| Institution: | 1. School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, 510006 P.R. China
These authors contributed equally to this work.;2. School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, 510006 P.R. China;3. School of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006 P.R. China;4. School of Basic Medical Sciences, Lanzhou University, Lanzhou, 730000 P.R. China |
| Abstract: | A palladium-catalyzed cross-coupling reaction with aryl halide functionalities has recently emerged as a valuable tool for protein modification. Herein, a new fluorogenic modification methodology for proteins, with genetically encoded fluorosulfate-l -tyrosine, which exhibits high efficiency and biocompatibility in bacterial cells as well as in aqueous medium, is described. Furthermore, the cross-coupling of 4-cyanophenylboronic acid on green fluorescent protein was shown to possess a unique fluorogenic property, which could open up the possibility of a responsive “off/on” switch with great potential to enable spectroscopic imaging of proteins with minimal background noise. Taken together, a convenient and efficient catalytic system has been developed that may provide broad utilities in protein visualization and live-cell imaging. |
