Date of Graduation

5-2025

Document Type

Thesis

Degree Name

Bachelor of Science in Biology

Degree Level

Graduate

Department

Biological Sciences

Advisor/Mentor

Thallapuranam, Suresh

Committee Member

Du, Yuchun

Second Committee Member

Walker, Kate

Third Committee Member

Wheeler, Jill

Abstract

The Fibroblast Growth Factor family consists of 23 different fibroblast growth factors (FGFs) that are each involved in various cellular processes, including cell proliferation and tissue repair. Fibroblast growth factor receptors (FGFR) are different tyrosine kinase receptors. There are four FGFRs in the human body, each binding to different combinations of FGFs. Fibroblast growth factor 1 (FGF1) is the only FGF that can bind with all four types of fibroblast growth factor receptors. Therefore, it is the most powerful mitogen. However, FGF1 has low thermodynamic stability under the physiological conditions. Prior work in the Kumar lab has constructed several points of mutations on FGF1 to create a more stable version of the universal mitogen (FGF1) with higher biological activity that is named super FGF1. Super FGF1 also lacks heparin binding.

My project focus is to design one point mutation on the N-terminus of Super FGF1 (C10K) to investigate if it will affect the heparin binding affinity, structural properties, and biological activity of the mitogen. The one-point mutation is resembled from the sequence of amino acids of fibroblast growth factor 10 (FGF10). FGF10 has a key role in keratinocyte growth in the human body. Therefore, the aim of the project is to produce a version of FGF1 that has the stability of superFGF1 and the keratinocyte growth activity of FGF10.

After finishing the experiments and research, it can be concluded that the one-point mutation, C10K (Super FGF1), does not affect the thermal, chemical, or biological activity of the protein.

Keywords

Fibroblast growth factor; heparin; Super FGF1; C10K

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