835-11-0Relevant articles and documents
Selective Oxidation of Alkylarenes to the Aromatic Ketones or Benzaldehydes with Water
Du, Jihong,Duan, Baogen,Liu, Kun,Liu, Renhua,Yu, Feifei,Yuan, Yongkun,Zhang, Chenyang,Zhang, Jin
supporting information, (2022/02/09)
Here a palladium-catalyzed oxidation method for converting alkylarenes into the aromatic ketones or benzaldehydes with water as the only oxygen donor is reported. This C-H bond oxidation functionalization does not require other oxidants and hydrogen accep
Rhodium-Catalyzed Directing-Group-Assisted Aldehydic C–H Arylations with Aryl Halides
Rao, Maddali L. N.,Ramakrishna, Boddu S.
, p. 5080 - 5093 (2017/09/20)
A rhodium-catalyzed general protocol for the directing-group-assisted arylation of aromatic aldehydic C–H bonds was developed. This method involves either hydroxy- or amino-group-directed aldehyde C–H arylation with various aryl halides. A broad synthetic scope for the preparation of 2-hydroxybenzophenones was established with electronically variant salicylaldehydes and aryl halides with chemo- and regioselective possibilities. The developed protocol was also applied in the synthesis of medicinally important 3-salicyloylpyridines in high yields.
2,2′-Dihydroxybenzophenones and their carbonyl N-analogues as inhibitor scaffolds for MDR-involved human glutathione transferase isoenzyme A1-1
Perperopoulou, Fereniki D.,Tsoungas, Petros G.,Thireou, Trias N.,Rinotas, Vagelis E.,Douni, Eleni K.,Eliopoulos, Elias E.,Labrou, Nikolaos E.,Clonis, Yannis D.
, p. 3957 - 3970 (2014/08/18)
The MDR-involved human GSTA1-1, an important isoenzyme overexpressed in several tumors leading to chemotherapeutic-resistant tumour cells, has been targeted by 2,2′-dihydroxybenzophenones and some of their carbonyl N-analogues, as its potential inhibitors. A structure-based library of the latter was built-up by a nucleophilic cleavage of suitably substituted xanthones to 2,2′-dihydroxy-benzophenones (5-9) and subsequent formation of their N-derivatives (oximes 11-13 and N-acyl hydrazones 14-16). Screening against hGSTA1-1 led to benzophenones 6 and 8, and hydrazones 14 and 16, having the highest inhibition potency (IC50 values in the range 0.18 ± 0.02 to 1.77 ± 0.10 μM). Enzyme inhibition kinetics, molecular modeling and docking studies showed that they interact primarily at the CDNB-binding catalytic site of the enzyme. In addition, the results from cytotoxicity studies with human colon adenocarcinoma cells showed low LC 50 values for benzophenone 6 and its N-acyl hydrazone analogue 14 (31.4 ± 0.4 μM and 87 ± 1.9 μM, respectively), in addition to the strong enzyme inhibition profile (IC50(6 ) = 1,77 ± 0.10 μM; IC50(14 ) = 0.33 ± 0.05 μM). These structures may serve as leads for the design of new potent mono- and bi-functional inhibitors and pro-drugs against human GTSs.