Ellingson, Mikael2020-09-222020-09-222020https://hdl.handle.net/11299/216282Faculty Advisor: William C.K. PomerantzThough bromodomain and extraterminal (BET) family proteins are important epigenetic regulating proteins, high sequence similarity makes selective binding challenging. Molecules selective to the N-terminal bromodomain of the human bromodomain-containing protein, BRD4, have only been characterized recently and have spurred on therapeutic applications of BET inhibition. Here, the affinity of a BRD4-selective 1,4,5-trisubstituted imidazole scaffold is improved ~14-fold with the addition of a N,N-dimethyl ethylamine moiety as measured by a fluorescence polarization assay. This improvement is hypothesized to be due to electrostatic interactions with a nearby aspartic acid residue. Limitations of this characterization and conclusion are discussedenCollege of Science and EngineeringDepartment of ChemistryReport