667905-05-7Relevant academic research and scientific papers
Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
Cao, Yuan,Nguyen, Giang K. T.,Tam, James P.,Liu, Chuan-Fa
, p. 17289 - 17292 (2015)
Using a recently discovered peptide ligase, butelase 1, we developed a novel method to access protein thioesters in good yield. We successfully combined it with native chemical ligation and sortase-mediated ligation in tandem for protein C-terminal labeling and dual-terminal labeling to exploit the orthogonality of these three ligation methods.
α-Methylphenacyl thioesters as convenient thioacid precursors
Hatanaka, Toru,Yuki, Ryosuke,Saito, Ryota,Sasaki, Kaname
supporting information, p. 10589 - 10592 (2016/11/30)
α-Methylphenacyl (Mpa) thioesters are described as precursors of thioacids. Mpa thioesters are accessible via the condensation of carboxylic acids and phenacyl thiol, which is easily prepared without column chromatography. The Mpa thioesters are selectively deprotected by reduction with zinc dust in the presence of conventional thioacid protecting groups. In addition, the Mpa group exhibits orthogonal reactivity to the Boc group. These features are expected to facilitate the preparation of complex thioacids, including those in peptides.
Cell-permeable small molecule probes for site-specific labeling of proteins.
Yeo, Dawn S Y,Srinivasan, Rajavel,Uttamchandani, Mahesh,Chen, Grace Y J,Zhu, Qing,Yao, Shao Q
, p. 2870 - 2871 (2007/10/03)
We have successfully synthesized a number of small molecule probes designed for site-specific labeling of N-terminal cysteine-containing proteins expressed in live cells. Their utility for site-specific, covalent modifications of proteins was successfully demonstrated with purified proteins in vitro, and with live bacterial cells in vivo.
