Abstract
The sustained release of growth factors plays a critical role in therapeutic applications because of the instability of these factors in the body. Here, we designed a fibroblast growth factor 2 (FGF2) fused with a collagen-binding domain (rhCBD-FGF2) for collagen-based sustained release of FGF2.The release profile of rhCBD-FGF2 showed sustained release from collagen matrices. Further, rhCBD-FGF2 also stimulated adhesion of the MC3T3-E1 cells to the collagen matrices. In addition, rhCBD-FGF2 increased the cell proliferation activity at 3 and 5 days in the MC3T3-E1 cells attached to the collagen matrices compared to that in the control. Further, rhCBD-FGF2 significantly induced the osteogenic differentiation of MC3T3-E1 cells on collagen matrices by up-regulating the alkaline phosphatase activity at 7 days. These osteogenic differentiation activities were confirmed in gene expression of MC3T3-E1 cell. Taken together, rhCBD-FGF2 could specifically bind with collagen matrices, which indicates important advancements in bone tissue engineering.
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