Date of Graduation
5-2026
Document Type
Thesis
Degree Name
Bachelor of Science in Chemistry
Degree Level
Undergraduate
Department
Chemistry & Biochemistry
Advisor/Mentor
Suresh Thallapuranam
Committee Member
Kate Walker
Second Committee Member
Margaret Hershberger
Abstract
Fibroblast Growth Factors (FGF) are a family of 23 proteins responsible for certain biological functions, such as angiogenesis, cell proliferation, metabolism, and wound healing. FGF1 is a universal ligand and stimulates cell proliferation in and around the wound. FGF2 stimulates angiogenesis, the growth and degradation of blood vessels, and endothelial cell survival. As both FGF1 and FGF2 are powerful wound-healing agents, an FGF1/FGF2 heterodimer was designed and created in Dr. Kumar’s Lab to enable dual signaling to both proteins, aiding in more effective and efficient wound healing. The FGF1/FGF2 dimer showed increased thermal stability and bioactivity compared to FGF1 and FGF2 alone. A mutation of cysteine to serine at position 101 on FGF2 was introduced in the sFGF1/FGF2 dimer, which was theorized to increase the dimer’s activity, prolong its half-life, and enhance its stability compared to the wtFGF1/FGF2 dimer. Additionally, using Super FGF1 (sFGF1), a hyper-stable variant of wtFGF1, in the dimer has the potential to aid in stability and biological activity. The specific aims of this research project were the overexpression and purification, characterization of the structure and stability, and the comparison of cell proliferation activity of the wtFGF1/FGF2 dimer and the sFGF1/C101SFGF2 dimer. The tertiary and secondary structures of the protein were unaffected by the mutation, as shown by circular dichroism and fluorescence spectroscopy. The mutated dimer was more thermally stable than wtFGF1 and the wtFGF1/FGF2 dimer, as determined by differential scanning calorimetry. Furthermore, the sFGF1/C101SFGF2 dimer was more resistant to trypsin and thrombin digestion compared to wtFGF1 and the wtFGF1/FGF2 dimer, as seen in the time-dependent trypsin and thrombin digestion results. Lastly, the C101S mutation did not affect the protein’s cell proliferative activity but rather showed higher overall activity than wtFGF1 and the wtFGF1/FGF2 dimer, largely due to improved stability.
Keywords
Fibroblast Growth Factors; FGF; Super FGF1; FGF1/FGF2 Dimer; Chronic Wounds; Cell Proliferation
Citation
Coppens, O. R. (2026). Design and Characterize a Single Mutation (C101S) on FGF2 of the sFGF1/FGF2 Dimer. Chemistry & Biochemistry Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/chbcuht/72
