BPC-157

BPC-157 (Body Protection Compound-157) is a synthetic pentadecapeptide (15 amino acids: Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val) derived from a partial sequence of human gastric juice protein BPC. It has become one of the most extensively published research peptides in the field of tissue biology, with over 100 peer-reviewed publications from multiple independent research groups examining its mechanisms across gastrointestinal, musculoskeletal, neurological, and vascular biology contexts.

The structural basis for BPC-157's unusual stability in biological media is the Pro-Pro-Pro sequence at positions 3-5, which forms a polyproline II (PPII) helix — a rigid left-handed helical structure that most endopeptidases cannot engage due to the absence of backbone NH groups (proline's pyrrolidine ring eliminates these) and the unusual surface topology of a PPII helix. This stability enables BPC-157 to maintain its biological activity in plasma, gastric acid, and cell culture media where most 15-residue peptides would be rapidly degraded.

BPC-157's mechanistic research profile centres on four interconnected pathways. The nitric oxide/eNOS axis is the most studied: BPC-157 research has examined eNOS expression, phosphorylation at Ser1177 (activating) and Thr495 (inhibitory), and NO production in endothelial and smooth muscle cell models. Experiments using L-NAME (NOS inhibitor) and L-arginine (NOS substrate) have characterised the extent to which BPC-157's effects are NOS-dependent.

The VEGF/EGR-1 angiogenic axis represents BPC-157's second major mechanistic theme. Early growth response 1 (EGR-1) is a zinc finger transcription factor that drives VEGF gene expression following growth factor stimulation. VEGF then activates VEGFR2 on endothelial cells, driving tube formation, cell migration, and neovascularisation. Research has examined BPC-157's effects on EGR-1 promoter activity, VEGF protein secretion (ELISA of conditioned medium), and tube formation on Matrigel.

The FAK-paxillin pathway connects BPC-157 to cell adhesion and cytoskeletal biology. FAK (focal adhesion kinase) autophosphorylation at Tyr397 initiates a cascade through Src kinase that activates paxillin, vinculin, and other focal adhesion complex proteins regulating cell migration and survival. BPC-157 research in tendon fibroblast models has examined FAK-paxillin signalling as a mechanism for tendon outgrowth and healing.

MW: 1419.56 g/mol. CAS: 137525-51-0. Molecular formula: C62H98N16O22. Reconstitute in bacteriostatic water at 1mg/mL. Stable lyophilised at -20°C for 2+ years. For laboratory and analytical research purposes only.