What is BPC-157?
BPC-157 (Body Protection Compound-157) is a synthetic pentadecapeptide with the amino acid sequence GEPPPGKPADDAGLV. It consists of 15 amino acids (CAS: 137525-51-0, MW: 1419.56 g/mol) and was originally isolated from human gastric juice. The high proline content — four of the fifteen amino acids are proline — confers BPC-157 with exceptional resistance to enzymatic degradation (proteolysis).
| Parameter |
Value |
| Sequence |
GEPPPGKPADDAGLV |
| Amino acids |
15 (pentadecapeptide) |
| Molecular weight |
1419.56 g/mol |
| CAS number |
137525-51-0 |
| Distinctive feature |
4/15 amino acids are proline → high proteolysis stability |
Research history
BPC-157 was synthesized and characterized in the 1990s by the research group led by Professor Predrag Sikiric at the University of Zagreb (Croatia). It is a partial sequence analog of the 'Body Protection Compound' — a naturally occurring protein in human gastric juice.
Since then, BPC-157 has been investigated in a wide variety of preclinical in vitro and in vivo studies. The publication base includes several hundred peer-reviewed articles, predominantly from the Croatian research group as well as increasingly from independent laboratories worldwide.
Research context
All published data on BPC-157 originate from preclinical in vitro and in vivo models. No phase II or phase III clinical trials exist. BPC-157 is not an approved medicinal product and is intended solely for research purposes.
Documented research areas
BPC-157 has been investigated in the following research areas in preclinical models:
- →VEGFR2 signal transduction — Angiogenesis signaling pathways in endothelial cell cultures
- →NO signaling system — eNOS expression analyses and NO modulation
- →Fibroblast migration — Scratch assays in fibroblast cultures
- →Gastrointestinal models — Gastric epithelial cell cultures
- →Musculoskeletal models — Tendon and cartilage cell cultures in vitro
Molecular stability
The exceptional proteolysis stability of BPC-157 is one of the peptide's most scientifically interesting properties. Proline disrupts the regular helical structure of peptide chains and makes the peptide bonds at these positions less accessible to many proteases.
With four proline residues out of fifteen amino acids — a proline content of 26.7% — BPC-157 exhibits significantly higher stability against gastrointestinal and serum proteases than most other linear peptides of comparable length. This makes it an analytically interesting model peptide for stability studies.