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.