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
Sheri Moxley
Second Committee Member
Crystal Archer
Third Committee Member
Paolo Mantero
Fourth Committee Member
Suresh Thallapuranam
Abstract
Fibroblast growth factors (FGFs) are a type of cell signaling proteins and play a major role in many cellular activities like embryonic development, cell growth, cell proliferation, cell differentiation, and wound healing. FGF1 is the protein of interest in this research project and belongs to the FGF1 subfamily, which consists of paracrine FGFs that play major roles in cell proliferation. FGF1s are extremely unstable and bind to heparin to operate at maximum activity, but their metabolic effects make them great candidates for more advanced wound-healing therapies. The Kumar Research Group previously designed a hyper stable FGF1, called “Super Fibroblast Growth Factor 1” (SFGF1), that contained five amino mutations. Two of the mutations were in the protein’s heparin binding pocket, which decreased its affinity to heparin. After purification and characterization of SFGF1, data showed decreased heparin binding and increased stability. The focus of this research project is changing the amino acid sequence of SFGF1 from cysteine to serine at position 131, which is exposed and on the exterior of the protein. Exterior cysteines possess the ability to intermolecularly disulfide bond, causing the formation of dimers or aggregates. By eliminating the exposed cysteine, the extent of its reactivity and role in metabolism and stability is investigated. This mutant C131S (SFGF1) was expressed through production of E. Coli and purified by affinity chromatography using a heparin sepharose column. Then, characterization experiments were completed for both C131S (SFGF1) and SFGF1 and the results were compared.
Based on the data achieved, the mutation does not affect the stability and biological activity of SFGF1. Therefore, the exposed cysteine’s intermolecular disulfide bond capabilities do not have a major role in the hyper stabilization of SFGF1.
Keywords
Fibroblast Growth Factors; Cysteine; Serine
Citation
Lauret, E. (2026). Design and characterization of hyper-stable fibroblast growth factor (Super FGF1) with single point mutation. Chemistry & Biochemistry Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/chbcuht/63
