52751-63-0Relevant academic research and scientific papers
Chemoselective metal-free aerobic alcohol oxidation in lignin
Rahimi, Alireza,Azarpira, Ali,Kim, Hoon,Ralph, John,Stahl, Shannon S.
supporting information, p. 6415 - 6418 (2013/06/05)
An efficient organocatalytic method for chemoselective aerobic oxidation of secondary benzylic alcohols within lignin model compounds has been identified. Extension to selective oxidation in natural lignins has also been demonstrated. The optimal catalyst system consists of 4-acetamido-TEMPO (5 mol %; TEMPO = 2,2,6,6-tetramethylpiperidine-N-oxyl) in combination with HNO3 and HCl (10 mol % each). Preliminary studies highlight the prospect of combining this method with a subsequent oxidation step to achieve C-C bond cleavage.
Regioselectivity of enzymatic and photochemical single electron transfer promoted carbon-carbon bond fragmentation reactions of tetrameric lignin model compounds
Cho, Dae Won,Latham, John A.,Park, Hea Jung,Yoon, Ung Chan,Langan, Paul,Dunaway-Mariano, Debra,Mariano, Patrick S.
scheme or table, p. 2840 - 2852 (2011/05/28)
New types of tetrameric lignin model compounds, which contain the common β-O-4 and β-1 structural subunits found in natural lignins, have been prepared and carbon-carbon bond fragmentation reactions of their cation radicals, formed by photochemical (9,10-dicyanoanthracene) and enzymatic (lignin peroxidase) SET-promoted methods, have been explored. The results show that cation radical intermediates generated from the tetrameric model compounds undergo highly regioselective C-C bond cleavage in their β-1 subunits. The outcomes of these processes suggest that, independent of positive charge and odd-electron distributions, cation radicals of lignins formed by SET to excited states of sensitizers or heme-iron centers in enzymes degrade selectively through bond cleavage reactions in β-1 vs β-O-4 moieties. In addition, the findings made in the enzymatic studies demonstrate that the sterically large tetrameric lignin model compounds undergo lignin peroxidase-catalyzed cleavage via a mechanism involving preliminary formation of an enzyme-substrate complex.
NEW DRUG FOR INHIBITING AGGREGATION OF PROTEINS INVOLVED IN DISEASES LINKED TO PROTEIN AGGREGATION AND/OR NEURODEGENERATIVE DISEASES
-
Page/Page column 43-44, (2010/04/03)
The present invention relates to a compound represented by formula (E). The present invention also relates to a compound represented by the formula (E) for use in the treatment or prevention of diseases linked to protein aggregation and/or neurodegenerative diseases. Moreover, the present invention relates to pharmaceutical and diagnostic compositions comprising the compound of the invention as well as to a kit. Furthermore, the present invention relates to a method of imaging deposits of aggregated protein. A kit for preparing a detectably labelled compound of the present invention is also disclosed.
Synthesis of dibenzoylmethane derivatives and inhibition of mutagenicity in Salmonella typhimurium
Choshi,horimoto,Wang,Nagase,Ichikawa,Sugino,Hibino
, p. 1047 - 1049 (2007/10/02)
Twenty dibenzoylmethanes with methyl, methoxy, bromo, chloro, or fluoro substitution on either one or both benzene rings were synthesized and assayed for inhibition of the mutagenicity of 2-nitrofluorene in S. typhimurium TA98. 2,2-Dimethoxy, 3,3-dimethoxy and 3,3,4,4-tetramethoxydibenzoylmethane was as active as dibenzoylmethane. None of the halogen-substituted dibenzoylmethanes were active. These results demonstrate that dibenzoylmethanes can inhibit the mutagenicity of 2-nitrofluorene, and that modifications made on the benzene rings of dibenzoylmethane cannot enhance the antimutagenicity of this parent compound.
