- Document
- CS-BPC157
- Type
- Compound handling sheet
- Revised
- Sources checked
- Bands
- −20 °C
BPC-157 Handling Sheet
Also known as Body Protection Compound 157, PL 14736, bepecin
A 15-residue, proline-rich, acidic peptide with no methionine, cysteine or tryptophan. Chemically one of the more robust research peptides; the main solution risk is slow aspartate isomerization.
Identity
- Sequence
GEPPPGKPADDAGLV- Formula
- C62H98N16O22
- Molecular weight
- 1419.5 g/mol (average)
- Usual supplied form
- Lyophilized powder, often as acetate or TFA salt
- Record
- PubChem
Formula and weight are for the free peptide. Salt forms (acetate, TFA) weigh more; use the figure on the lot's COA.
Storage & sensitivity
- Oxidation
- Low
- Light
- Low
- Moisture
- Moderate
Some compound data exists; the rest follows general peptide chemistry.
Bench card
- Store sealed powder at −20 °C with desiccant; equilibrate before opening.
- No Met, Cys or Trp, so oxidation and light risk are low compared with most peptides.
- Net charge about −2 at neutral pH; it usually dissolves readily in water.
- Asp-Asp and Asp-Ala sites can isomerize slowly in solution, faster at neutral to basic pH.
- Freeze single-use aliquots of solutions; do not refreeze.
Handling-relevant features
| Feature | Why it matters for handling |
|---|---|
| No Met, Cys or Trp | Removes the main oxidation and photo-oxidation sites |
| Asp10-Asp11-Ala12 | Aspartate can isomerize through a succinimide; slower than an Asp-Gly site but not negligible in warm, neutral solution |
| Four prolines (P3, P4, P5, P8) | Proline-rich stretches are relatively rigid and resistant to many proteases |
| Net charge about −2 (E2, D10, D11, C-terminus vs K7, N-terminus) | Acidic peptide: water or a dilute ammonium bicarbonate solution are typical first choices |
| Hydrophobic C-terminus (A-G-L-V) | Modest adsorption risk at low concentration; use low-binding tubes for dilute solutions |
What it is
BPC-157 is a synthetic 15-amino-acid peptide (Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) described by Sikiric and colleagues as a partial sequence of a protein found in gastric juice. Most of the published literature comes from a single research group and is preclinical.
Stability profile
The sequence lacks the residues most associated with oxidation (Met, Cys, Trp) and has no Asn or Gln to deamidate. Its originators describe it as stable in gastric juice, and a 2022 pharmacokinetic study by He and colleagues developed analytical methods for it in biological samples. Neither source is a formal shelf-life study of research material, so the storage advice below follows standard practice for a robust, acidic short peptide.
Storage
| Form | Recommended | Notes |
|---|---|---|
| Sealed powder | −20 °C | With desiccant; 2–8 °C acceptable for short holds |
| Solution, days | 2–8 °C | Sterile, slightly acidic to neutral |
| Solution, longer | −20 °C or colder | Single-use aliquots |
Dissolving
With a net charge of about −2 at neutral pH and a short length, BPC-157 usually dissolves in sterile water. If it does not, a dilute ammonium bicarbonate solution is the conventional next step for an acidic peptide. See Solvent Selection.
Analytical notes
Expected [M+H]+ is about m/z 1420 (average), with [M+2H]2+ near m/z 710.8. A +16 Da peak would be unusual given the sequence and is worth questioning. Aspartate isomers can elute close to the main peak on reversed-phase HPLC.
References
- Sikiric P, Seiwerth S, Rucman R, et al. Stable gastric pentadecapeptide BPC 157: novel therapy in gastrointestinal tract. Curr Pharm Des. 2011;17(16):1612–1632. PubMed
- He L, Feng D, Guo H, et al. Pharmacokinetics, distribution, metabolism, and excretion of body-protective compound 157, a potential drug for treating various wounds, in rats and dogs. Front Pharmacol. 2022;13:1026182. PubMed
- Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: succinimide-linked reactions that contribute to protein degradation. J Biol Chem. 1987;262(2):785–794. PubMed
- Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27(4):544–575. DOI
- Kristensen K, Henriksen JR, Andresen TL. Adsorption of cationic peptides to solid surfaces of glass and plastic. PLoS One. 2015;10(5):e0122419. DOI
This sheet covers laboratory storage and handling of research material only. It does not describe use in humans or animals, and the supplier's datasheet for your lot takes priority.