885228-14-8Relevant articles and documents
Unimolecular artificial transmembrane channel with terminal dihydrogen phosphate groups showing transport selectivity for ammonium
Chen, Jian-Yu,Xiao, Qi,Behera, Harekrushna,Hou, Jun-Li
, (2019)
A new artificial transmembrane channel molecule bearing dihydrogen phosphate groups has been synthesized. The terminal dihydrogen phosphate groups enable the channel to be highly negatively charged at both ends of the channel structures. The artificial channel could incorporate into the lipid bilayer efficiently under low concentration. The channel displays high NH4+/K+ selectivity due to the electrostatic interaction and hydrogen bonding between NH4+ and the terminal dihydrogen phosphate groups.
Optimised synthesis of a nitroCBI hypoxia-activated prodrug with substantial anticancer activity
Lee, Ho H.,Dickson, Benjamin D.,Stevenson, Ralph J.,Yang, Shangjin,Tercel, Moana
, p. 3001 - 3007 (2019/05/01)
An optimised synthesis of a hypoxia-activated anticancer prodrug related to the duocarmycin family of natural products is described. The improved 10-step synthesis increases the overall yield from 4.4% to over 40% while requiring just 2 chromatography-bas
Virtual screening, selection and development of a benzindolone structural scaffold for inhibition of lumazine synthase
Talukdar, Arindam,Morgunova, Ekaterina,Duan, Jianxin,Meining, Winfried,Foloppe, Nicolas,Nilsson, Lennart,Bacher, Adelbert,Illarionov, Boris,Fischer, Markus,Ladenstein, Rudolf,Cushman, Mark
experimental part, p. 3518 - 3534 (2010/08/05)
Virtual screening of a library of commercially available compounds versus the structure of Mycobacterium tuberculosis lumazine synthase identified 2-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)acetic acid (9) as a possible lead compound. Compound 9 proved to be an effective inhibitor of M. tuberculosis lumazine synthase with a Ki of 70 μM. Lead optimization through replacement of the carboxymethylsulfonamide sidechain with sulfonamides substituted with alkyl phosphates led to a four-carbon phosphate 38 that displayed a moderate increase in enzyme inhibitory activity (Ki 38 μM). Molecular modeling based on known lumazine synthase/inhibitor crystal structures suggests that the main forces stabilizing the present benzindolone/enzyme complexes involve π-π stacking interactions with Trp27 and hydrogen bonding of the phosphates with Arg128, the backbone nitrogens of Gly85 and Gln86, and the side chain hydroxyl of Thr87.