboratory applications, reconstituting lyophilized DSIP in sterile bacteriostatic water, phosphate-buffered saline (PBS, pH 7.4), or sterile 0.9% sodium chloride yields a clear, colorless solution.

Researchers should avoid high-shear mechanical vortexing during dissolution; mild vessel inversion is recommended. To compute accurate volumetric additions for specific target concentrations in microplates or tissue cultures, utilize the laboratory reconstitution calculator prior to media preparation.

Physicochemical Properties & Reference Data

To assist laboratory researchers in setting up analytical instrumentation (e.g., LC-MS, HPLC, NMR), the following table summarizes the confirmed physical and chemical properties of synthetic DSIP.

Physicochemical Reference Values: - Isoelectric Point (pI): Calculated ~3.8 (acidic due to Asp and Glu side chains) - Hydrophobicity index: Low (-0.22 on Kyte-Doolittle scale) - Extinction Coefficient: 5,500 M⁻¹cm⁻¹ at 280 nm (driven by Trp1 residue) - Extinction Coefficient (205 nm): ~31,000 M⁻¹cm⁻¹ (backbone peptide bonds) - Solubilization Limit: >10 mg/mL in PBS (pH 7.4) - Recommended Storage (Lyophilized): -20°C, desiccated, protected from light - Recommended Storage (Reconstituted): 2°C to 8°C for short-term assays (<7 days); -80°C for long-term storage

Quality Assurance & Analytical Standards at PX1 Research

PX1 Research enforces strict quality control standards for all analytical compounds. Every lot of DSIP manufactured in our USA-based facilities undergoes rigorous testing in ISO 17025 accredited laboratories to ensure consistency across experimental trials.

Purity is verified using high-performance liquid chromatography (HPLC), guaranteeing high purity (typically ≥98.0%). Mass identity is confirmed via electrospray ionization mass spectrometry (ESI-MS). Furthermore, routine kinetic chromogenic LAL assays verify that bacterial endotoxin levels remain strictly controlled (<0.01 EU/mg), making our compounds suitable for sensitive cellular assays and preclinical models. For detailed documentation on our protocols, explore our central research library.