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.
","abstract_html":"<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>","abstract_has_math":false,"creators":["Filani, Oluwadamilola"],"institution":null,"degree_name":"Master of Science","degree_level":null,"degree_discipline":"Department of Chemistry","degree_department":null,"school":null,"contributors":["Rajalingam Dakshinamurthy (Director) , Cathleen Webb, and Kevin Williams"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-10-01T07:00:00Z","date_published":"2015-10-01T07:00:00Z","updated_at":"2026-07-24T06:08:52Z","subjects":["FGFR-2. FGF-1","FGF","Biochemistry, Biophysics, and Structural Biology","Cell and Developmental Biology","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.wku.edu/theses/1549","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Rajalingam Dakshinamurthy (Director) , Cathleen Webb, and Kevin Williams"]},{"key":"dc:creator","label":"Author","values":["Filani, Oluwadamilola"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Department of Chemistry"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["FGFR-2. FGF-1","FGF","Biochemistry, Biophysics, and Structural Biology","Cell and Developmental Biology","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.wku.edu/theses/1549"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:title","label":"Title","values":["Expression and Purification of Unlabelled and Isotopically Labelled Human Fibroblast Growth Factor-1 and its Receptor Relevance in Cancer Research"]}]}],"canonical_facts":{"dc:contributor":["Rajalingam Dakshinamurthy (Director) , Cathleen Webb, and Kevin Williams"],"dc:creator":["Filani, Oluwadamilola"],"dc:description.abstract":["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.
"],"dc:identifier":["https://digitalcommons.wku.edu/theses/1549"],"dc:subject":["FGFR-2. FGF-1","FGF","Biochemistry, Biophysics, and Structural Biology","Cell and Developmental Biology","Chemistry"],"dc:title":["Expression and Purification of Unlabelled and Isotopically Labelled Human Fibroblast Growth Factor-1 and its Receptor Relevance in Cancer Research"],"dc:type":["Thesis"],"thesis:degree_discipline":["Department of Chemistry"],"thesis:degree_name":["Master of Science"]},"updated_at":"2026-07-24T06:08:52Z"}