Date Approved

9-8-2021

Embargo Period

9-10-2021

Document Type

Thesis

Degree Name

M.S. Pharmaceutical Sciences

Department

Chemistry and Biochemistry

College

College of Science & Mathematics

Advisor

Gregory A. Caputo, Ph.D.

Committee Member 1

Timothy Vaden, Ph.D.

Committee Member 2

Venkatesh Nemmara, Ph.D.

Keywords

antimicrobial resistance, antimicrobial agents, peptides, polymethacrylates, hydrophobicity

Subject(s)

Anti-infective agents; Peptide antibiotics; Antimicrobial polymers

Disciplines

Medicinal and Pharmaceutical Chemistry

Abstract

Due to the increase prevalence of antimicrobial resistance (AMR) antibiotic alternatives have been of great interest. Antimicrobial peptides (AMPs) and polymers like polymethacrylates that mimic AMPs are two non-traditional antimicrobial agents that have been investigated thoroughly over the years as a potential solution to the AMR problem. This study will further the understanding of the L1 peptide by investigating the role hydrophobic amino acids have on the antimicrobial activity. Biophysical and microbiological techniques were utilized to show that the L1 hydrophobic derivative showed enhanced binding to anionic lipid bilayers while maintaining low hemolytic activity. This study also elucidates the effect of charge and hydrophobicity on polymethacrylate polymers by imploring the same techniques and methods used to investigate the Ponericin L1 peptide. These results indicate that both charge and hydrophobicity have an impact on activity and selectivity. As hydrophobicity increased, so did the hemolytic activity, suggesting a balance between hydrophobicity and charge is needed to optimize antimicrobial activity as well as selectivity. Overall, the results show that these AMPs and polymethacrylates have great potential as a platform against AMR.

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