Date of Thesis

Spring 2022


Interactions between proteins that regulate how the protein complex, as a whole, functions are integral to almost every biological function. Many diseases result when normal protein-protein interactions (PPIs) are altered, and the ability to manipulate these PPIs would enable the development of new classes of therapeutic agents. α-helices are a type of protein secondary structure that are commonly found at the interface between two proteins. There is a large body of ongoing research into the development of short protein fragments, or peptides, that can be engineered to fold into an α-helical structure to mimic a natural PPI. However, most peptides do not spontaneously fold into an α-helical structure, which is needed to mimic native biological interactions for the peptide to have a better binding affinity to the protein of interest. In this study, we have designed peptides to bind to and prevent the function of Ribose-5-phosphate isomerase B (RPIB), a relevant target in the development of new treatments for parasitic diseases. We have utilized four different crosslinking strategies to induce an α-helical fold, including metal-binding hybrid-coordination motifs, ring-closing metathesis reactions, thioether crosslinks, and lactam bridges.


protein, secondary structure, protein folding

Access Type

Honors Thesis (Bucknell Access Only)

Degree Type

Bachelor of Science


Cell Biology/Biochemistry

Minor, Emphasis, or Concentration

Classics & Mediterranean Studies

First Advisor

Sarah Smith