OP-1 / BMP-7
Overview
OP-1, or osteogenic protein-1, is the recombinant form of bone morphogenetic protein-7 (BMP-7), a member of the transforming growth factor-beta superfamily. This homodimeric protein induces differentiation of mesenchymal stem cells into osteoblasts and chondrocytes, stimulating new bone formation. It was developed primarily for spinal fusion procedures and long bone non-unions where autologous bone graft is not feasible.
Key Research Findings
OP-1 received a Humanitarian Device Exemption from the FDA in 2001 for use in recalcitrant long bone non-unions. Clinical trials in tibial non-union demonstrated healing rates comparable to autograft in selected populations, though the product was withdrawn from the U.S. market in 2014 due to commercial considerations.
Implantation at surgical site
FDA Approved
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BPC-157
Research PhaseA synthetic gastric pentadecapeptide derived from a protein found in human gastric juice. BPC-157 promotes angiogenesis and the expression of growth factors including VEGF, EGF, and NO-mediated pathways. It has demonstrated cytoprotective and wound-healing properties across multiple tissue types in preclinical models, including tendon, muscle, ligament, and gastrointestinal mucosa.
TB-500 (Thymosin Beta-4)
In Clinical TrialsThymosin Beta-4 is a 43-amino acid actin-sequestering protein involved in cell migration, differentiation, and tissue repair. It promotes wound healing by upregulating cell-building proteins such as actin and laminin, facilitating cell migration to sites of injury. TB-500 also has anti-inflammatory properties mediated through NF-kB pathway modulation.
GHK-Cu
Research PhaseA naturally occurring copper-binding tripeptide (glycyl-L-histidyl-L-lysine) found in human plasma, saliva, and urine. GHK-Cu activates tissue remodeling by stimulating collagen synthesis, glycosaminoglycan production, and angiogenesis while suppressing fibrinogen synthesis. It modulates the activity of matrix metalloproteinases and influences over 4,000 genes related to tissue repair.
DSIP (Delta Sleep-Inducing Peptide)
Research PhaseA naturally occurring nonapeptide (Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu) originally isolated from cerebral venous blood of rabbits during induced sleep. DSIP modulates sleep architecture by promoting delta wave (slow-wave) sleep through interactions with the GABAergic system and hypothalamic sleep centers. It also exhibits stress-protective, analgesic, and neuromodulatory properties.