92210-90-7

Upstream product

• 55477-80-0 methyl 2-[(tert-butoxycarbonyl)amino]acrylate 
• 108-98-5 thiophenol 
• 2766-43-0 N-tert-butyloxycarbonyl-L-serine methyl ester 
• 1621706-89-5 C₉H₁₅NO₇S 
• 369-57-3 benzenediazonium tetrafluoroborate 
• 172749-96-1 (S)-methyl 2-((tert-butoxycarbonyl)amino)-3-mercaptopropanoate 
• 187035-34-3 (S)-2-tert-butoxycarbonylamino-3-methanesulfonyloxypropionic acid methyl ester 

Relevant academic research and scientific papers

Modelling the Inhibition of Selenoproteins by Small Molecules Using Cysteine and Selenocysteine Derivatives

Small molecule-based electrophilic compounds such as 1-chloro-2,4-dinitrobenzene (CDNB) and 1-chloro-4-nitrobenzene (CNB) are currently being used as inhibitors of cysteine- and selenocysteine-containing proteins. CDNB has been used extensively to determine the activity of glutathione S-transferase and to deplete glutathione (GSH) in mammalian cells. Also, CDNB has been shown to irreversibly inhibit thioredoxin reductase (TrxR), a selenoenzyme that catalyses the reduction of thioredoxin (Trx). Mammalian TrxR has a C-terminal active site motif, Gly-Cys-Sec-Gly, and both the cysteine and selenocysteine residues could be the targets of the electrophilic reagents. In this paper we report on the stability of a series of cysteine and selenocysteine derivatives that can be considered as models for the selenoenzyme–inhibitor complexes. We show that these derivatives react with H2O2 to generate the corresponding selenoxides, which undergo spontaneous elimination to produce dehydroalanine. In contrast, the cysteine derivatives are stable towards such elimination reactions. We also demonstrate, for the first time, that the arylselenium species eliminated from the selenocysteine derivatives exhibit significant redox activity by catalysing the reduction of H2O2 in the presence of GSH (GPx (glutathione peroxidase)-like activity), which suggests that such redox modulatory activity of selenium compounds may have a significant effect on the cellular redox state during the inhibition of selenoproteins.

Nucleophile promoted gold redox catalysis with diazonium salts: C-Br, C-S and C-P bond formation through catalytic Sandmeyer coupling

Gold-catalyzed C-heteroatom (C-X) coupling reactions are evaluated without using sacrificial oxidants. Vital to the success of this methodology is the nucleophile-assisted activation of aryldiazonium salts, which could be an effective oxidant for converting Au(i) to Au(iii) even without the addition of an assisting ligand or photocatalyst. By accelerating the reaction kinetics to outcompete C-C homo-coupling or diazonium dediazoniation, gold-catalyzed Sandmeyer reactions were achieved with different nucleophiles, forming C-Br, C-S and C-P bonds in high yields and selectivities.

A DEHYDROALANINE ROUTE TO AN ACTIVATED PHENOLIC SPARSOMYCIN ANALOG

The addition of p-mercaptophenol to an N-protected dehydroalanine methyl ester is utilized in the synthesis of novel activated sparsomycin analog MDL 20,093.