BPC-157 5 mg

What is BPC-157?

BPC-157 is a fully synthetic, linear peptide of 15 amino acids, i.e. a pentadecapeptide. The abbreviation stands for “Body Protection Compound 157”. In databases and journal articles the substance also appears as BPC 157 or as “Gastric Pentadecapeptide BPC 157”. The literature describes its sequence as a partial sequence of a protein that is said to have been isolated from human gastric juice and is referred to as Body Protection Compound. However, no sequence has been deposited publicly for this parent protein, so the stated origin rests solely on its description in the scientific literature. PubChem lists the peptide with, among others, the synonym “Gastric Juice Peptide Fragment”.

Structure and key data

• Sequence: H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH (one-letter code GEPPPGKPADDAGLV)
• Structure: 15 amino acids, linear, free N- and C-terminus
• Molecular formula: C62H98N16O22
• Molar mass: 1419.5 g/mol (average); monoisotopic mass 1418.70 Da
• CAS number: 137525-51-0
• PubChem CID: 9941957

The formula and masses apply to the free peptide without counter-ions. Structurally, the high proline content stands out: four of the 15 positions are occupied by proline, three of them in direct succession at positions 3 to 5. The three acidic residues, one glutamate and two aspartates, are offset by only one basic side chain, that of lysine.

Classification: BPC-157 and related peptides

In research catalogues BPC-157 is often mentioned in the same breath as TB-500, although the two molecules have little in common. BPC-157 comprises 15 unmodified amino acids and is attributed to a gastric juice protein. TB-500 is an N-terminally acetylated heptapeptide that represents a section of thymosin β4. Both fragments are also available together in the BPC-157 + TB500 set. The third single peptide in the Peptide Fragments category is KPV, a tripeptide from the C-terminal end of the α-MSH sequence.

Research context

No defined receptor or other molecular target protein has yet been identified for BPC-157, and the scientific literature regards the mechanism as unresolved. The peptide is studied predominantly in connection with the signalling pathways of angiogenesis and cell migration. In vitro, the focus is on assays with tendon fibroblasts that record the outgrowth, survival and migration of the cells. Preclinically, BPC-157 is examined in rodent models that concentrate on tendon, ligament, muscle and gastrointestinal tissue.

Analytics at GPeptides

For BPC-157, HPLC provides the purity value: the area of the main peak is expressed relative to the total area of all signals. Mass spectrometry establishes whether this main peak really is BPC-157. A signal matching the monoisotopic mass of 1418.70 Da is expected; with electrospray ionisation the peptide typically appears as a singly protonated ion at about m/z 1419.7 or, doubly protonated, at about m/z 710.4.

Like the rest of the range, BPC-157 is regularly tested externally by HPLC and mass spectrometry in an independent laboratory. Available certificates of analysis can be found in the lab area; if no certificate has been filed there yet, the status is “pending”. What lies behind percentage figures and secondary peaks is explained in the guide Purity of research peptides.