Year: 2020
Type: dissertation
Abstract: Non-natural peptide mimics are referred to as peptidomimetics, which contains unnatural backbones that mimic the primary peptide structure. There are a large number of peptidomimetics that have been developed including α-peptides, β-peptides, peptoids, arylamide oligomers, cationic polymers, and other peptidomimetics in the last decades. Compared to conventional peptides, these peptidomimetics have many advantages such as resistance to proteolysis, improved bioavailability, and reduced immunogenicity. However, the development of peptidomimetics is still far below the expectation due to the limitation of the availability of backbones. It is an urgent need to generate a new diverse library for novel drug discovery, design antimicrobial agents, and disrupt protein-protein interaction, etc. In the commitment to the development of a new class of peptidomimetics, our group describes a family of chemically diverse peptidomimetics based on the backbone of γ-chiral peptide nucleic acid (γ-PNA). They are termed “γ -AApeptides” because they are comprised of γ -substituted-N-acylated-N-aminoethyl amino acids. In this dissertation, I explored the development of three key aspects of γ-AApeptides. Firstly, the lipo-γ-AApeptides as a new class of antimicrobial peptidomimetics that mimic the bactericidal functions of Host-defense peptides (HDPs). Secondly, γ-AApeptides applied to the development of combinatorial chemistry. Finally, the synthetic γ-AApeptide as protein mimics. The findings in this dissertation may lead to the development of a new class of antimicrobial agents and novel drug discovery.
Author: Wei, Lulu
Institution: University of South Florida
Language: English
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W7056115351