138038-96-7Relevant articles and documents
Methods and compositions for protein labeling using lipoic acid ligases
-
Sheet 15, (2016/04/05)
The present disclosure provides compositions and methods of use thereof for labeling peptide and proteins in vitro or in vivo. The methods described herein employ lipoic acid ligase or mutants thereof, and lipoic acid analogs (e.g., lipoic acid analogs comprising a resorufin moiety) recognized by lipoic acid ligase and lipoic acid ligase mutants. Also provided herein is a method of imaging protein-protein interaction via a reaction mediated by lipoic acid ligase.
Highly reactive trialkylsilylation reagents derived from bis(trifluoromethanesulfonyl)imide - Silylation of functional groups, alkines and reactive aromatics
Simchen, Gerhard,Jonas, Simon
experimental part, p. 506 - 512 (2011/10/17)
The synthesis of trialkylsilyl-bis(trifluormethanesulfonyl)imides 3 is described. Compounds 3 with bulky trialkylsilyl groups 3a,b only exist in the silatautomeric form 3a′,b′ under usual conditions, 3c in the N-trimethylsilyl structure. Despite of the bulky silyl substituents in 3a′,b′ their reactivity is higher than that of trimethylsilyltriflate. Alcohols, carbonyl compounds, nitroalkanes and carboxylic acid esters are silylated in good yields, especially by the more reactive triisopropylsilyl derivative 3b′ in presence of tertiary amines, tert.-Butyl carboxylates and benzylcarboxylates are cleaved. Monosubstituted alkines and electron-rich (hetero) aromatics are carbosilylated in presence of N-ethyl-diisopropylamine.