84624-28-2Relevant articles and documents
Method for selective structural modification of L-lysine
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Paragraph 0025; 0053-0057, (2020/07/15)
The invention belongs to the field of chemical synthesis, and particularly relates to a method for selective structural modification of L-lysine. According to a specific technical scheme in the invention, L-lysine is taken as a raw material, silicon dioxide nanoparticles surface-functionalized by beta-cyclodextrin are taken as a catalyst, water is taken as a solvent, and a reaction is performed for 3-5 hours at 25 DEG C in the presence of an amino protective agent to obtain a final product of the reaction; the final reaction product is subjected to standing, and an upper-layer product is takenand subjected to washing, separating and filtering to obtain selectively-modified L-lysine. The used catalyst is odorless and non-toxic; the synthesis method is simple; catalytic performance is excellent; product separation is easy; the catalyst can be repeatedly used; the method effectively solves the problem that a mixture of a common beta-cyclodextrin catalyzed product and cyclodextrin floatson a liquid level and is difficult to separate, simplifies post-treatment steps, reduces the use amount of an organic solvent, and greatly reduces the amount of waste liquid generated in the stage ofpurification.
Decomposition of copper-amino acid complexes by sodium sulfide
Nowshuddin, Shaik,Reddy, A. Ram
, p. 5159 - 5161 (2007/10/03)
Sodium sulfide very efficiently removes copper from protected amino acid-copper complexes. The copper in the amino acid complex was reduced to insoluble cuprous sulfide and the free amino acid was released in pure form. This method is very convenient and rapid, requiring only 5-10 min and 0.55-0.75 equiv of sodium sulfide.
Chemistry in living cells: Detection of active proteasomes by a two-step labeling strategy
Ovaa, Huib,Van Swieten, Paul F.,Kessler, Benedikt M.,Leeuwenburgh, Michiel A.,Fiebiger, Edda,Van den Nieuwendijk, Adrianus M. C. H.,Galardy, Paul J.,Van der Marel, Gijsbert A.,Ploegh, Hidde L.,Overkleeft, Herman S.
, p. 3626 - 3629 (2007/10/03)
In vivo targeting of the proteasome: Probe 1 is a cell-permeable irreversible inhibitor that alkylates the active-site residues of the proteasome in a Michael fashion. After cell lysis, a biotin moiety is introduced by Staudinger ligation to yield construct 2. This strategy allows activity profiling of the catalytic activities of the proteasome in vivo.
