Graduation Year

2023

Document Type

Dissertation

Degree

Ph.D.

Degree Name

Doctor of Philosophy (Ph.D.)

Degree Granting Department

Chemistry

Major Professor

Jianfeng Cai, Ph.D.

Committee Member

Feng Cheng, Ph.D.

Committee Member

Kirpal Bisht, Ph.D.

Committee Member

Wayne Guida, Ph.D.

Keywords

Enzyme-like catalyst, Hydrolysis, Alzheimer’s disease, Aβ inhibition, macrocyclic combinatorial library

Abstract

This dissertation investigates the multifaceted utility of γ-AA peptides in various biological contexts, highlighting their capability in mimicking bioactive proteins, facilitating novel drug discovery, and obstructing protein-protein interactions. Initially, we introduced the design of an ingenious γ-AA peptide scaffold that replicates the hydrolysis capabilities of natural enzymes, with the intention to overcome their stability limitations. Notably, the designed catalyst exhibited excellent esterase activity with the coordination of Zn2+. Subsequently, optimization of a linear γ-AA peptide compound through a dimeric strategy resulted in P3-1, a potent inhibitor of amyloid-β 42. Evidenced by both in vivo and in vitro experiments, its potential for contributing to the early detection and treatment of Alzheimer's Disease was demonstrated. Furthermore, the investigation of cyclic γ-AA peptide library was pursued as an efficient strategy for uncovering bioactive molecules. Two compounds, P4-1, and P4-2, identified from the macrocyclic combinatorial library, displayed a remarkable binding affinity towards Prostaglandin E2 receptor 2, marking a significant stride towards the development of potential therapeutics.

Included in

Chemistry Commons

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