BPC-157

BPC-157 (also written BPC 157) is a synthetic peptide of 15 amino acids, a pentadecapeptide with the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. BPC stands for body protection compound, the name its discoverers gave to a protein isolated from human gastric juice, and BPC-157 is a partial sequence of that protein (Chang et al., 2011).

The published work is overwhelmingly preclinical, from cell culture and animal studies: a 2025 systematic review of the musculoskeletal literature included 35 preclinical studies and one clinical study (Vasireddi et al., 2025).

The sequence and aliases are from PubChem (CID 9941957), which lists the molecular weight as 1419.5 g/mol.

Published work on BPC-157 falls into five areas, most of it in animal models and cultured cells. Each summary below states the model used.

Gastrointestinal lesion models

Much of the literature uses rat models of gastric and intestinal injury. One study tested BPC-157 against ethanol-induced gastric lesions alongside agents that block or supply nitric oxide (NO), and found that in rat gastric mucosa homogenates the peptide generated NO at a level comparable to L-arginine (Sikiric et al., 1997).

In a four-week rat model of short bowel syndrome after extensive small-bowel resection, investigators tracked body weight, villus height, crypt depth, muscle thickness and anastomosis breaking strength, and reported weight gain above preoperative values in the BPC-157 groups (Sever et al., 2009). Reviews from the discovering group summarize this work and describe the peptide as stable in human gastric juice (Sikiric et al., 2016).

Tendon (soft tissue) models

In rats with a transected Achilles tendon, BPC-157 was evaluated with biomechanical, functional, microscopic and macroscopic measures over 14 days. In cultured tendocytes it countered the growth inhibition caused by 4-hydroxynonenal (Staresinic et al., 2003). A separate group in Taiwan found that BPC-157 increased outgrowth from rat tendon explants, survival of tendon fibroblasts under hydrogen peroxide stress and fibroblast migration, with activation of the FAK-paxillin pathway (Chang et al., 2011). The same group reported raised growth hormone receptor expression in tendon fibroblasts (Chang et al., 2014).

Blood vessels and nitric oxide signaling

In isolated rat aorta, BPC-157 produced concentration-dependent, endothelium-dependent vasodilation that NO inhibition blocked. In endothelial cells it induced NO generation and phosphorylation of Src, caveolin-1 and eNOS, and promoted cell migration (Hsieh et al., 2020). A 2025 review cites VEGFR2 activation and the Akt-eNOS axis as recurring mechanisms in angiogenesis (blood vessel growth) models (McGuire et al., 2025), and the discovering group has reviewed the peptide's interactions with the NO system (Sikiric et al., 2014).

Metabolism and analytical detection

Because BPC-157 has turned up in confiscated vials, anti-doping laboratories have characterized it. Incubation in plasma showed that the peptide forms a stable metabolite, and a validated weak cation-exchange extraction method for urine had a limit of detection of 0.1 ng/mL for BPC-157 (Cox et al., 2017).

A stable-isotope-labeling study identified nine in vitro metabolites, one from a previously undescribed pathway, and validated a urine method for the parent peptide and five main metabolites (Tian et al., 2023). In rats and beagle dogs, the intact peptide had an elimination half-life under 30 minutes, broke down into small fragments and amino acids, and was excreted mainly in urine and bile (He et al., 2022).

Where the human evidence stands

Human data are thin. The discovering group reports Phase II testing in inflammatory bowel disease under the code PL 14736 (Sikiric et al., 2012). A 2025 review identified only three small human pilot studies and noted that rigorous, large-scale human clinical trials are lacking (McGuire et al., 2025).