What Is BPC-157? Sequence, Structure and Research

BPC-157 is a synthetic 15-amino-acid peptide (Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) with a molecular weight of about 1419.5 g/mol. It was described in 1993 by Predrag Sikirić's group in Zagreb as a fragment of a larger protein, called BPC, isolated from human gastric juice. It is an investigational compound: no drug containing it is approved by the FDA or any other regulator, and nearly all of the published work on it comes from cell culture and animal models.

The rest of this profile covers what is actually known about the molecule: its identity, where the sequence came from, the signaling pathways it has been linked to, the models it has been studied in, its regulatory position in the United States and in sport, and the practical points that matter when it arrives in a lab as a lyophilized powder.

Identity at a glance

The values below are taken from the PubChem record for BPC-157 (CID 9941957). Where a supplier's certificate reports a different mass, the usual reason is a salt form: BPC-157 is sold both as the free peptide and as an acetate salt, and FDA's 2026 briefing material lists the two as separate substances.

A few structural points follow directly from the sequence. There are four prolines, three of them in a row (residues 3 to 5), which restricts backbone flexibility in that stretch. There is one basic residue (Lys7) against three acidic ones (Glu2, Asp10, Asp11), so the peptide carries a net negative charge at neutral pH. There are no cysteines, so there are no disulfide bonds to form or scramble, and no methionine or tryptophan, the residues most prone to oxidation in storage. For a broader primer on how residues, bonds and termini define a peptide, see what peptides are.

Where BPC-157 came from

The name stands for "body protection compound." In a 1993 overview in the Journal of Physiology (Paris), Sikirić and colleagues reported a gastric juice protein of roughly 40,000 Da, which they named BPC, and described a 15-amino-acid fragment of it, BPC 157, as the part they considered essential for its activity. The fragment was characterized and synthesized, and essentially all later work has used the synthetic peptide rather than material purified from gastric juice.

Two points from the later literature are worth knowing. First, a 2025 literature and patent review by Józwiak and colleagues notes that the sequence shows no homology with known intestinal peptides, so BPC-157 is not a recognized fragment of a characterized human hormone in the way that, for example, many growth hormone fragments are. Second, the same review attributes the peptide's reported stability in water and gastric juice to its N-terminal glycine and the triple-proline motif, which are thought to resist nonspecific proteolysis. That stability claim comes largely from the originating group and has not been the subject of independent, standardized degradation studies of the kind a regulator would expect.

It helps to be clear about what "from gastric juice" does and does not mean. The peptide sold today, including research-grade material, is made by solid-phase peptide synthesis. It is not extracted from any biological source.

Proposed mechanisms in the literature

No single receptor for BPC-157 has been identified. The published mechanistic work instead reports changes in several signaling pathways, mostly in cultured cells. The main threads are:

• VEGFR2 and nitric oxide. Work by Hsieh and colleagues (2017) in human vascular endothelial cells reported increased expression and internalization of vascular endothelial growth factor receptor 2 (VEGFR2), and time-dependent activation of the VEGFR2–Akt–eNOS pathway. The effect on tube formation was blocked by dynasore, an endocytosis inhibitor, which the authors took as evidence that receptor internalization is involved. The Józwiak review describes the nitric oxide system as the most frequently proposed target overall.
• FAK–paxillin and cell migration. In fibroblasts isolated from rat Achilles tendon, a 2011 study by Chang and colleagues reported increased phosphorylation of focal adhesion kinase (FAK) and paxillin, increased cell spreading and F-actin formation, and increased migration in transwell assays, without a direct effect on proliferation.
• Growth hormone receptor. A follow-up study by the same group in 2014 used a cDNA microarray on the same tendon fibroblasts and found the growth hormone receptor among the most strongly up-regulated genes. Adding growth hormone to BPC-157-treated cells activated Janus kinase 2 (JAK2), the receptor's downstream kinase.
• Other reported pathways. The 2025 review also lists early growth response-1 (EGR-1) gene expression, antioxidant enzymes such as heme oxygenase-1, and interactions with dopamine and serotonin systems in rodent models.

These observations come from a small number of laboratories, several of them sharing authors, and the upstream event, meaning what BPC-157 binds first, remains unknown. That is the honest summary of the mechanism: a set of downstream signaling changes with no identified primary target.

Models it has been studied in

The Józwiak review catalogs the experimental systems used. In vivo work has been carried out mainly in rats (Sprague-Dawley and Wistar strains), with some studies in mice, beagle dogs and broiler chicks. The rodent models span gastrointestinal lesion and colitis models, tendon and muscle injury models, burn and skin wound models, and a range of behavioral and neurological models. In vitro systems include vascular endothelial cells, the Caco-2 intestinal epithelial line, HEK 293 cells and primary tendon fibroblasts, and the chick chorioallantoic membrane assay has been used for vessel formation.

Human data are thin. One Phase 1 study, sponsored by PharmaCotherapia d.o.o., was registered on ClinicalTrials.gov in 2015 (NCT02637284) to look at the safety and pharmacokinetics of an oral product, PCO-02, whose active ingredient was BPC-157, in an estimated 42 volunteers. The registry lists its status as unknown, and no outcome data have been posted. The review also notes a small retrospective report and an older pharmacokinetic estimate, neither of which meets the standard of a controlled trial.

Regulatory status

BPC-157 is not an approved drug in the United States or, as far as published sources show, anywhere else. Its current position has three parts.

FDA and compounding. Under section 503A of the Federal Food, Drug, and Cosmetic Act, a compounder may only use a bulk substance that has a USP monograph, is a component of an approved drug, or appears on FDA's 503A bulks list. BPC-157 meets none of these. FDA had placed it in "Category 2" of its interim policy, the group of nominated substances that raise significant safety concerns. FDA's page for that category, last updated April 22, 2026, now lists BPC-157 among substances whose nominations were withdrawn by the nominators. The page records FDA's concerns: possible immunogenicity for certain routes, complexity around peptide-related impurities and characterization of the active ingredient, and a lack of information on whether it would cause harm in people.

FDA nonetheless took BPC-157 to its compounding advisory committee (PCAC) on July 23, 2026. The agency's briefing document states that FDA proposed that neither BPC-157 free base nor BPC-157 acetate be included on the 503A bulks list, and that it does not intend to issue a final determination until the advisory process has been considered and all reviews are finalized. A committee vote is advisory; it does not add a substance to the list.

Sport. The World Anti-Doping Agency added BPC-157 to its Prohibited List in 2022 under S0, "Non-approved substances," which covers pharmacological substances with no current approval by any governmental regulatory authority. The 2026 list, in force from January 1, 2026, still names BPC-157 as an example in that class, prohibited at all times.

Research supply. Outside those frameworks, BPC-157 is sold as a research chemical. That is the only basis on which Anhydrolabs supplies it: for in-vitro laboratory research, not for human or veterinary diagnosis, treatment, or consumption. The research-use page sets out the terms.

BPC-157 in the lab

Anhydrolabs supplies BPC-157 as a lyophilized powder in vacuum-sealed vials, and as 10-vial kits for groups that want one lot across a longer series of experiments. It is also available pre-combined with TB-500 in a single vial, BPC-157 / TB-500, which is compared in detail in the profile of TB-500.

Handling follows the general rules for short, unmodified peptides:

• Storage. Keep the sealed lyophilized vial frozen, dry and dark. Allow a cold vial to reach room temperature before opening so that moisture does not condense on the powder. The site's storage and handling guide gives the temperatures and the reasons for them.
• Reconstitution. BPC-157 is a hydrophilic peptide (PubChem's computed XLogP is about −9), and it is typically dissolved in sterile water or an aqueous buffer to make an in-vitro stock. Record the net peptide content from the certificate, not only the gross vial mass, when calculating molar concentrations; at 1419.5 g/mol, 1 mg of peptide is 0.70 µmol. The step-by-step method is in how to reconstitute lyophilized peptides.
• Aliquoting. Divide a stock into single-use aliquots and freeze them, rather than thawing and refreezing one tube.
• Identity and purity. Reversed-phase HPLC gives purity as the area of the principal peak relative to all detected signal, and mass spectrometry confirms identity against the monoisotopic mass of 1418.70 Da (the singly protonated ion appears near m/z 1419.7, the doubly protonated ion near m/z 710.4). An acetate salt changes the gross mass of the powder but not the mass of the peptide ion.

A certificate of analysis covers the lot it was written for and no other, so record the lot number with the experiment. To see the certificate for a lot, write to [email protected] with that number.

What is not known

A fair profile should be as specific about gaps as about findings. For BPC-157, the gaps are large:

• No primary receptor or binding partner has been identified.
• The parent 40,000 Da BPC protein has not been characterized in the public literature to the degree its fragment has.
• Most mechanistic and animal work comes from a small number of research groups, and independent replication is limited.
• There are no published, controlled human trials, and the one registered Phase 1 study has no posted outcome data.
• FDA has said, in its own words, that it lacks sufficient information to know whether the substance would cause harm in people.

Those gaps are the reason BPC-157 remains a research compound, and the reason a careful lab records lot, salt form and net peptide content for every experiment that uses it.