Date of Graduation


Document Type


Degree Name

Bachelor of Science in Chemistry

Degree Level



Chemistry & Biochemistry


Thallapuranam, Suresh

Committee Member/Reader

Aloia, Lindsey

Committee Member/Second Reader

Dong, Bin

Committee Member/Third Reader

Chapman, Kate


The FGF-1 subfamily, composed of FGF-1 and FGF-2, assists in broad health-related processes such as cell proliferation and angiogenesis respectively.1,2 The subfamily shows promising signs as a therapeutic, however, the inherent thermal instability leads to a low half-life in vivo.3 To assist in improving the stability, FGF-1 and FGF-2 were connected via a 12-residue glycine linker ultimately producing a heterodimer. This heterodimer was further examined to discover its novel properties. Inspiration for this project was drawn from previous research which performed five mutations on FGF-1 ultimately improving stability in the protein complex. In addition to these five mutations on the FGF-1, sequence homology highlighted six residues on FGF-2 that could improve stability. Working with the second mutation on FGF-2 or the seventh mutation total, the heptamutant was a point mutation of K119N where a positively charged lysine was exchanged with a polar uncharged asparagine. The goal of this mutation was to reduce the overall positive charge on a region of the FGF-2 molecule called the heparin-binding pocket via a substitution. This mutation was believed to reduce the electrostatic strain, thus stabilizing the molecule. The structures and stability were tested to determine the impact of this mutation on the heterodimer. It was found that the mutation did not impact the secondary or tertiary structures. The Differential Scanning Calorimetry for the heptamutant demonstrated an increase in Tm of 7.61 °C compared to the wild-type. Similarly, a urea denaturation test showed an increase of Cm of approximately 1 M. Overall, it was found that the mutation increased stability without compromising a structural change showing promising signs for further endeavors towards wound healing applications.


Fibroblast Growth Factor, FGF, Cell Proliferation, Angiogenesis, FGF-1-FGF-2 Heterodimer

Available for download on Sunday, March 01, 2026