Date of Award

Spring 5-2014

Degree Type

Honors College Thesis

Department

Polymers and High Performance Materials

First Advisor

Sarah E. Morgan

Advisor Department

Polymers and High Performance Materials

Abstract

Each day, antibiotic resistance affects the livelihood of individuals worldwide, especially in relation to hospital-acquired diseases. In an effort to combat this resistance, antimicrobial peptides, small biopolymers produced naturally by multicellular organisms, can be used to selectively eliminate bacteria and have demonstrated great potential as alternatives to conventional antibiotics. Many naturally-occurring antimicrobial peptides possess high concentrations of lysine and arginine amino acid residues, which are protonated and positively-charged at physiological pH. Herein, we describe the design and synthesis of antimicrobial peptide mimics, using amino acid mimics. N-3-aminopropyl methacrylamide (APMA) and 3-guanidinopropyl methacrylamide (GPMA) monomers mimic the amino acid residues lysine and arginine, respectively. Statistical copolymers of these two monomers were synthesized via aqueous reversible addition-fragmentation chain transfer (RAFT) polymerization and exhibited antimicrobial activity and low eukaryotic cell toxicity. To further analyze the mode of activity of these antimicrobial peptide mimics, large unilamellar vesicles (LUVs) containing fluorescent dye were prepared in an attempt to study the mechanisms of copolymer interactions with bacteria. . Developing a greater understanding of the relationship between the structure of synthetic antimicrobial peptide mimics and their respective mode of antimicrobial activity will aid in the design of tailored systems to target specific bacterial species.

Comments

Honors College Award: Top Thesis

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