Reflecting recent work in the Wiedman

Azobenzenes are a series of compounds that can be isomerized upon irradiation with light. These molecules can modify the physical, chemical, and biological properties of a diverse range of materials. They can control protein structure and function with temporal and spatial precision. In work published in Peptide Science, Charnette Frederic in the Gregory R. Wiedman group, investigated the possible interaction between azobenzene and aromatic amino acids.

Charnette and Greg hypothesized that aromatic amino acids, such as tryptophan, would show altered photochemical properties when conjugated with azobenzene. When irradiated at either 365nm or 465nm, the molecule now lacks the usually characteristic photoswitch capabilities and is visibly fluorescent at 365nm.

To their knowledge, this is the first evidence to suggest that primary protein structure could affect photoswitch activity. The knowledge gained from this research will help to further the understanding of azobenzenes as they are used in biomolecules.