2227199-79-1Relevant academic research and scientific papers
Suzuki Cross-Coupling Reaction with Genetically Encoded Fluorosulfates for Fluorogenic Protein Labeling
Zhao, Qian,Guo, Guoying,Zhu, Weiwei,Zhu, Liping,Da, Yifan,Han, Ying,Xu, Hongjiao,Wu, Shuohan,Cheng, Yaping,Zhou, Yani,Cai, Xiaoqing,Jiang, Xianxing
, p. 15938 - 15943 (2020)
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-tyro
Genetically encoding fluorosulfate- l -tyrosine to react with lysine, histidine, and tyrosine via SuFEx in proteins in vivo
Wang, Nanxi,Yang, Bing,Fu, Caiyun,Zhu, He,Zheng, Feng,Kobayashi, Tomonori,Liu, Jun,Li, Shanshan,Ma, Cheng,Wang, Peng G.,Wang, Qian,Wang, Lei
, p. 4995 - 4999 (2018)
Introducing new chemical reactivity into proteins in living cells would endow innovative covalent bonding ability to proteins for research and engineering in vivo. Latent bioreactive unnatural amino acids (Uaas) can be incorporated into proteins to react with target natural amino acid residues via proximity-enabled reactivity. To expand the diversity of proteins amenable to such reactivity in vivo, a chemical functionality that is biocompatible and able to react with multiple natural residues under physiological conditions is highly desirable. Here we report the genetic encoding of fluorosulfate-l-tyrosine (FSY), the first latent bioreactive Uaa that undergoes sulfur-fluoride exchange (SuFEx) on proteins in vivo. FSY was found nontoxic to Escherichia coli and mammalian cells; after being incorporated into proteins, it selectively reacted with proximal lysine, histidine, and tyrosine via SuFEx, generating covalent intraprotein bridge and interprotein cross-link of interacting proteins directly in living cells. The proximity-activatable reactivity, multitargeting ability, and excellent biocompatibility of FSY will be invaluable for covalent manipulation of proteins in vivo. Moreover, genetically encoded FSY hereby empowers general proteins with the next generation of click chemistry, SuFEx, which will afford broad utilities in chemical biology, drug discovery, and biotherapeutics.
Semisynthesis of a Bacterium with Non-canonical Cell-Wall Cross-Links
Chen, Jason S.,Dik, David A.,Schultz, Peter G.,Webb, Bill,Zhang, Nan
supporting information, p. 10910 - 10913 (2020/07/08)
The cell wall is an elaborate framework of peptidoglycan that serves to protect the bacterium against osmotic challenge. This exoskeleton is composed of repeating saccharides covalently cross-linked by peptide stems. The general structure of the cell wall is widely conserved across diverse Gram-negative bacteria. To begin to explore the biological consequence of introducing non-canonical cross-links into the cell wall of Escherichia coli, we generated a bacterium where up to 31percent of the cell-wall cross-links are formed by a non-enzymatic reaction between a sulfonyl fluoride and an amino group. Bacteria with these non-canonical cell-wall cross-links achieve a high optical density in culture, divide and elongate successfully, and display no loss of outer membrane integrity. This work represents a first step in the design of bacteria with non-canonical "synthetic"cell walls.
