Travers, Jennifer A., authorWilliams, Robert M., advisor2022-11-282022-11-281996https://hdl.handle.net/10217/235829This Ph.D. project involved using the filamentous phage as a tool to express peptide libraries on its external appendage called the pIII protein. The peptide libraries were designed based on a motif of the honeybee toxin Apamin. Apamin is expressed on the end of the pIII protein and a portion of the apamin section is randomized to produce all possible combinations of amino acids to give a peptide library. The library phage are then panned on a derivatized solid support to determine if any library members have an affinity to a target ligand. The target chosen is a portion of the peptidoglycan layer in bacterial cells called L-lysine-D-alanine-D-alanine. This is the site for binding of the antibiotic vancomycin. Library members that bind to this site should have vancomycin-like activity. This project entailed preparing the libraries, synthesizing the ligand, and derivatizing a variety of solid supports for panning. Many different panning experiments were performed on several libraries and the results are described herein.doctoral dissertationsengCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.Peptides -- SynthesisBacteriophagesText