Expression and Purification of Unlabelled and Isotopically Labelled Human Fibroblast Growth Factor-1 and its Receptor Relevance in Cancer Research

<p>Studies show that fibroblast growth factors (FGFs) control variety of cellular activities such as mitosis, cell differentiation, survival and angiogenesis. The FGF family consists of 23 different heparin-binding proteins. One of the most intensively studied members is human FGF-1 (hFGF-1) because of its critical role in the formation of blood vessels and cell proliferation in some types of cancer. The biological activities of FGFs are primarily mediated via interactions with fibroblast growth factor receptors (FGFR) and are a potent target in cancer. In this study, we report an efficient affinity column purification of hFGF-1 and the D2 domain of FGFR-2 from bacterial expression followed by SDSPAGE analysis. Steady state fluorescence results showed that both proteins were in their native conformation. The 1 H-15N HSQC NMR analysis of hFGF-1 was further performed. The data confirmed the purity and well-conserved native state of the protein. The findings of this study can be used in designing hFGF-1 antagonists with competitive inhibition characteristics. These antagonists could result in possible inhibition of hFGF-1 cell proliferation and angiogenesis associated in tumorigenesis.</p>

Name thesis:degree_name

Master of Science

Discipline thesis:degree_discipline

Department of Chemistry

Year

2015

Author dc:creator

• Filani, Oluwadamilola

Contributors dc:contributor

• Rajalingam Dakshinamurthy (Director) , Cathleen Webb, and Kevin Williams

• FGFR-2. FGF-1
• FGF
• Biochemistry, Biophysics, and Structural Biology
• Cell and Developmental Biology
• Chemistry

Repository record dc:identifier

https://digitalcommons.wku.edu/theses/1549

OAI identifier oai:identifier

oai:digitalcommons.wku.edu:theses-2552