223438-52-6Relevant articles and documents
Structure-based design of a new series of d-glutamic acid based inhibitors of bacterial UDP-N-acetylmuramoyl-l-alanine: D-glutamate ligase (MurD)
Toma?i?, Tihomir,Zidar, Nace,?ink, Roman,Kova?, Andreja,Blanot, Didier,Contreras-Martel, Carlos,Dessen, Andréa,Müller-Premru, Manica,Zega, Anamarija,Gobec, Stanislav,Kikelj, Danijel,Peterlin Ma?i?, Lucija
supporting information; experimental part, p. 4600 - 4610 (2011/09/14)
MurD ligase is one of the key enzymes participating in the intracellular steps of peptidoglycan biosynthesis and constitutes a viable target in the search for novel antibacterial drugs to combat bacterial drug-resistance. We have designed, synthesized, and evaluated a new series of d-glutamic acid-based Escherichia coli MurD inhibitors incorporating the 5-benzylidenethiazolidin-4- one scaffold. The crystal structure of 16 in the MurD active site has provided a good starting point for the design of structurally optimized inhibitors 73-75 endowed with improved MurD inhibitory potency (IC50 between 3 and 7 μM). Inhibitors 74 and 75 showed weak activity against Gram-positive Staphylococcus aureus and Enterococcus faecalis. Compounds 73-75, with IC 50 values in the low micromolar range, represent the most potent d-Glu-based MurD inhibitors reported to date.
The design and synthesis of a novel, orally active, selective ETA antagonist
Rawson, David J.,Dack, Kevin N.,Dickinson, Roger P.,James, Kim,Long, Clive,Walker, Don
, p. 149 - 157 (2007/10/03)
The potency and pharmacokinetic properties of an indole-based series of endothelin antagonists have been optimised using in vitro, in silico and in vivo methods. Compound 8 is oxidised in vivo to the active metabolite 7 and has been highlighted as an oral
