6701-13-9Relevant articles and documents
METHOD FOR PRODUCING (METH)ACRYLATE COMPOUND CONTAINING HYDROXYL GROUP AND METHOD FOR PRODUCING (METH)ACRYLATE COMPOUND CONTAINING PHOSPHORIC ACID GROUP
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Paragraph 0054-0057, (2021/09/29)
PROBLEM TO BE SOLVED: To provide a method for producing a (meth)acrylate compound containing a hydroxyl group, which, when producing a (meth)acrylate compound containing a hydroxyl group, can suppress formation of by-products. SOLUTION: Provided is a method for producing a (meth)acrylate compound (A) which is a (meth)acrylate compound containing a hydroxyl group, comprising a step of reacting an alcohol compound containing a halogen atom and a (meth)acrylic acid salt to obtain the (meth)acrylate compound (A). SELECTED DRAWING: None COPYRIGHT: (C)2021,JPOandINPIT
Chemo- and Regioselective Hydrogenolysis of Diaryl Ether C-O Bonds by a Robust Heterogeneous Ni/C Catalyst: Applications to the Cleavage of Complex Lignin-Related Fragments
Gao, Fang,Webb, Jonathan D.,Hartwig, John F.
, p. 1474 - 1478 (2016/02/12)
We report the chemo- and regioselective hydrogenolysis of the C-O bonds in di-ortho-substituted diaryl ethers under the catalysis of a supported nickel catalyst. The catalyst comprises heterogeneous nickel particles supported on activated carbon and furnishes arenes and phenols in high yields without hydrogenation. The high thermal stability of the embedded metal particles allows C-O bond cleavage to occur in highly substituted diaryl ether units akin to those in lignin. Preliminary mechanistic experiments show that this catalyst undergoes sintering less readily than previously reported catalyst particles that form from a solution of [Ni(cod)2].
Catechol-based substrates of chalcone synthase as a scaffold for novel inhibitors of PqsD
Allegretta, Giuseppe,Weidel, Elisabeth,Empting, Martin,Hartmann, Rolf W.
, p. 351 - 359 (2015/02/19)
A new strategy for treating Pseudomonas aeruginosa infections could be disrupting the Pseudomonas Quinolone Signal (PQS) quorum sensing (QS) system. The goal is to impair communication among the cells and, hence, reduce the expression of virulence factors and the formation of biofilms. PqsD is an essential enzyme for the synthesis of PQS and shares some features with chalcone synthase (CHS2), an enzyme expressed in Medicago sativa. Both proteins are quite similar concerning the size of the active site, the catalytic residues and the electrostatic surface potential at the entrance of the substrate tunnel. Hence, we evaluated selected substrates of the vegetable enzyme as potential inhibitors of the bacterial protein. This similarity-guided approach led to the identification of a new class of PqsD inhibitors having a catechol structure as an essential feature for activity, a saturated linker with two or more carbons and an ester moiety bearing bulky substituents. The developed compounds showed PqsD inhibition with IC50 values in the single-digit micromolar range. The binding mode of these compounds was investigated by Surface Plasmon Resonance (SPR) experiments revealing that their interaction with the protein is not influenced by the presence of the anthranilic acid bound to active site cysteine. Importantly, some compounds reduced the signal molecule production in cellulo.