862120-56-7Relevant academic research and scientific papers
Site-Selective δ-C(sp3)?H Alkylation of Amino Acids and Peptides with Maleimides via a Six-Membered Palladacycle
Zhan, Bei-Bei,Li, Ya,Xu, Jing-Wen,Nie, Xing-Liang,Fan, Jun,Jin, Liang,Shi, Bing-Feng
supporting information, p. 5858 - 5862 (2018/04/17)
The site-selective functionalization of unactivated C(sp3)?H bonds remains one of the greatest challenges in organic synthesis. Herein, we report on the site-selective δ-C(sp3)?H alkylation of amino acids and peptides with maleimides
Synthesis of novel potent hepatitis C virus NS3 protease inhibitors: Discovery of 4-hydroxy-cyclopent-2-ene-1,2-dicarboxylic acid as a N-acyl-l-hydroxyproline bioisostere
Thorstensson, Fredrik,Wangsell, Fredrik,Kvarnstroem, Ingemar,Vrang, Lotta,Hamelink, Elizabeth,Jansson, Katarina,Hallberg, Anders,Rosenquist, Asa,Samuelsson, Bertil
, p. 827 - 838 (2007/10/03)
Potent tetrapeptidic inhibitors of the HCV NS3 protease have been developed incorporating 4-hydroxy-cyclopent-2-ene-1,2-dicarboxylic acid as a new N-acyl-l-hydroxyproline mimic. The hydroxycyclopentene template was synthesized in eight steps from commercially available (syn)-tetrahydrophthalic anhydride. Three different amino acids were explored in the P1-position and in the P2-position the hydroxyl group of the cyclopentene template was substituted with 7-methoxy-2-phenyl-quinolin-4-ol. The P3/P4-positions were then optimized from a set of six amino acid derivatives. All inhibitors were evaluated in an in vitro assay using the full-length NS3 protease. Several potent inhibitors were identified, the most promising exhibiting a Ki value of 1.1 nM.
