6968-11-2Relevant articles and documents
Visible-Light-Mediated S?H Bond Insertion Reactions of Diazoalkanes with Cysteine Residues in Batch and Flow
Chen, Lin,Cui, Yu-Sheng,Duan, Xiu,Guo, Kai,Qin, Long-Zhou,Qiu, Jiang-Kai,Sun, Qi,Yuan, Xin,Zhuang, Kai-Qiang
supporting information, p. 5093 - 5104 (2020/09/23)
We describe the application of S?H bond insertion reactions of aryl diazoacetates with cysteine residues that enabled metal-free, S?H functionalization under visible-light conditions. Moreover, this process could be intensified by a continuous-flow photomicroreactor on the acceleration of the reaction (6.5 min residence time). The batch and flow protocols described were applied to obtain a wide range of functionalized cysteine derivatives and cysteine-containing dipeptides, thus providing a straightforward and general platform for their functionalizations in mild conditions. (Figure presented.).
Application of a novel small scale UV LED photochemical batch reactor for the thiol-yne reaction
Griebenow, Nils,Br?se, Stefan,Dilmac, Alica M.
, p. 54301 - 54303 (2015/07/01)
The application of a novel small scale UV LED photochemical batch reactor for the thiol-yne click reaction was investigated. Optimization of the reaction conditions yielded high conversions. Finally, the methodology could be successfully expanded to the one pot insertion of functionalized alkynes into the disulfide bond of a cysteine derivative.
Acyl transfer from carboxylate, carbonate, and thiocarbonate esters to enzymatic and nonenzymatic thiolates
Gravel, Christian,Lapierre, Danielle,Labelle, Judith,Keillor, Jeffrey W.
, p. 164 - 174 (2008/02/13)
Transglutaminases (EC 2.3.2.13) (TGases) catalyze calcium-dependent acyl transfer reactions between peptide-bound glutamine residues as acyl donors and peptide-bound lysine residues as acyl acceptors, resulting in the formation of intermolecular ε-(γ-glutamyl)lysine crosslinks. The mechanistic details of its "ping-pong" transamidation reaction remain unknown. In particular, few studies have been published probing the nucleophilicity of TGase using acyl-donor substrates of varied electrophilicity. Herein we report the synthesis of activated esters of carbonates, carbamates, and thiocarbonates and their reactions with simple thiols, as a nonenzymatic point of reference, and with the catalytic cysteine residue of guinea pig liver TGase. Our kinetic results show that the simple substitution of a side chain methylene unit by oxygen or sulphur had a surprising effect on both substrate affinity and acylation reactivity. Furthermore, they provide unexpected insight into the importance of a side chain heteroatom for conferring affinity for tissue TGase as well as revealing an interesting class of irreversible inhibitors.