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
