DSIP 10MG
$40.00
Research-grade DSIP nonapeptide. 10mg lyophilized powder for laboratory applications.
~99% HPLC purity.
Third-Party tested:
DSIP-10MG
Description
CAS Number: 62568-57-4
Molecular Formula: C₃₅H₄₈N₁₀O₁₅
Molecular Weight: 848.81 g/mol
Sequence: Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu
Alternative Names: Delta Sleep-Inducing Peptide, DSIP
Form: Lyophilized powder (not reconstituted)
Purity: ~99% HPLC
Storage: Store at -20°C. Protect from light and moisture.
Vial: 3mL sealed vial with flip-top cap
Content: 10mg per vial
FULL PRODUCT DESCRIPTION:
DSIP Research Peptide (10mg)
Peptide Minds offers high-purity Delta Sleep-Inducing Peptide (DSIP) manufactured exclusively for laboratory research applications. This nonapeptide is supplied as a lyophilized powder with verified quality specifications through comprehensive third-party testing.
Molecular Profile
DSIP is a nonapeptide with the amino acid sequence Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu and a molecular weight of 848.81 g/mol. Originally isolated from rabbit cerebral venous blood during laboratory research in the 1970s by Swiss researchers investigating endogenous peptide factors.
The peptide’s structure consists of nine amino acids with tryptophan at the N-terminus and glutamic acid at the C-terminus. This sequence exhibits chemical stability compared to many bioactive peptides, with the free acid form (rather than amidated C-terminus) contributing to its chemical characteristics. The presence of glycine residues at positions 3 and 4 provides conformational flexibility, while the tryptophan residue contributes to the molecule’s spectroscopic properties.
DSIP does not share structural homology with other known neuropeptide families, positioning it as a unique molecular entity within peptide research. Its distinctive sequence and lack of similarity to opioid, somatostatin, or other classical neuropeptide families have made it a subject of ongoing investigation in neuroscience research contexts.
Research Applications
DSIP has been investigated across multiple research domains since its initial discovery. Laboratory studies have examined its interactions with various neurotransmitter systems, receptor binding characteristics, and cellular signaling pathways in experimental models.
Research applications have included investigations into circadian rhythm mechanisms, neuroendocrine signaling pathways, cellular stress response systems, and central nervous system receptor interactions. Studies have utilized DSIP in rodent models, cell culture systems, and ex vivo tissue preparations to characterize its pharmacological properties and receptor binding profiles.
In preclinical research contexts, DSIP has been examined for its biochemical interactions including hormone receptor binding assays, neurotransmitter release measurements in cell cultures, and cellular signaling pathway activation studies. Researchers have investigated its distribution in brain tissue, cerebrospinal fluid concentrations following administration, and interactions with various receptor systems in laboratory models.
The peptide serves as a research tool for examining peptidergic signaling mechanisms, receptor-ligand interactions, and neuroendocrine pathway mapping. Its unique structure and binding properties have positioned it as a valuable compound for studying peptide chemistry in laboratory settings.
Quality Specifications
Each vial contains lyophilized powder with the following quality parameters:
- Purity: ~99% by HPLC analysis
- Content: 10mg DSIP per vial
- Form: Sterile lyophilized powder
- Reconstitution: Supplied in powder form; requires reconstitution with appropriate solvent for research use
- Third-Party Testing: Each batch undergoes independent laboratory analysis for purity, identity, and endotoxin content
Storage and Handling
Store unopened vials at -20°C protected from light and moisture. DSIP in lyophilized form demonstrates chemical stability when stored under proper conditions. Once reconstituted, peptide solutions should be stored at 2-8°C and used within the timeframe established by stability studies for your specific research protocol.
Avoid repeated freeze-thaw cycles as these can degrade peptide integrity. Handle using aseptic technique in appropriate laboratory settings. Reconstitute with sterile water, bacteriostatic water, or phosphate-buffered saline depending on experimental requirements.
Important Research Use Information
This product is manufactured and supplied exclusively for laboratory research purposes. It is not intended for human consumption, veterinary use, or any clinical applications. Researchers should follow all applicable institutional guidelines, biosafety protocols, and regulatory requirements when handling research peptides.
RESEARCH BACKGROUND: DSIP IN LABORATORY PEPTIDE RESEARCH
Discovery and Historical Context
Delta Sleep-Inducing Peptide was first isolated in 1977 by Schoenenberger and Monnier from rabbit cerebral venous blood during laboratory experiments. The initial characterization involved bioassay-guided fractionation of blood samples using techniques including ion exchange chromatography, gel filtration, and amino acid sequencing to elucidate the nonapeptide structure.
Subsequent synthesis of DSIP through solid-phase peptide synthesis enabled controlled research applications and confirmed the synthetic peptide structure. Following its discovery, DSIP became a subject of investigation across multiple research disciplines including neuroscience, endocrinology, and peptide chemistry research.
Structural Characteristics and Peptide Chemistry
The nonapeptide sequence Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu contains several notable structural features. The N-terminal tryptophan residue provides an aromatic chromophore useful for spectroscopic detection and quantification through UV absorbance measurements at 280 nm.
The presence of two glycine residues (positions 3-4 and position 8) introduces conformational flexibility in the peptide backbone. Glycine, lacking a side chain beyond a single hydrogen atom, permits greater rotational freedom compared to other amino acids, allowing DSIP to adopt multiple conformations in solution.
The acidic residues (aspartic acid at position 5 and glutamic acid at position 9) provide negative charges at physiological pH, contributing to the peptide’s overall charge distribution and aqueous solubility. The serine residue at position 7 provides a polar hydroxyl group capable of hydrogen bonding. Alanine residues at positions 2 and 6 contribute hydrophobic character while maintaining relatively small side chains.
Unlike many bioactive peptides that require C-terminal amidation, DSIP naturally occurs with a free carboxyl terminus. This structural feature distinguishes it from peptide families where C-terminal amidation is required for receptor binding.
Receptor Binding and Molecular Interactions
Laboratory research has investigated DSIP’s binding interactions with various receptor systems. Unlike peptides with well-defined receptor families (such as opioid receptors or specific GPCR families), DSIP’s molecular targets remain a subject of ongoing research investigation.
Studies have examined potential binding to various neurotransmitter receptor systems including GABAergic, serotonergic, and dopaminergic receptors using radioligand binding assays. Research has investigated interactions with intracellular signaling cascades including calcium mobilization, cAMP production, and kinase activation pathways in cell culture models.
The peptide’s distribution following administration has been studied using radiolabeled DSIP in animal models. Research indicates tissue distribution patterns and brain penetration characteristics following peripheral administration, with uptake measured through autoradiography and tissue sampling techniques.
Neuroendocrine Research Applications
Laboratory studies have investigated DSIP’s interactions with various endocrine receptor systems. Research in experimental animals has examined binding to hypothalamic-pituitary hormone receptors, including corticotropin receptors, growth hormone receptors, and thyroid hormone receptors using in vitro binding assays.
Studies have measured hormone concentrations in biological samples following DSIP administration in rodent models, utilizing radioimmunoassay and ELISA techniques to quantify circulating hormone levels. Research protocols have examined temporal patterns of hormone secretion, receptor occupancy measurements, and dose-response relationships in controlled laboratory settings.
Investigations have employed cell culture systems to examine DSIP’s effects on hormone-secreting cell lines, measuring secretion rates, receptor expression changes, and intracellular signaling activation. These in vitro systems provide controlled environments for examining direct cellular interactions independent of systemic factors.
Circadian Biology and Neuroscience Research
Laboratory research has utilized DSIP in studies examining circadian timing mechanisms and neural signaling pathways. Electroencephalographic (EEG) recording studies in animal models have measured electrical activity patterns in brain tissue following DSIP administration.
Research has examined DSIP’s distribution in brain regions involved in circadian regulation using immunohistochemistry, in situ hybridization, and autoradiography techniques. Studies have measured peptide concentrations in cerebrospinal fluid samples and brain tissue homogenates at different circadian time points.
The peptide has served as a research tool for investigating peptidergic signaling in neural circuits, examining receptor localization in brain tissue, and studying peptide transport mechanisms across biological membranes. Research applications include receptor binding studies, neural activity recording, and peptide pharmacokinetic investigations.
Cellular Signaling Research
Laboratory investigations have examined DSIP’s interactions with various cellular signaling pathways. Research using cultured cell systems has measured intracellular calcium concentrations using fluorescent calcium indicators, cAMP levels through radioimmunoassay or ELISA, kinase phosphorylation states using Western blot analysis, and gene expression changes through quantitative PCR.
Studies have investigated DSIP’s influence on receptor expression levels, examining changes in mRNA transcription and protein expression in response to peptide exposure. Research has employed receptor knockout cell lines and pharmacological antagonists to probe specific signaling mechanisms and pathway interactions.
Experimental Methodologies in DSIP Research
Research utilizing DSIP employs diverse methodological approaches depending on specific questions being addressed. Common experimental paradigms include receptor binding assays using radiolabeled peptide, cell culture signaling studies measuring second messenger production, animal model pharmacokinetic studies tracking peptide distribution, and in vitro receptor activation assays using fluorescent or luminescent reporters.
Dosing in animal research has varied from microgram to milligram quantities, with administration routes including intraperitoneal injection, subcutaneous injection, intracerebroventricular delivery, and intravenous infusion. Pharmacokinetic studies measure plasma concentrations, tissue distribution, and elimination half-life using analytical techniques.
Analytical methods for DSIP detection and quantification include HPLC-based separation with UV or fluorescence detection, radioimmunoassay for biological samples, mass spectrometry for structural confirmation, and spectrophotometric quantification based on tryptophan absorbance. These techniques enable precise measurement of peptide concentrations in experimental samples.
Contemporary Research Directions
Current research applications of DSIP include investigating peptide-receptor interactions using surface plasmon resonance and isothermal titration calorimetry, examining peptide stability in biological matrices through degradation kinetic studies, studying blood-brain barrier transport mechanisms using in vitro and in vivo permeability models, characterizing cellular uptake pathways through fluorescently-labeled peptide tracking, and investigating structure-activity relationships through systematic amino acid substitution.
Research continues to utilize DSIP as a molecular probe for examining peptidergic signaling systems, studying receptor pharmacology, investigating peptide chemistry, and characterizing biochemical pathways in laboratory settings.
Analytical Characterization and Quality Control
High-quality DSIP for research applications requires rigorous analytical characterization. HPLC analysis confirms purity by separating DSIP from potential impurities including truncated sequences, deletion peptides, synthesis by-products, and degradation products. Analytical HPLC achieves resolution of peptides differing by a single amino acid.
Mass spectrometry provides molecular weight confirmation, verifying that the synthesized peptide matches the expected mass for the Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu sequence (848.81 g/mol). High-resolution mass spectrometry detects impurities or modifications that might affect experimental results.
Additional quality control measures include endotoxin testing using Limulus Amebocyte Lysate (LAL) assay to quantify bacterial endotoxin levels, amino acid analysis to confirm sequence composition, peptide content assay to verify actual peptide concentration, and water content determination by Karl Fischer titration.
Proper storage conditions maintain DSIP chemical integrity. Lyophilized peptide stored at -20°C with desiccation demonstrates long-term stability. Once reconstituted, chemical degradation processes including tryptophan oxidation, peptide bond hydrolysis, and deamidation can occur, particularly at elevated temperatures or non-optimal pH values.
Structure-Activity Relationship Studies
Research has employed synthetic analogs of DSIP to investigate structure-activity relationships. Studies have examined N-terminal modifications including tryptophan substitution or deletion, glycine residue replacements to reduce conformational flexibility, acidic residue modifications (Asp, Glu) to alter charge properties, and C-terminal modifications including amidation or extension.
These analog studies provide insights into which structural features are essential for receptor binding, which regions can tolerate modification without loss of binding affinity, and how chemical modifications affect peptide stability and pharmacokinetic properties. Such research contributes to understanding peptide structure-function relationships in broader peptide chemistry contexts.
Peptide Synthesis and Chemical Modification
DSIP synthesis typically employs solid-phase peptide synthesis (SPPS) using Fmoc chemistry. The synthesis proceeds through stepwise addition of protected amino acids to a growing peptide chain attached to a solid resin support. Following synthesis, the peptide is cleaved from the resin, deprotected, and purified through preparative HPLC.
Research applications may employ chemically modified DSIP variants including fluorescently-labeled derivatives for cellular uptake studies, biotinylated versions for pull-down assays and protein interaction studies, radiolabeled peptides for pharmacokinetic and distribution research, and PEGylated forms for examining effects of molecular weight on pharmacological properties.
These modified peptides serve as research tools for examining peptide pharmacology, cellular localization, receptor binding kinetics, and biochemical interactions in controlled laboratory settings.
REFERENCES
- Schoenenberger GA, Monnier M. Characterization of a delta-electroencephalogram (-sleep)-inducing peptide. Proc Natl Acad Sci U S A. 1977;74(3):1282-1286. https://doi.org/10.1073/pnas.74.3.1282
- Graf MV, Kastin AJ. Delta-sleep-inducing peptide (DSIP): a review. Neurosci Biobehav Rev. 1984;8(1):83-93. https://doi.org/10.1016/0149-7634(84)90037-7
- Iyer KS, McCann SM. Delta sleep inducing peptide (DSIP) stimulates the release of LH but not FSH via a hypothalamic site of action in the rat. Brain Res Bull. 1987;19(5):535-538. https://doi.org/10.1016/0361-9230(87)90067-8
- Kovalzon VM, Strekalova TV. Delta sleep-inducing peptide (DSIP): a still unresolved riddle. J Neurochem. 2006;97(2):303-309. https://doi.org/10.1111/j.1471-4159.2006.03693.x
REGULATORY COMPLIANCE STATEMENT
FOR RESEARCH USE ONLY. NOT FOR HUMAN CONSUMPTION OR VETERINARY USE.
This product is sold exclusively for laboratory research applications conducted by qualified researchers in appropriate institutional settings. It is not approved by the FDA for human use, clinical applications, or any diagnostic or therapeutic purposes. Purchasers assume full responsibility for compliance with all applicable federal, state, and local regulations governing the purchase, possession, and use of research peptides.
This product is not intended to diagnose, treat, cure, or prevent any disease in humans or animals. It is the sole responsibility of the purchaser to ensure proper handling, storage, and use in accordance with institutional biosafety protocols and regulatory requirements.
ABOUT PEPTIDE MINDS
Peptide Minds provides high-purity research peptides manufactured to rigorous quality standards for laboratory applications. Every batch undergoes third-party laboratory testing for purity (HPLC), identity (mass spectrometry), and endotoxin content. We maintain transparent quality documentation with batch-specific Certificates of Analysis available upon request.
Our commitment to the research community includes:
- ≥99% peptide purity by HPLC
- Comprehensive third-party testing
- Batch traceability with documented CoA
- Proper cold-chain shipping with ice packs
- Technical support for research applications
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