Date of Graduation

5-2016

Document Type

Thesis

Degree Name

Bachelor of Science

Degree Level

Undergraduate

Department

Chemistry & Biochemistry

Advisor/Mentor

Kumar, T.K.S.

Committee Member/Reader

Greathouse, Denise

Committee Member/Second Reader

Henry, Leah Jean

Committee Member/Third Reader

Goodman-strauss, Chaim

Abstract

Fibroblast growth factors (FGFs) are family of proteins that belong to a group of growth factors that are found in mammals and play an important role in angiogenesis, differentiation, organogenesis, and tissue repair. In summary, their main functionality is involved in cell division and proliferation. Because FGFs plays such a vital role in cell proliferation, they are mainly involved in the process of wound healing and injuries. FGF binds to its ligand, heparin—a heavily sulfated glycosaminoglycan. The binding of heparin to FGF occurs through electrostatic interactions, specifically between the negatively charged sulfate groups on heparin and positively charged residues such as arginine and lysine in the heparin binding pocket of FGF.

FGF1, a prototype of the FGF family, has many potential applications since it is heavily involved in wound healing, however, FGF1 does not remain active for very long when it is not bound to heparin. With this in mind, this research project focuses on increasing the half-life of FGF1 while maintaining its stability. To achieve this objective, residue threonine at position 137, which is located near the heparin binding pocket was mutated to glutamic acid. Preliminary biophysical characterization of the mutant FGF1 protein has been discussed in this dissertation.

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