BPC-157 is one of the most talked-about research peptides, and also one of the most misunderstood. It is a short synthetic peptide whose amino acid sequence is taken from a protein found in gastric juice. In the lab it is studied for the way it interacts with signaling pathways tied to tissue repair and blood vessel formation. Here is a plain look at what it actually is.
What is BPC-157?
BPC-157 is a pentadecapeptide, which simply means a peptide made of 15 amino acids. The name stands for "Body Protection Compound," and the sequence is derived from a larger protein present in the stomach. It is produced synthetically for research through solid-phase peptide synthesis rather than extracted from tissue. Its CAS number is 137525-51-0 and its molecular formula is C62H98N16O22, with a molecular weight near 1419 g/mol. If the difference between a short peptide like this and a full protein is unclear, our note on amino acids, peptides, and proteins covers it.
Where does the sequence come from?
The BPC-157 sequence corresponds to a fragment of a protective protein identified in gastric juice. That origin is part of why it draws attention in research: peptides that stay intact in an acidic environment are interesting to study, and much of the early literature looked at BPC-157 in exactly that context. The version used in labs today is fully synthetic and characterized by its certificate of analysis rather than by its source.
The BPC-157 amino acid sequence
A pentadecapeptide has fifteen residues. In BPC-157 they run, N-terminus to C-terminus, in three-letter code:
Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val
In one-letter code the same chain is GEPPPGKPADDAGLV, and the free-acid form is written H-GEPPPGKPADDAGLV-OH. Both notations are registered synonyms on the PubChem record, so either can be used to confirm that a listing describes the same molecule.
| Position | Residue | Code | Position | Residue | Code |
|---|---|---|---|---|---|
| 1 | Glycine | Gly / G | 9 | Alanine | Ala / A |
| 2 | Glutamic acid | Glu / E | 10 | Aspartic acid | Asp / D |
| 3 | Proline | Pro / P | 11 | Aspartic acid | Asp / D |
| 4 | Proline | Pro / P | 12 | Alanine | Ala / A |
| 5 | Proline | Pro / P | 13 | Glycine | Gly / G |
| 6 | Glycine | Gly / G | 14 | Leucine | Leu / L |
| 7 | Lysine | Lys / K | 15 | Valine | Val / V |
| 8 | Proline | Pro / P |
Only eight of the twenty standard amino acids appear. Proline is the most frequent with four residues, glycine appears three times, alanine and aspartic acid twice each, and glutamic acid, lysine, leucine and valine once each. Two structural points follow directly. There is no cysteine, so the molecule has no disulfide bridge and no free thiol. And positions 3, 4 and 5 are three consecutive prolines, a run described in the review literature as conformationally rigid and likely to adopt a polyproline II helix, a left-handed structure that is sterically awkward for proteolytic enzymes to attack.
The term itself is only a count. "Pentadeca-" is Greek for fifteen, from penta (five) and deka (ten), so a pentadecapeptide has exactly fifteen residues, the same way a dipeptide has two.
Molecular formula, molecular weight and identifiers
These are the public identifiers a catalogue listing and a certificate of analysis should agree on:
| Attribute | Value |
|---|---|
| Molecular formula | C62H98N16O22 |
| Average molecular weight | 1419.5 g/mol (often quoted as 1419.53 Da) |
| Monoisotopic mass | 1418.704 Da |
| CAS Registry Number | 137525-51-0 |
| PubChem CID | 9941957 |
| UNII | 8ED8NXK95P |
| ChEMBL ID | CHEMBL4297358 |
The formula can be checked against the sequence. Add up the atoms of the fifteen free amino acids, subtract the fourteen water molecules lost as the peptide bonds form, and the result is exactly C62H98N16O22: the sixteen nitrogens, for example, are the fifteen backbone amide nitrogens plus the one side-chain nitrogen of the lysine at position 7.
The two mass figures do different jobs. The average weight near 1419.5 accounts for natural isotope abundances and is the number used for weighing and concentration arithmetic. The monoisotopic mass of 1418.704 uses only the most abundant isotope of each element, and it is the figure a mass spectrometry identity check is matched against.
Where the name comes from, and when it was described
BPC is short for Body Protection Compound. The name belongs first to a larger protein of roughly 40 kDa found in gastric juice; BPC-157 is the fifteen-residue fragment taken from its N-terminal end, a relationship stated in the same terms in both the patent and the analytical literature. It entered the scientific literature in 1993, in a paper by Sikiric, Petek, Rucman, Seiwerth and colleagues in Zagreb, with the chemistry developed in parallel at the Slovenian company Diagen.
The patent trail is public. The earliest filings, including US Patent 5,288,708, concern the natural BPC protein isolated from gastric juice. Later filings, EP 0572688 and US Patent 6,268,346, concern the synthetic fragment. A 2014 international application, WO2014142764A1, assigned to Diagen with Rudolf Rucman named as inventor, covers stable salts of the pentadecapeptide and restates both the sequence and its gastric origin. A patent describes a claimed invention, not a regulatory status.
How is BPC-157 studied?
Published research on BPC-157 has mostly used cell culture and animal models. Recurring themes in that work include:
- Angiogenesis: how the peptide relates to the formation of new blood vessels in model systems.
- Nitric oxide signaling: its interaction with a pathway involved in vascular tone and tissue response.
- Tissue and connective structures: models looking at tendon, muscle, and gastrointestinal tissue.
It is worth being precise here. These are observations from laboratory models, not conclusions about people or animals. BPC-157 is a research compound, and the honest summary is that it remains an active area of preclinical study rather than a settled one.
How BPC-157 is made
Nothing is extracted from tissue. Research-grade BPC-157 is assembled residue by residue using solid-phase peptide synthesis, which builds the chain on an insoluble polymeric support; the Diagen patent documents credit Sikiric and Rucman with the synthetic route and reference preparation on solid polymeric carriers. The starting materials are protected amino acid derivatives, not biological material. After assembly the chain is cleaved from the support, purified by reversed-phase HPLC, confirmed by mass spectrometry and freeze-dried. Because reversed-phase purification isolates peptides as salts, the dried solid carries a counterion such as trifluoroacetate plus residual water, so the weighed mass is not one hundred percent peptide; our guide to reading a certificate of analysis explains how that is reported.
One storage detail follows from the sequence itself: BPC-157 contains no asparagine, glutamine, cysteine, methionine or tryptophan, the residues peptide manufacturers single out as shortening shelf life because they are the most prone to deamidation or oxidation.
Quality, purity, and handling
Because a short peptide is only as reliable as the batch you actually receive, purity matters more than the name on the label. Research-grade BPC-157 is verified by HPLC for purity and by mass spectrometry for identity, and each batch should come with its own certificate of analysis. It typically ships lyophilized, and you can check any Codex Research vial by its batch number.
Research use only
All products sold by Codex Research, including BPC-157, are strictly for laboratory research and development. They are not for human or animal consumption and are not intended to diagnose, treat, cure, or prevent any disease.
The compound at Codex Research
BPC-157, 10 mg per vial — batch-verified, with its certificate of analysis.
Frequently asked questions
What does BPC-157 stand for?
BPC stands for "Body Protection Compound." BPC-157 is a synthetic pentadecapeptide (15 amino acids) whose sequence is derived from a protein found in gastric juice. It is used strictly for laboratory research.
Is BPC-157 a natural or synthetic peptide?
The sequence originates from a naturally occurring gastric protein, but the BPC-157 used in research is made synthetically by solid-phase peptide synthesis and verified by HPLC and mass spectrometry.
How is BPC-157 studied in the lab?
Most published work uses cell culture and animal models, looking at pathways associated with angiogenesis, nitric oxide signaling, and connective tissue. These are preclinical observations, not conclusions about use in people or animals.
What is the amino acid sequence of BPC-157?
In one-letter code the sequence is GEPPPGKPADDAGLV; in three-letter code, Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, read from the N-terminus to the C-terminus. The free-acid form is written H-GEPPPGKPADDAGLV-OH. Only eight different amino acids appear in the chain, and proline occupies four of the fifteen positions.
What is the molecular formula and molecular weight of BPC-157?
The molecular formula is C62H98N16O22. PubChem lists the average molecular weight as 1419.5 g/mol, commonly quoted in the literature as 1419.53 Da, and the monoisotopic mass as 1418.704 Da. Its CAS Registry Number is 137525-51-0 and its PubChem CID is 9941957.
Why is BPC-157 called a pentadecapeptide?
"Pentadeca-" is Greek for fifteen, from penta (five) and deka (ten), so a pentadecapeptide is a peptide of exactly fifteen amino acid residues. The term describes chain length and nothing else.
When was BPC-157 first described, and is there a patent?
It entered the scientific literature in 1993 in a paper by Sikiric, Petek, Rucman, Seiwerth and colleagues in Zagreb, with the chemistry developed at the Slovenian company Diagen. The related patent family includes US 5,288,708 on the natural gastric protein, EP 0572688 and US 6,268,346 on the synthetic fragment, and the 2014 application WO2014142764A1 on stable salts of the pentadecapeptide.
References
- BPC-157 compound summary (CID 9941957). PubChem, National Library of Medicine.
- Mateescu et al. BPC-157 as an investigational peptide: biopharmaceutical challenges, formulation strategies and translational development barriers. Pharmaceutics, 2026.
- Tian T, Jing J, Li Y, Wang Y, Deng X, Shan Y. Characterization of the in vitro metabolic profile of BPC-157 by UHPLC-HRMS. Molecules, 2023.
- Patent WO2014142764A1, stable pentadecapeptide salts (applicant Diagen d.o.o.; inventor R. Rucman). Google Patents.
- Sikiric P, Petek M, Rucman R, Seiwerth S, et al. Journal of Physiology (Paris), 1993;87(5):313-327 (PMID 8298609). First published description of the gastric juice peptide BPC.