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BPC-157

BPC-157 is a synthetic 15-amino-acid peptide whose sequence was derived from a protein fraction of gastric juice. It is studied mainly in rodent models of gastrointestinal, tendon and soft-tissue injury and is not approved for any use.

Last reviewed 2026-10-25 by the PeptideWiki editorial team. Editorial policy.

Overview

BPC-157 is a pentadecapeptide, a chain of fifteen amino acids, described as a partial sequence of a larger protein ("body protection compound") reported in gastric juice. Most of the published work comes from a single research group in Zagreb, Croatia, which has studied the peptide since the early 1990s. The group has described it as notably stable in gastric juice, which led to experiments using oral as well as parenteral administration in animals.

The research literature is large in volume but narrow in origin. Most studies are rodent experiments on gastrointestinal lesions, tendon and ligament injury, muscle damage, and vascular and nervous-system models, with a smaller body of in-vitro work on cultured cells. Controlled human data are very limited, and independent replication outside the originating group is comparatively sparse. Readers should treat reported effects as preclinical findings whose relevance to people has not been established.

Compare: BPC-157 vs TB-500.

Structure

BPC-157 is a linear peptide of 15 residues with the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val (GEPPPGKPADDAGLV), with a free N-terminus and a free C-terminal acid. It contains no cysteine, methionine or tryptophan, so it lacks the most common oxidation-prone residues. Research material is usually supplied as a lyophilized salt; acetate and trifluoroacetate (TFA) salts are common, and arginine salt preparations have also been described. The salt form changes the net peptide content of a given mass of powder and should be stated on the certificate of analysis.

Mechanism

No single receptor for BPC-157 has been identified. Proposed mechanisms come largely from rodent and cell-culture studies and include effects on the nitric oxide system, on angiogenesis-related signaling such as the VEGF receptor 2 pathway, on focal adhesion kinase and paxillin signaling involved in cell migration, and on growth hormone receptor expression in cultured tendon fibroblasts. These observations are not yet integrated into an established mechanism, and many have not been independently confirmed. Because most findings originate from one laboratory network, their generality remains uncertain.

Research

Gastrointestinal models

The earliest and most numerous studies examine BPC-157 in rodent models of gastric and intestinal injury, including lesions induced by alcohol, nonsteroidal anti-inflammatory drugs and other irritants, as well as models of inflammatory bowel disease and fistula formation. Authors have reported reduced lesion size and faster healing in treated animals. A form designated PL 14736 was reported to have entered early clinical testing for inflammatory bowel disease, but detailed peer-reviewed human results are scarce, and the gastrointestinal evidence remains overwhelmingly preclinical.

Tendon, ligament and muscle

A second cluster of rodent studies looks at transected or crushed tendons, ligaments and skeletal muscle, reporting improved functional and histological measures in treated animals. In-vitro work on tendon fibroblasts has examined cell survival, migration and outgrowth from explants. These studies are the main basis for interest in the peptide in musculoskeletal research. They are small animal experiments with heterogeneous designs, and there are no adequately powered controlled trials in people.

Vascular and nervous-system models

Several rodent papers describe effects of BPC-157 in models of vessel occlusion, thrombosis, blood pressure disturbance, and drug-induced or traumatic nervous-system injury. Other studies report interactions with dopaminergic and serotonergic systems in behavioral models. This literature is broad and frequently hypothesis-generating, but it is almost entirely from animal experiments, often from the same research group, and should be read as exploratory rather than as evidence of any effect in humans.

Evidence quality

Overall, the BPC-157 literature is characterized by many positive animal reports, few independent laboratories, little standardized dosing or characterization of the test material, and an almost complete absence of published randomized controlled human trials. Small human reports exist but are uncontrolled or preliminary. Safety in people has not been systematically characterized. These limitations were among the points raised in regulatory review, and they mean the compound should be regarded as an investigational research peptide.

Regulatory status

BPC-157 is not approved by the FDA for any use. In July 2026 the FDA's Pharmacy Compounding Advisory Committee (PCAC) voted 8-6-1 to recommend adding BPC-157 to the Section 503A bulk drug substances list, although FDA's own reviewers had recommended against it. The vote is advisory; FDA must act through notice-and-comment rulemaking, and no final FDA action has been announced. FDA noted unsettled identity and characterization issues, such as variable sequences and salt forms, among research-grade material. BPC-157 is prohibited at all times by WADA under class S0 (non-approved substances).

Status changes often. See the regulatory tracker for dated updates.

Quality and identity testing

A good certificate of analysis should confirm identity by mass spectrometry, with the observed mass matching the expected mass shown on this page, and report purity by reverse-phase HPLC with the chromatogram. Because research material circulates as acetate, TFA and arginine salt forms, the COA should name the counter-ion and ideally report net peptide content, since salt and water can make up a substantial fraction of the powder. Sequence errors such as deletions in the proline-rich stretch or substitutions near the aspartate residues are a known characterization risk, so MS/MS or amino acid analysis adds confidence. Aspartate-glycine and aspartate-alanine motifs can be sites of degradation, so related-substance peaks should be reported.

Open BPC-157 in the sequence analyzer to see the expected [M+H]+ and multiply charged ions for an MS identity check.

For a walkthrough of each section of a certificate, see how to read a COA.

Storage and stability

Store lyophilized BPC-157 sealed at -20 °C or colder, protected from light and moisture, and allow vials to reach room temperature before opening to limit condensation. The peptide lacks cysteine and methionine, so oxidation is less of a concern than for many peptides, but hydrolysis and aspartate-related degradation can still occur in solution. Prepare solutions in sterile buffer or water for lab use, keep them refrigerated for short-term work, aliquot for longer storage at -20 °C or below, and avoid repeated freeze-thaw cycles.

Latest research

The newest PubMed-indexed papers that mention BPC-157 in their title or abstract, retrieved through Europe PMC and refreshed automatically. Inclusion is not an endorsement of a paper's findings.

  1. Loading the latest papers…

All BPC-157 papers on PubMed, newest first

Frequently asked questions

Is BPC-157 FDA approved?

No. BPC-157 is not approved by the FDA for any use. In July 2026 an FDA advisory committee voted to recommend adding it to the 503A bulk drug substances list for compounding, but that vote is advisory only. FDA must go through notice-and-comment rulemaking, and no final action has been announced.

Where does BPC-157 come from?

BPC-157 is a synthetic peptide. Its 15-residue sequence was described as a partial sequence of a protein fraction reported in human gastric juice, and the name stands for body protection compound. Research material is made by solid-phase peptide synthesis rather than extracted from biological sources.

What is the difference between BPC-157 and TB-500?

They are unrelated peptides. BPC-157 is a 15-residue sequence linked to a gastric juice protein, while TB-500 refers to a short synthetic fragment derived from thymosin β4, though the name is also applied loosely to full-length thymosin β4. Both are studied in tissue-repair models, mostly in animals, and both were reviewed by the FDA advisory committee in 2026.

Is BPC-157 banned in sport?

Yes. WADA lists BPC-157 under class S0, non-approved substances, which are prohibited at all times in and out of competition. Researchers working with athletes or in anti-doping should consult the current WADA Prohibited List for the latest wording. The listing reflects the fact that BPC-157 is not approved for human use by any major regulator.

  • TB-500

    TB-500 is a research name most often applied to a short synthetic N-acetylated fragment of thymosin β4, Ac-LKKTETQ, but it is also used loosely for full-length thymosin β4. There are no direct human studies of the fragment.

  • Thymosin β4

    Thymosin β4 is a naturally occurring 43-amino-acid peptide that binds monomeric actin and is abundant in many cell types. It has been studied in animal models of tissue repair and in human trials of ophthalmic and topical formulations, and is not approved.

  • KPV

    KPV is the tripeptide lysine-proline-valine, the C-terminal sequence of alpha-melanocyte-stimulating hormone. It is studied for anti-inflammatory effects in cell and rodent models, particularly of intestinal inflammation, and is not approved for any use.

  • GHK-Cu

    GHK-Cu is the copper(II) complex of GHK (glycyl-histidyl-lysine), a tripeptide found in human plasma. It is widely used as a cosmetic ingredient and studied in cell, animal and small human skin studies.

References

  1. PubMed: all indexed literature on BPC-157
  2. ClinicalTrials.gov: registered studies mentioning BPC-157

Cite this page

PeptideWiki. (2026). BPC-157. Retrieved from https://peptidewiki.net/compounds/bpc-157/