Naturally occurring antimicrobial peptides (AMPs) are amphipathic molecules that have been shown to eliminate a wide range of bacteria. The hydrophilic regions of AMPs have an abundance of lysine and arginine amino acid residues, which are protonated and positively charged under physiological conditions. Due to electrostatic attraction, the positively charged AMPs bind with the negatively charged bacterial cell membrane and promote cell death. Literature on AMPs mimics has shown, however, that depending upon the prevalence of either lysine or arginine, the mechanism of cell death varies from membrane disrupting to cell penetrating, respectively. The goal of this research, therefore, is to determine the bacterial toxicity and selectivity of AMP mimics that are comprised of varying ratios of aminopropyl methacrylamide (APMA), a lysine mimic, and guanadinopropyl methacrylamide (GPMA), an arginine mimic, and analyze how compositional changes affect the mechanism of cell death in gram-positive (B. subtilis) and gram-negative (E. coli) bacteria. This is accomplished through the synthesis, via RAFT polymerization, of various statistical copolymers that demonstrate well-defined compositional ratios of APMA and GPMA, antimicrobial, biocompatibility and membrane disruption testing.

Polymeric antimicrobial peptide mimics containing primary amine and guanidinium moieties prepared via aqueous RAFT polymerization

246th National Meeting (2013)

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