613688-05-4Relevant articles and documents
Traceless Staudinger ligation enabled parallel synthesis of proteolysis targeting chimera linker variants
Bemis, Troy A.,La Clair, James J.,Burkart, Michael D.
supporting information, p. 1026 - 1029 (2021/02/06)
A parallel, one-pot assembly approach to proteolysis targeting chimeras (PROTACs) is demonstrated utilizing activated esters generatedin situ, and traceless Staudinger ligation chemistry. The method described allows for rapid structure-activity relationship studies of PROTAC linker variants. Two previously studied systems, cereblon and BRD4 degraders, are examined as test cases for the synthetic method. The two related strategies to assemble PROTAC linker variants discussed can accommodate the chromotographic separations capabilities of labs of many sizes and incorporates commercially available degrader building blocks, thereby easing synthetic entry into PROTAC chemical space.
A Versatile Approach for Site-Specific Lysine Acylation in Proteins
Wang, Zhipeng A.,Kurra, Yadagiri,Wang, Xin,Zeng, Yu,Lee, Yan-Jiun,Sharma, Vangmayee,Lin, Hening,Dai, Susie Y.,Liu, Wenshe R.
, p. 1643 - 1647 (2017/02/05)
Using amber suppression in coordination with a mutant pyrrolysyl-tRNA synthetase-tRNAPylpair, azidonorleucine is genetically encoded in E. coli. Its genetic incorporation followed by traceless Staudinger ligation with a phosphinothioester allows the convenient synthesis of a protein with a site-specifically installed lysine acylation. By simply changing the phosphinothioester identity, any lysine acylation type could be introduced. Using this approach, we demonstrated that both lysine acetylation and lysine succinylation can be installed selectively in ubiquitin and synthesized histone H3 with succinylation at its K4 position (H3K4su). Using an H3K4su-H4 tetramer as a substrate, we further confirmed that Sirt5 is an active histone desuccinylase. Lysine succinylation is a recently identified post-translational modification. The reported technique makes it possible to explicate regulatory functions of this modification in proteins.
Stereoselective N-glycosylation by Staudinger ligation
He, Yi,Hinklin, Ronald J.,Chang, Jiyoung,Kiessling, Laura L.
, p. 4479 - 4482 (2007/10/03)
(Chemical equation presented) Stereoselective methods for the chemical synthesis of β-N-glycosyl amides are needed to generate glycopeptides and glycoproteins. Here, we report that the Staudinger ligation can be used to form glycosylated asparagine deriva
