4. CONCLUSION
We herein developed the circularly permuted variant
cp-hFGF7115-114 without any deletion of the wild type
hFGF7. This protein proved to be more soluble and stabile than the wild
type, and had comparable or greater biological activity than the wild
type protein. Taken together, although more sophisticated analyses and
preclinical trials are needed for practical application, we expect that
the variant cp-hFGF7115-114 could be a potential
alternative drug candidate for related symptoms. In addition, the CP
technique was also broadly applicable for the generation of functionally
soluble variants of the FGF family proteins.