A Palladium-Catalyzed Ullmann-Ziegler Cross-Coupling for Sterically Hindered Biaryls

Synthesis ◽  
2011 ◽  
Vol 2011 (08) ◽  
pp. 1249-1254 ◽  
Author(s):  
Richard Göttlich ◽  
Max Nüllen
2016 ◽  
Vol 52 (32) ◽  
pp. 5617-5620 ◽  
Author(s):  
Ran Ding ◽  
Zhi-Dao Huang ◽  
Zheng-Li Liu ◽  
Tian-Xiang Wang ◽  
Yun-He Xu ◽  
...  

Palladium-catalyzed intermolecular alkylation of enamides with α-bromo carbonyls was developed. Under mild reaction conditions, various cyclic and acyclic enamides reacted well with α-bromo carbonyls to afford the corresponding multi-substituted alkene products in good yields. The coupling products could be converted into very useful γ-amino acid, δ-amino alcohol, 1,4-dicarbonyl and γ-lactam derivatives.


2019 ◽  
Vol 21 (19) ◽  
pp. 7976-7981 ◽  
Author(s):  
Chengwei Liu ◽  
Roger Lalancette ◽  
Roman Szostak ◽  
Michal Szostak

ChemInform ◽  
2016 ◽  
Vol 47 (34) ◽  
Author(s):  
Ran Ding ◽  
Zhi-Dao Huang ◽  
Zheng-Li Liu ◽  
Tian-Xiang Wang ◽  
Yun-He Xu ◽  
...  

2020 ◽  
Author(s):  
Jian Cao ◽  
Ernest Armenta ◽  
Lisa Boatner ◽  
Heta Desai ◽  
Neil Chan ◽  
...  

Bioorthogonal chemistry is a mainstay of chemoproteomic sample preparation workflows. While numerous transformations are now available, chemoproteomic studies still rely overwhelmingly on copper-catalyzed azide –alkyne cycloaddition (CuAAC) or 'click' chemistry. Here we demonstrate that gel-based activity-based protein profiling (ABPP) and mass-spectrometry-based chemoproteomic profiling can be conducted using Suzuki–Miyaura cross-coupling. We identify reaction conditions that proceed in complex cell lysates and find that Suzuki –Miyaura cross-coupling and CuAAC yield comparable chemoproteomic coverage. Importantly, Suzuki–Miyaura is also compatible with chemoproteomic target deconvolution, as demonstrated using structurally matched probes tailored to react with the cysteine protease caspase-8. Uniquely enabled by the observed orthogonality of palladium-catalyzed cross-coupling and CuAAC, we combine both reactions to achieve dual protein labeling.


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