Abstract by Shannon Smith
Chemistry and Biochemistry
Selective Stapling of Natural, Unprotected Amino Acids to Induce Helicity and Increase Peptide Stability
Peptides have long since been used as medications and therapies, but the issue with using peptides revolves around the body’s natural ability to break them down rendering them ineffective. For a peptide drug or therapeutic to be useful, it must remain in it’s primary, secondary, and tertiary structures in order to interact with cells and cause the desired effect. To address this issue many scientists have attempted stapling peptides. Stapling peptides will increase the helicity and stability of a peptide, allowing it to stand up against the many proteases and temperatures in the bodily environment. Unfortunately, in the past, this has come at the cost of using hydrophobic staples, or unnatural amino acids. Our goal is to create a small, hydrophilic, natural amino acid staple that increases helicity, melting temperature and stability of peptides. I have been manufacturing the peptide backbones which have varying tethers. These tethers allow for stapling under different buffered conditions. I have also been manufacturing two squaric acid staples that will be applied to the peptide back bones. Testing will be done to determine helicity, melting temp, and stability.