Dimerization of Tryptophan Sidechains in Peptides and Proteins

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This is a Faculty Early Career project. In research, the work will study ditryptophan crosslinking units within proteins. The ditryptophans are highly fluorescent and easily detected for that reason. The fluorescence will be studied in model systems with constrained geometries. Combinatorial chemistry will be used to optimize the ditryptophan chromophore formation. The work will determine the structural consequences of tryptophan dimerization within peptides. Hen egg white lysozyme will be used as a substrate and the work will demonstrate that fluorescence of ditryptophan units can be coupled to antibody binding. In education, Dr. VanVranken will develop a graduate class which applies advanced concepts in organic chemistry to biology, will organize a seminar at the biology/chemistry interface, and will mentor students from small colleges and minority students in research. This project will develop a light-initiated technique for stabilizing the structure of proteins. A fluorescent probe will result and it will be used to study biological events. The project will develop educational activities at the chemistry/biology interface and will involve mentoring minority students and students from small colleges.