Research Context
- Stability and solubility assessments
- Cell-based sequence response assays
- Peptide–protein interaction studies
Molecular Structure and Properties
BPC-157 (Body Protection Compound-157) is a stable pentadecapeptide consisting of 15 amino acids with the sequence:Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. This sequence represents a partial fragment derived from human gastric juice proteins, specifically designed to maintain structural integrity under challenging laboratory conditions.
Key Molecular Characteristics:
- Molecular Formula: C62H98N16O22
- Molecular Weight: 1419.53 g/mol
- CAS Number: 137525-51-0
- Isoelectric Point (pI): Approximately 4.2
- Net Charge at pH 7.0: -2
- Hydrophobicity Index: Moderately hydrophilic
The pentadecapeptide exhibits remarkable stability due to its unique proline-rich regions that provide structural rigidity while maintaining solubility characteristics suitable for various research applications. The presence of three proline residues contributes to conformational constraints that enhance resistance to enzymatic degradation in laboratory environments.
Analytical Characterization Methods
Comprehensive analytical characterization of BPC-157 requires multiple complementary techniques to ensure structural integrity, purity, and stability for research applications.
High-Performance Liquid Chromatography (HPLC)
Reverse-phase HPLC serves as the primary analytical method for BPC-157 purity assessment. Typical conditions utilize C18 columns (4.6 × 250 mm, 5 μm) with acetonitrile-water gradients containing 0.1% TFA. Detection at 220 nm provides optimal sensitivity for peptide quantification.
Learn more about HPLC methods →Mass Spectrometry Analysis
ESI-MS and MALDI-TOF MS confirm molecular identity with expected [M+H]+ ion at m/z 1420.5. Fragmentation patterns provide sequence confirmation, while high-resolution MS distinguishes between closely related impurities and degradation products.
Explore MS techniques →NMR Spectroscopy for Structural Verification
1H NMR spectroscopy in D2O provides detailed structural information, with characteristic signals for proline residues appearing at δ 3.6-4.4 ppm. 2D NMR techniques (COSY, TOCSY) enable complete assignment of peptide resonances and confirmation of sequence integrity.
- • Solvent: D2O with DSS internal standard
- • Temperature: 298K for optimal resolution
- • Acquisition time: 16-32 hours for complete dataset
BPC-157 Stability Studies and Storage Requirements
BPC-157 demonstrates exceptional stability compared to many peptides, attributed to its unique sequence composition and structural features. Comprehensive stability studies inform optimal storage and handling protocols for research applications.
Accelerated Stability Testing Results
| Storage Condition | Time Period | Purity Retention | Notes |
|---|---|---|---|
| -20°C, dry | 24 months | >99% | No degradation observed |
| 2-8°C, dry | 12 months | 98.5-99.2% | Minimal deamidation |
| Room temp, dry | 3 months | 96.8-98.1% | Slight oxidation observed |
| 2-8°C, reconstituted | 7 days | 97.2-98.6% | Sterile conditions |
Critical Storage Parameters
- Primary Storage: -20°C or below, sealed in original vials with desiccant
- Working Stocks: 2-8°C for short-term use (<30 days)
- Humidity Control: Relative humidity <30% to prevent moisture uptake
- Light Protection: Store in amber vials or protect from direct light
- pH Considerations: Maintain neutral pH (6.5-7.5) in solution
Laboratory Handling Protocols
Proper handling of BPC-157 in laboratory environments requires adherence to established protocols that maintain peptide integrity while ensuring researcher safety and experimental reproducibility.
Reconstitution Protocol
- Allow vial to reach room temperature (15-20 minutes)
- Add sterile water or appropriate buffer slowly along vial wall
- Gently swirl without vortexing to dissolve completely
- Prepare 1-10 mg/mL working concentrations as needed
- Filter through 0.22 μm membrane if sterility required
Safety Considerations
- • Use appropriate PPE (gloves, lab coat, safety glasses)
- • Work in well-ventilated areas or fume hoods
- • Avoid direct skin contact with dry powder
- • Use proper waste disposal procedures
- • Maintain detailed handling logs
Buffer System Compatibility
BPC-157 demonstrates excellent compatibility with common laboratory buffer systems, maintaining stability across a range of pH values and ionic strengths.
Optimal Buffers:
- • PBS (pH 7.4)
- • HEPES (pH 7.0-7.5)
- • Tris-HCl (pH 7.0-8.0)
Compatible Additives:
- • 0.1% BSA (stabilizer)
- • Glycerol (5-20%)
- • Trehalose (1-5%)
Avoid:
- • Extreme pH (<3.0, >9.0)
- • High salt (>1M NaCl)
- • Oxidizing agents
Quality Control and Testing Specifications
Rigorous quality control testing ensures BPC-157 meets the highest standards for research applications. Multiple analytical methods provide comprehensive characterization of each batch.
Standard QC Testing Panel
Chemical Analysis:
- HPLC Purity:≥99%
- Water Content:<8%
- TFA Content:<3%
- Acetate Content:<15%
- Peptide Content:≥80%
Physical Analysis:
- Appearance:White powder
- Molecular Weight:1419.53 ± 1.0
- Solubility:>1 mg/mL
- pH (1% solution):6.0-7.5
- Heavy Metals:<10 ppm
Advanced Characterization Methods
Amino Acid Analysis (AAA)
Confirms sequence composition through quantitative analysis of constituent amino acids following acid hydrolysis. Results must match theoretical composition within ±10%.
Peptide Mapping
Enzymatic digestion followed by LC-MS analysis provides sequence verification and identifies potential sequence variants or modifications.
Circular Dichroism Spectroscopy
Assesses secondary structure integrity and conformational stability under various solution conditions relevant to research applications.
Research Applications and Use Cases
BPC-157's unique structural properties and stability characteristics make it valuable for diverse research applications in laboratory settings. Its sequence-specific interactions provide opportunities for studying peptide behavior and molecular mechanisms.
Cell Culture Studies
Investigation of peptide-cell interactions, uptake mechanisms, and cellular response pathways in various cell lines. Concentration ranges typically 1-1000 μM for in vitro studies.
Protein Interaction Assays
Surface plasmon resonance, fluorescence polarization, and other biophysical methods for characterizing binding interactions with target proteins and receptors.
Stability Research
Comparative studies of peptide degradation pathways, formulation optimization, and development of improved storage and handling protocols.
Experimental Considerations
Concentration Guidelines:
- • Stock solutions: 1-10 mg/mL
- • Working concentrations: 1-1000 μM
- • IC50 determinations: 0.1-100 μM range
- • Binding assays: nM to μM range
Control Requirements:
- • Vehicle controls (buffer/solvent only)
- • Scrambled sequence controls
- • Positive controls (known peptides)
- • Time-course controls
View Product Details
Access full specifications, pricing, and ordering information
RUO Disclaimer
All Biovera products are for laboratory research use only (RUO).
Not for human, diagnostic, therapeutic, or veterinary use. Not evaluated or approved by the TGA or Medsafe.