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Engineering and application of collagen‐binding fibroblast growth factor 2 for sustained release
Author(s) -
Jeon Eunyi,
Yun YeRang,
Kim HaeWon,
Jang JunHyeog
Publication year - 2014
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.34689
Subject(s) - fibroblast , fibroblast growth factor , materials science , microbiology and biotechnology , alkaline phosphatase , tissue engineering , adhesion , cell growth , growth factor , cell adhesion , biophysics , biomedical engineering , biochemistry , in vitro , chemistry , biology , receptor , enzyme , medicine , composite material
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. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 102A: 1–7, 2014.