22248-60-8Relevant articles and documents
Visible-Light-Driven, Copper-Catalyzed Decarboxylative C(sp3)?H Alkylation of Glycine and Peptides
Wang, Chao,Guo, Mengzhun,Qi, Rupeng,Shang, Qinyu,Liu, Qiang,Wang, Shan,Zhao, Long,Wang, Rui,Xu, Zhaoqing
, p. 15841 - 15846 (2018/11/23)
Despite a well-developed and growing body of work in Cu catalysis, the potential of Cu to serve as a photocatalyst remains underexplored. Reported herein is the first example of visible-light-induced Cu-catalyzed decarboxylative C(sp3)?H alkylation of glycine for preparing α-alkylated unnatural α-amino acids. It merits mentioning that the mild conditions and the good functional-group tolerance allow the modification of peptides using this method. The mechanistic studies revealed that a radical–radical coupling pathway is involved in the reaction.
Synthesis and biological evaluation of potential bisubstrate inhibitors of protein farnesyltransferase. Design and synthesis of functionalized imidazoles
De Figueiredo, Renata Marcia,Coudray, Laetitia,Dubois, Joelle
, p. 3299 - 3309 (2008/09/20)
A novel series of compounds, derived from 2,5-functionalized imidazoles, have been synthesized as potential bisubstrate inhibitors of protein farnesyltransferase (FTase) using structure-based design. These compounds have a 1,4-diacid chain and a tripeptid
Selectivity in the Trimethylsilylation and Acylation of Peptide Bonds, and its Application to Modification of the Enkephalins
Davies, John S.,Merritt, Raymond K.,Treadgold, Richard C.,Morley, John S.
, p. 2939 - 2948 (2007/10/02)
N.m.r. spectra of N-acylated peptides, formed by reaction of protected peptides with silylating agents followed by acylation, have provided a means for assessing selectivity in the acylation of amide bonds.Amino-acids such as valine and phenylalanine prev