Construction of a bFGF-tethered extracellular matrix using a coiled-coil helical interaction.

A novel method for construction of biomaterials for tissue engineering was developed. Noncovalent associations between extracellular matrix (ECM) and growth factors were achieved by engineering recombinant versions of both proteins that included helical peptides that could form a coiled-coil structure. The helix A peptide, which is capable of forming a coiled-coil helical structure, was fused with a matrix protein that contains a cell-adhesive RGD sequence. The helix B peptide, which is also capable of forming a coiled-coil helical structure, was fused with basic fibroblast growth factor (bFGF). Each protein retained its original activity of promoting cell adhesion and cell proliferation, respectively. These recombinant proteins associated noncovalently through coiled-coil helix formation between helix A and helix B. The resulting complex combined the functions of both proteins, and this method of joining proteins with different functionalities could be used to develop biomaterials for tissue engineering.