Article
Investigating the Interaction of Azobenzene Moiety on the Aromatic Amino Acid Tryptophan
Peptide Science
(2024)
Abstract
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.
Disciplines
Publication Date
March, 2024
DOI
10.1002/pep2.24334
Citation Information
Charnette Frederic and Gregory Wiedman. "Investigating the Interaction of Azobenzene Moiety on the Aromatic Amino Acid Tryptophan" Peptide Science Vol. 116 Iss. 2 (2024) p. e24334 ISSN: 2475-8817 Available at: http://works.bepress.com/gregory-wiedman/34/