154596-15-3Relevant articles and documents
Reversible and Tunable Photoswitching of Protein Function through Genetic Encoding of Azobenzene Amino Acids in Mammalian Cells
Luo, Ji,Samanta, Subhas,Convertino, Marino,Dokholyan, Nikolay V.,Deiters, Alexander
, p. 2178 - 2185 (2018)
The genetic encoding of three different azobenzene phenylalanines with different photochemical properties was achieved in human cells by using an engineered pyrrolysyl tRNA/tRNA synthetase pair. In order to demonstrate reversible light control of protein function, azobenzenes were site-specifically introduced into firefly luciferase. Computational strategies were applied to guide the selection of potential photoswitchable sites that lead to a reversibly controlled luciferase enzyme. In addition, the new azobenzene analogues provide enhanced thermal stability, high photoconversion, and responsiveness to visible light. These small-molecule photoswitches can reversibly photocontrol protein function with excellent spatiotemporal resolution, and preferred sites for incorporation can be computationally determined, thus providing a new tool for investigating biological processes.
Photoswitching of the enzymatic activity of semisynthetic ribonuclease S' bearing phenylazophenylalanine at a specific site
Hamachi, Itaru,Hiraoka, Takashi,Yamada, Yasuhiro,Shinkai, Seiji
, p. 537 - 538 (2007/10/03)
Photos witching of the enzymatic activity of ribonuclease S' was successfully carried out by site specific incorporation of phenylazophenylalanine into S-peptide skeleton by semisynthesis.