Collagen alpha-1(I) chain (residues 769-783) (COL1A1 (769-783))

The Type I collagen cell-binding domain (residues 769-783), commonly known as the P-15 peptide, is a specific sequence within the alpha-1 chain of Type I collagen that facilitates cell-matrix interactions (UniProt: P02452). This domain is a critical recognition site for integrin receptors, particularly the alpha2beta1 integrin, which is expressed on the surface of osteoblasts and other mesenchymal cells (Bhatnagar et al., 1999, PubMed: 10467021). By binding to these receptors, the domain triggers intracellular signaling pathways that promote cell adhesion, migration, and differentiation into bone-forming cells (PubMed: 11530005). In therapeutic contexts, synthetic P-15 is used as a biomimetic component in bone graft substitutes, such as i-FACTOR, to enhance the rate and quality of bone repair in spinal fusion and dental applications (FDA: P120025). This target is essential for maintaining the structural integrity of the extracellular matrix and coordinating the cellular responses necessary for tissue regeneration and skeletal homeostasis (PubMed: 10467021).

Other names

P-15 peptideType I collagen cell-binding domainIntegrin recognition site of Type I collagenP15

Acts as a biomimetic ligand that binds to integrin receptors (specifically alpha2beta1) on osteogenic cells to promote cell attachment, proliferation, and osteogenic differentiation (PubMed: 10467021).