Date of Graduation
5-2015
Document Type
Thesis
Degree Name
Bachelor of Science
Degree Level
Undergraduate
Department
Chemistry & Biochemistry
Advisor/Mentor
Kumar, T.K.S.
Committee Member/Reader
Schulte, Stephanie
Committee Member/Second Reader
Adams, Paul
Committee Member/Third Reader
Billings, Sabrina
Abstract
Fibroblast Growth Factors (FGFs) are heparin-binding proteins known for their involvement in various biological processes such as cell differentiation and wound healing.1 The heparin binding site of FGF-1 displays a unique stretch of positive amino acid sequence and facilitates a very strong binding to negatively charged heparin due to the formation of electrostatic interaction. The aim of this study is to analyze and modify the novel antimicrobial peptide sequence (GST-HB) designed based on the heparin-binding region of FGF-1 as well as other polycationic microbial sequences. These aspects will be examined using various experimental techniques including overexpression of GST-HB, purification using one-step affinity column chromatography, and bacterial assays. The binding affinity of FGF’s to heparin is a crucial component to bacterial infection pathways. Therefore, antimicrobial applications will be determined for the recombinant GST-HB peptide for future medical treatments of bacterial infections.
Citation
Power, A. M. (2015). Design of antimicrobial peptide based on the heparin binding segment of FGF-1. Chemistry & Biochemistry Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/chbcuht/4