Abstract by Dallin Ashton

Personal Infomation

Presenter's Name

Dallin Ashton

Degree Level


Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

Josh Price


Interhelical stapling using PEG


The coiled coil motif is a common structure in many biologically relevant peptides and proteins. This motif derives its functional structure from interactions between alpha helices that wrap around each other to form oligomers. The interactions between the helices are usually dominated by the hydrophobic effect and interhelical salt bridges. Previous work in the Price lab has shown that a polyethylene glycol (PEG) linker covalently attached on both ends to a single -sheet peptide (stapling), has the capacity to stabilize the peptide, which leads to a increased proteolytic stability. We tested this technique that has worked well within a single peptide to a coiled coil system where it is used to form an interhelical covalent link. When the PEG staple is used to connect the two helices, the conformational stability of the dimer increases.