90819-30-0Relevant articles and documents
Elucidating the Structural Requirement of Uridylpeptide Antibiotics for Antibacterial Activity
Terasawa, Yuma,Sataka, Chisato,Sato, Toyotaka,Yamamoto, Kazuki,Fukushima, Yukari,Nakajima, Chie,Suzuki, Yasuhiko,Katsuyama, Akira,Matsumaru, Takanori,Yakushiji, Fumika,Yokota, Shin-Ichi,Ichikawa, Satoshi
, p. 9803 - 9827 (2020)
The synthesis and biological evaluation of analogues of uridylpeptide antibiotics were described, and the molecular interaction between the 3′-hydroxy analogue of mureidomycin A (3′-hydroxymureidomycin A) and its target enzyme, phospho-MurNAc-pentapeptide
Aminodiol HIV protease inhibitors. Synthesis and structure - Activity relationships of P1/P1′ compounds: Correlation between lipophilicity and cytotoxicity
Chen, Ping,Cheng, Peter T. W.,Alam, Masud,Beyer, Barbara D.,Bisacchi, Gregory S.,Dejneka, Tamara,Evans, Adelaide J.,Greytok, Jill A.,Hermsmeier, Mark A.,Humphreys, W. Griffith,Jacobs, Glenn A.,Kocy, Octavian,Lin, Pin-Fang,Lis, Karen A.,Marella, Michael A.,Ryono, Denis E.,Sheaffer, Amy K.,Spergel, Steven H.,Sun, Chong-Qing,Tino, Joseph A.,Vite, Gregory,Colonno, Richard J.,Zahler, Robert,Barrish, Joel C.
, p. 1991 - 2007 (2007/10/03)
A series of novel aminodiol inhibitors of HIV protease based on the lead compound 1 with structural modifications at P1′ were synthesized in order to reduce the cytotoxicity of 1. We have observed a high degree of correlation between the lipophilicity and the cytotoxicity of this series of inhibitors. It was found that appropriate substitution at the para position of the P1′ phenyl group of 1 resulted in the identification of equipotent (both against the enzyme and in cell culture) compounds (101, 10m, 10n, and 15c) which possess significantly decreased cytotoxicity.