Activation of demineralized bone matrix by genetically engineered human bone morphogenetic protein-2 with a collagen binding domain derived from von Willebrand factor propolypeptide.

There is a large demand for new bone regeneration to restore the function during bone injuries. Bone filling materials are important in bone tissue restoration. In this study, the demineralized bone matrix (DBM) was activated with the engineering human bone morphogenetic protein-2 (BMP-2). To enhance the binding of BMP-2 to the DBM scaffolds, a collagen-binding peptide was fused to the N-terminal of BMP-2. The in vitro results showed that the engineered collagen-targeted BMP-2 (rhBMP2-v) bound to DBM scaffolds specifically and the rhBMP2-v had increased alkaline phosphatase activity in C2C12 cells. In vivo, the DBM scaffolds impregnated with rhBMP2-v showed greater effect on ectopic bone formation. Our data suggested that the collagen-based BMP-2 targeting bone repair system had greater bone inducing ability than DBM loaded with regular BMP-2. Copyright 2006 Wiley Periodicals, Inc.