Date of Graduation

5-2026

Document Type

Thesis

Degree Name

Bachelor of Science in Chemistry

Degree Level

Undergraduate

Department

Chemistry & Biochemistry

Advisor/Mentor

Thallapuranam, Suresh

Abstract

Human Fibroblast Growth Factors (FGFs) are a family of 22 signaling proteins that have an essential role in all phases of healing as they regulate important cellular processes. However, current treatments using growth factor proteins are limited as these proteins are unstable, resulting in short therapeutic half-lives. This research aims to characterize a novel fibroblast growth factor variant referred to as N-terminal SuperFGF-1 mutant, which was designed to incorporate the best features of three growth factors to create a stable and long-lasting treatment that could revolutionize wound care and significantly improve outcomes. The N-terminal SuperFGF-1 mutant was developed by introducing five N-terminal mutations derived from the sequence of Fibroblast Growth Factor-10 (FGF-10) into the previously engineered hyper-stable SuperFGF-1 protein. SuperFGF-1 was designed by the Kumar Lab and was developed by incorporating five stabilizing mutations into the sequence of wild-type FGF-1. SuperFGF-1 had improved thermal and proteolytic stability, however its affinity to heparan was drastically reduced. The novel N-terminal SuperFGF-1 mutant was designed to restore the heparan interaction by introducing positively charged lysine residues that mirror the secondary heparan sulfate binding site of FGF-10.

Based on the data achieved from the experiments, the N-terminal SuperFGF-1 mutant successfully combines the exceptional stability of SuperFGF-1 and the high heparin-binding affinity of FGF-10 within a single novel protein. This research also establishes N-terminal SuperFGF-1 mutant as a promising candidate for future chronic wound treatments and future studies.

Keywords

Proteins; Fibroblast Growth Factors; Chronic Wounds; SuperFGF1; FGF10; Diabetic Ulcers

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Available for download on Saturday, May 01, 2027

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