Graduation Year


Document Type




Degree Name

Doctor of Philosophy (Ph.D.)

Degree Granting Department


Major Professor

Jianfeng Cai, Ph.D.

Committee Member

Shengqian Ma, Ph.D.

Committee Member

Kirpal Bisht, Ph.D.

Committee Member

Feng Cheng, Ph.D.


γ-AApeptide, antimicrobial agents, protein interaction, OBTC library, left-handed peptidomimetic foldamers


Peptidomimetics are synthetic foldamers that expected more resistant to proteolytic degradation and enormous chemodiversity when compared with peptides. To date, the functional peptidomimetics such as β-peptides, peptoids, oligoureas, etc have been developed in many science fields. In order to explore the unnatural foldameric architectures, it’s necessary to discover the novel frameworks and molecular scaffolds. γ-AApeptides were reported to be a new class of peptidomimetics that showed its potential applications in drug discovery and chemical biology. However, a wide function and property of γ-AApeptides need to be further explored. To expand the potential application of γ-AApeptides in biochemistry, I have been focusing on the development of bioactive peptidomimetics, such as exploring the antibacterial activity of helical 1:1 α-sulfono-γ-AA heterogeneous peptides, developing the helical peptidomimetic as the inhibitor of the protein Ras_Raf interaction, identifying the protein/peptide ligands by the novel one-bead-two compound macrocyclic γ-AApeptide screening library, and elucidating the de novo dragon-boat-shaped synthetic foldamers.

Included in

Chemistry Commons