Improvement of FGF7 Thermal Stability by Introduction of Mutations in Close Vicinity to Disulfide Bond and Surface Salt Bridge

Abstract Fibroblast Growth Factor 7 (FGF7), a growth factor specific to epithelial cells, has attracted attention as therapeutic protein. However, FGF7 limitation in its use due low protein stability. Here, the mutations were designed increase stability of by analyzing 3D structure and sequence other FGFs. Palifermin, N-terminal truncated is known have improved was used control our study. The K126 K178 substituted into glutamate form salt bridge with neighboring residue R175 respectively A120C mutation introduced close vicinity disulfide bond between C133 C137. data Circular Dichroism (CD) showed that all mutant proteins tested had higher T m value than Palifermin A120C/K126E/K178E 15.24 °C Palifermin. results cell proliferation activity soluble analyzed sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) after 37 or 45 incubation exhibited A120C-including improved. These suggest amino acid at surface enhanced thermal make more useful for pharmaceutical cosmetical application.