10286-92-7Relevant articles and documents
KINETICS AND MECHANISM OF THE AMINOLYSIS OF BENZOIC ANHYDRIDES
Lee, Byung Choon,Yoon, Ji Hyun,Lee, Cheal Gyu,Lee, Ikchoon
, p. 273 - 279 (1994)
Nucleophilic substitution reactions of benzoic anhydrides, in which one of the rings is substituted, with anilines were investigated in methanol.The product-formation step coincides with the rate-limiting step so that the two rate constants, kXY and kXZ, for the competitive reaction pathways can be dissected.The two cross-interaction constants, ρXY and ρXZ, especially an unusually large magnitude of the latter, indicate that the reaction proceeds by a frontside SN2 attack on either one of the carbonyl carbon with a strong interaction between the nucleophile (X) and the leaving group (Z).The mechanism is also supposed by the trends in the activation parameters.
N-Phenylbenzamide derivatives as alternative oxidase inhibitors: Synthesis, molecular properties, 1H-STD NMR, and QSAR
Barsottini, Mario R. O.,Carazzolle, Marcelo F.,Costa, Paulo C. S.,Evangelista, Joel S.,Miranda, Paulo C. M. L.,Nascimento, Andrey F. Z.,Pereira, Gon?alo A. G.,Pires, Bárbara A.,Rocco, Silvana A.,Sfor?a, Maurício L.,Silva, Jaqueline S.,Vieira, Maria L. L.,Zeri, Ana C. M.
, (2020/02/27)
In the present work, 117 N-phenylbenzamides (NPDs) were prepared and evaluated against recombinant AOX from the fungal pathogen Moniliophthora perniciosa. 1H, 13C NMR, FTIR, and mass spectra provided structural information on NPDs. The library compounds were tested as Alternative Oxidase inhibitors in two different assays using the model yeast Pichia pastoris: cell growth and oxygen consumption assays. The most active compound, 3FH, was further characterized by DRX and 1H-NMR-STD. Single crystal X-ray diffraction showed intra- and intermolecular interactions of 3FH in solid-state and elucidated its 3D structural configuration. 1H-NMR-STD allowed us to derive protein-ligand interactions in a membrane-mimetic system and evidenced an outstanding interaction of 3FH with this enzyme. Results of both biological assays were used as input to Quantitative Structure-Activity Relationship models, which highlighted the more important molecular fragments contributions for protein-ligand interaction.
Synthesis and Biological Evaluation of 2,3,5-Substituted [1,2,4]Thiadiazoles as Allosteric Modulators of Adenosine Receptors
Van Den Nieuwendijk, Adrianus M. C. H.,Pietra, Daniele,Heitman, Laura,G?bly?s, Anikó,IJzerman, Adriaan P.
, p. 663 - 672 (2007/10/03)
A number of 2,3,5-substituted [1,2,4]thiadiazole analogues of SCH-202676 (N-(2,3-diphenyl-[1,2,4]thiadiazole-5(2H)-ylidene)methanamine, 7a) were synthesized and tested as potential allosteric modulators of adenosine receptors. All compounds were capable of displacing the binding of the radiolabeled agonist [3H]CCPA to human A1 adenosine receptors, whereas modest and varying effects were observed on the binding of [3H]DPCPX, a radiolabeled antagonist for this receptor subtype. Four compounds, 7a (SCH-202676), 7k (LUF5792), 71 (LUF5794), and 8e (LUF5789), were selected for more detailed characterization. They all proved allosteric inhibitors of agonist binding, with 7k being most potent, whereas their effects on antagonist binding were more ambiguous. Subsequently, experiments were done on human adenosine A2A and A3 receptors. Compounds 7a and 7l displayed peculiar displacement characteristics of both radiolabeled agonist and antagonist binding to A2A receptors, whereas 7a showed some activity on A3 receptors.
