5467-09-4Relevant academic research and scientific papers
Synthesis of unsymmetrical diarylureas via Pd-catalyzed C-N cross-coupling reactions
Breitler, Simon,Oldenhuis, Nathan J.,Fors, Brett P.,Buchwald, Stephen L.
supporting information; experimental part, p. 3262 - 3265 (2011/08/07)
A facile synthesis of unsymmetrical N,N′-diarylureas is described. The utilization of the Pd-catalyzed arylation of ureas enables the synthesis of an array of diarylureas in good to excellent yields from benzylurea via a one-pot arylation-deprotection protocol, followed by a second arylation.
Synthesis of substituted [11C]ureas and [11C] sulphonylureas by Rh(I)-mediated carbonylation
Aberg, Ola,Langstroem
experimental part, p. 38 - 42 (2011/09/21)
The urea moiety is present in many biologically active compounds and thus an attractive target for 11C-labelling. To extend the scope of the rhodium(I)-mediated carbonylative cross-coupling reaction between an azide and an amine and investigate
Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid
Baures, Paul W.,Oza, Vibha B.,Peterson, Scott A.,Kelly, Jeffery W.
, p. 1339 - 1347 (2007/10/03)
A light scattering-based amyloid fibril formation assay was employed to evaluate potential inhibitors of transthyretin (TTR) amyloid fibril formation in vitro. Twenty nine aromatic small molecules, some with homology to flufenamic acid (a known non-steroidal anti-inflammatory drug) were tested to identify important structural features for inhibitor efficacy. The results of these experiments and earlier data suggest that likely inhibitors will have aromatic-based structures with at least two aromatic rings. The ring or fused ring system occupying the outermost TTR binding pocket needs to be substituted with an acidic functional group (e.g. a carboxylic acid) to interact with complimentary charges in the TTR binding site. The promising TTR amyloid fibril inhibitors ranked in order of efficacy are: 2>4~7>3>9>6>21 (see Structural summary of the best transthyretin amyloid fibril formation inhibitors identified in this study. The order of efficacy is: 2>4~7>3>9>6>21.). Copyright (C) 1999 Elsevier Science Ltd.
