1036991-25-9Relevant articles and documents
Amide Effects in C?H Activation: Noncovalent Interactions with L-Shaped Ligand for meta Borylation of Aromatic Amides
Bisht, Ranjana,Hoque, Md Emdadul,Chattopadhyay, Buddhadeb
, p. 15762 - 15766 (2018/11/10)
A new concept for the meta-selective borylation of aromatic amides is described. It has been demonstrated that while esters gave para borylations, amides lead to meta borylations. For achieving high meta selectivity, an L-shaped bifunctional ligand has been employed and engages in an O???K noncovalent interaction with the oxygen atom of the moderately distorted amide carbonyl group. This interaction provides exceptional control for meta C?H activation/borylation.
para-Selective C?H Borylation of (Hetero)Arenes by Cooperative Iridium/Aluminum Catalysis
Yang, Lichen,Semba, Kazuhiko,Nakao, Yoshiaki
supporting information, p. 4853 - 4857 (2017/04/11)
para-Selective C?H borylation of benzamides and pyridines has been achieved by cooperative iridium/aluminum catalysis. A combination of iridium catalysts commonly employed for arene C?H borylation and bulky aluminum-based Lewis acid catalysts provides an unprecedented strategy for controlling the regioselectivity of C?H borylation to give variously substituted (hetero)arylboronates, which are versatile synthetic intermediates for complex multi-substituted aromatic compounds.
Kinase scaffold repurposing for neglected disease drug discovery: Discovery of an efficacious, lapatanib-derived lead compound for trypanosomiasis
Patel, Gautam,Karver, Caitlin E.,Behera, Ranjan,Guyett, Paul J.,Sullenberger, Catherine,Edwards, Peter,Roncal, Norma E.,Mensa-Wilmot, Kojo,Pollastri, Michael P.
supporting information, p. 3820 - 3832 (2013/06/27)
Human African trypanosomiasis (HAT) is a neglected tropical disease caused by the protozoan parasite Trypanosoma brucei. Because drugs in use against HAT are toxic and require intravenous dosing, new drugs are needed. Initiating lead discovery campaigns b
Design and synthesis of a second series of triazole-based compounds as potent dual mPGES-1 and 5-lipoxygenase inhibitors
Chini, Maria Giovanna,De Simone, Rosa,Bruno, Ines,Riccio, Raffaele,Dehm, Friederike,Weinigel, Christina,Barz, Dagmar,Werz, Oliver,Bifulco, Giuseppe
, p. 311 - 323 (2012/09/08)
Microsomal prostaglandin E2 synthase (mPGES)-1 and 5-lipoxygenase (5-LO) are pivotal enzymes in the biosynthesis of the pro-inflammatory PGE2 and leukotrienes, respectively. The design and synthesis of a second series of mPGES-1 inhibitors based on a triazole scaffold are described. Our studies allowed us to draw a tentative SAR profile and to optimize this series with the identification of compounds 10, 11 and 14-15 which displayed potent mPGES-1 inhibition in a cell-free assay. In addition, compounds 5, 10, 12 and 14-16 also blocked 5-LO activity in cell-free and cell-based test systems, emerging as very promising candidates for the development of safer and more effective anti-inflammatory drugs.
Identification of new γ-hydroxybutenolides that preferentially inhibit the activity of mPGES-1
De Simone, Rosa,Bruno, Ines,Riccio, Raffaele,Stadler, Katharina,Bauer, Julia,Schaible, Anja M.,Laufer, Stefan,Werz, Oliver
, p. 5012 - 5016 (2012/09/22)
Microsomal prostaglandin E2 synthase-1 (mPGES-1) has been recognized as novel, promising drug target for anti-inflammatory and anticancer drugs. mPGES-1 catalyzes the synthesis of the inducible prostaglandin E 2 in response to pro-inflammatory stimuli, rendering this enzyme extremely interesting in drug discovery process owing to the drastic reduction of the severe side effects typical for traditional non-steroidal anti-inflammatory drugs. In the course of our investigations focused on this topic, we identified two interesting molecules bearing the γ- hydroxybutenolide scaffold which potently inhibit the activity of mPGES-1. Notably, the lead compound 2c that inhibited mPGES-1 with IC50 = 0.9 μM, did not affect other related enzymes within the arachidonic acid cascade.
