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BPC-157 / Studies
Synthetic fragment · 15 amino acids · 1,419.5 Da

BPC-157 studies and research data

PepBank has 168 BPC-157 studies with results. 162 of them gave BPC-157, with 987 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 987 results and 236 papers. Newer studies from Europe PMC

Results in people
12
1% of 987 results
Results in animals
907
92% of 987 results
Results in lab cells
68
7% of 987 results
From computer models
0
0% of 987 results
The molecule

BPC-157 identity

Identifiers, parent molecule, targets and development stage, from curated data.

BPC-157 is a linear pentadecapeptide (GEPPPGKPADDAGLV) with free termini. Published papers describe it as a partial sequence of 'body protection compound' (BPC), a protein reported in human gastric juice; UniProt has no entry for that protein or sequence. Animal and cell studies report pro-angiogenic effects linked to increased VEGFR2 expression and VEGFR2-Akt-eNOS signalling, and increased fibroblast migration with FAK and paxillin phosphorylation. Human data are limited: two small uncontrolled reports (a 2021 retrospective chart review of 16 patients given intra-articular injections, PMID 34324435; a 2025 intravenous safety pilot in 2 adults, PMID 40131143), a phase 1 study registered in 2015 (status unknown) and a phase 2 trial that started in 2026.

Kind
Synthetic fragment · 15 residues
Identifiers
ChEMBLCHEMBL4297358 (opens in a new tab)PubChem CID9941957 (opens in a new tab)UNII8ED8NXK95P (opens in a new tab)DrugBankDB11882 (opens in a new tab)CAS137525-51-0
Development
Phase 2No single developer. Trial sponsors: PharmaCotherapia d.o.o. (NCT02637284), Hudson Biotech (NCT07437547), University of Arkansas (NCT07803250).NCT07437547: phase 2, randomized, placebo-controlled, subcutaneous BPC-157 for acute hamstring strain, recruiting, start 2026-02-02, Shenzhen, China, 120 planned. NCT02637284: phase 1 oral tablets (PCO-02) in healthy volunteers, Tijuana, Mexico, start 2015-10, status unknown. NCT07803250: phase 1, rotator cuff repair, not yet recruiting (planned start 2027-01). NCT07752381 tested supplement gummies (phase not applicable). ChEMBL gives max_phase 1.0 with no indication rows. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Vascular endothelial growth factor receptor 2KDRP35968 (opens in a new tab)Increased expression, internalisation and vegfr2 akt enos pathway activation (indirect; no binding data)proposed (primary literature: rat hind-limb ischemia model and human vascular endothelial cells, 2017)Source (opens in a new tab)

Sequence and structure

Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.

Sequence

15 amino acids

H-
Residues 1 to 10:
GEPPPGKPAD
Residues 11 to 15:
DAGLV
-OH
  • HydrophobicA V I L M
  • PositiveK R H
  • NegativeD E
  • SpecialC G P

Properties

From identity sources

Formula
C62H98N16O22
Molecular weight
1,419.5 g/mol
Monoisotopic mass
1,418.7042 Da

Calculated from the sequence

Average mass
1,419.55 Da
Sum of ExPASy residue masses + water · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
1,418.7041 Da
Sum of ExPASy residue masses + water · ExPASy FindMod
Isoelectric point (pI)
3.88
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
−2.06
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
−0.693
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced)
0 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
No Trp or Tyr: absorbance at 280 nm cannot measure this peptide.
Instability index
39.32
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
58.7
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
0.96 kcal/mol
Mean solubility value (negated) · Boman 2003
2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH)
0.365
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
pI with each pKa set
EMBOSS 3.88Bjellqvist (ExPASy) 4.03IPC peptide 3.74IPC protein 3.79
  • Defined and validated for proteins; use with care for short peptides.
  • Assumes an ideal alpha helix. Many short peptides are not helical.

@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses

Net charge by pH

pI 3.88 · Net charge at pH 7.4: −2.06

Point or use arrow keys

Net charge of BPC-157 from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 3.88. Net charge at pH 7.4: -2.06.−4−20+202468101214pHNet chargepH 7.4pI 3.88

Henderson-Hasselbalch, EMBOSS pKa set. Calculated, not measured.

Show as table
pHNet charge
02.00
11.99
21.94
31.50
4−0.27
5−1.70
6−1.97
7−2.02
8−2.20
9−2.73
10−3.10
11−3.61
12−3.94
13−3.99
14−4.00

Composition

  • Hydrophobic27% (4)
  • Positive7% (1)
  • Negative20% (3)
  • Special47% (7)

15 residues. Each residue counts in one class; F and W count as aromatic.

A Ala2 · 13%
I Ile0 · 0%
L Leu1 · 7%
M Met0 · 0%
V Val1 · 7%
F Phe0 · 0%
W Trp0 · 0%
Y Tyr0 · 0%
H His0 · 0%
K Lys1 · 7%
R Arg0 · 0%
D Asp2 · 13%
E Glu1 · 7%
N Asn0 · 0%
Q Gln0 · 0%
S Ser0 · 0%
T Thr0 · 0%
C Cys0 · 0%
G Gly3 · 20%
P Pro4 · 27%

3D structure

No 3D structure

No experimental structure (PDB) and no UniProt entry for an AlphaFold model are listed for this peptide. Synthetic peptides often have neither. The sequence view above is the reference.

2D structure

Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).

SMILES fromPubChem CID 9941957(opens in a new tab)

C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H]2CCCN2C(=O)[C@@H]3CCCN3C(=O)[C@@H]4CCCN4C(=O)[C@H](CCC(=O)O)NC(=O)CN

Helical wheel

An ideal alpha-helix projection. It shows where the hydrophobic residues fall if the peptide folds as a helix. It does not show that it does.

Helical wheel of BPC-157, 15 residues at 100 degrees per residue. Hydrophobic moment 0.19 pointing at 33 degrees.Gly 1, Eisenberg consensus (normalized) 0.48G1Glu 2, Eisenberg consensus (normalized) -0.74E−2Pro 3, Eisenberg consensus (normalized) 0.12P3Pro 4, Eisenberg consensus (normalized) 0.12P4Pro 5, Eisenberg consensus (normalized) 0.12P5Gly 6, Eisenberg consensus (normalized) 0.48G6Lys 7, Eisenberg consensus (normalized) -1.50K+7Pro 8, Eisenberg consensus (normalized) 0.12P8Ala 9, Eisenberg consensus (normalized) 0.62A9Asp 10, Eisenberg consensus (normalized) -0.90D−10Asp 11, Eisenberg consensus (normalized) -0.90D−11Ala 12, Eisenberg consensus (normalized) 0.62A12Gly 13, Eisenberg consensus (normalized) 0.48G13Leu 14, Eisenberg consensus (normalized) 1.06L14Val 15, Eisenberg consensus (normalized) 1.08V15
μH, residues shown
0.187
μH, best 11-residue window
0.365
Arrow direction
33°
Residues
15
HydrophilicHydrophobic

Eisenberg consensus (normalized) scale · + K, R · − D, E

Assumes an ideal α-helix: 100° per residue, 3.6 residues per turn. The arrow is the mean hydrophobic moment (Eisenberg et al. 1984) and points at the hydrophobic face.

Show as table
PositionResidueAngleEisenberg consensus (normalized)
1G0°0.48
2E100°-0.74
3P200°0.12
4P300°0.12
5P40°0.12
6G140°0.48
7K240°-1.50
8P340°0.12
9A80°0.62
10D180°-0.90
11D280°-0.90
12A20°0.62
13G120°0.48
14L220°1.06
15V320°1.08
Results by area

What the studies measured

People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.

Trials and papers
Status and safety
Data

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