Investigating the interaction of azobenzene moiety on the aromatic amino acid tryptophan

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 this work, we investigated the possible interaction between azobenzene and aromatic amino acids. We hypothesized that aromatic amino acids, such as tryptophan, would show altered photochemical properties when conjugated with azobenzene. When irradiated at either 365 nm or 465 nm, the molecule now lacks the usually characteristic photoswitch capabilities and is visibly fluorescent at 365 nm. To our 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.

Automated summary

In this study, the possible interaction between azobenzene and aromatic amino acids was investigated, and evidence was found suggesting that primary protein structure could affect photoswitch activity. This research is of significance for further understanding the application of azobenzenes in biomolecules.