Construction of a bFGF-tethered multi-functional extracellular matrix protein through coiled-coil structures for
Masayasu Mie1, Shoichi Sasaki, Eiry Kobatake
1Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8502, Japan.
Abstract:
In this study, an artificial multi-functional extracellular matrix (ECM) protein, tethered with a growth factor, was developed for neurite outgrowth induction. The designed ECM protein was comprised of an elastin-like peptide, as a structural unit, as well as the AG73 peptide sequence derived from the laminin and the C3 peptide sequence, which binds to neural cell adhesion molecules (derived from a synthetic peptide library) as functional units. Both AG73 and C3 have been demonstrated to promote cell adhesion and enhance neurite outgrowth. For the tethering of basic fibroblast growth factor (bFGF) to the ECM protein, helical peptides were fused to the ECM protein to form a coiled-coil helical structure with helical peptide-fused bFGF. Neurite outgrowth was induced in the PC12 cells that were cultured on this ECM protein as a result of the tethered-bFGF. Moreover, neurite outgrowth was enhanced by the AG73 and C3 peptides of the ECM protein.
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