496-72-0Relevant articles and documents
Differential antiproliferative activity of new benzimidazole-4,7-diones
Garuti, Laura,Roberti, Marinella,Pizzirani, Daniela,Pession, Annalisa,Leoncini, Emanuela,Cenci, Valentina,Hrelia, Silvana
, p. 663 - 668 (2004)
Ten benzimidazole-4,7-diones were synthesized and tested in vitro on two tumor cell lines. Several compounds showed a significant antiproliferative activity on K562 cells, although to a different extent, whereas compound 1i showed a highly significant activity on SW620 cells, comparable to that of doxorubicin. Both the substituents in the quinone ring and the position of the nitrogen atom in the pyridine moiety play a crucial role for the biological activity.
Pd-Pt/modified GO as an efficient and selective heterogeneous catalyst for the reduction of nitroaromatic compounds to amino aromatic compounds by the hydrogen source
Salahshournia, Hossein,Ghiaci, Mehran
, (2019/02/14)
In this work, different nitroaromatic compounds were successfully reduced to their corresponding aromatic amines with excellent conversion and selectivity in methanol at 50?°C by using Pd-Pt nanoparticles immobilized on the modified grapheme oxide (m-GO) and hydrogen as the reducing source. The catalytic efficiency of Pd and Pd-Pt loading on the modified GO was investigated for the reduction of various nitroaromatic compounds, and the Pd-Pt/m-GO system demonstrated the highest conversion and selectivity. The catalyst was characterized by different techniques including FT-IR, Raman, UV–Vis, XRD, BET, XPS, FESEM, EDS, and TEM. The metal nanoparticles with the size of less than 10?nm were uniformly distributed on the m-GO. The catalyst could be reused at least five times without losing activity, showing the stability of the catalyst structure. Finally, the efficiency of the prepared catalyst was compared with Pd-Pt/AC, and Pd-Pt/GO catalysts.
Novel cathepsin K inhibitors block osteoclasts in vitro and increase spinal bone density in zebrafish
Xue, Si-Tu,Wang, Ya-Li,Han, Xiao-Wan,Yi, Hong,Jiang, Wei,Si, Shu-Yi,Guo, Hui-Fang,Li, Zhuo-Rong
, p. 8600 - 8607 (2019/03/21)
Cathepsin K (Cat K) is a predominant cysteine protease and highly potent collagenase expressed in osteoclasts. Cat K inhibitors are anti-resorptive agents to treat osteoporosis. A novel scaffold of cathepsin K inhibitors, exemplified by lead compound 1x, was used as the template for designing and synthesizing a total of 61 derivatives that have not been reported before. An exploratory structure-activity relationship analysis identified the potent Cat K inhibitor A22, which displayed an IC50 value of 0.44 μM against Cat K. A22 was very specific for Cat K and caused a significantly higher in vitro inhibition of the enzyme as compared to that of lead compound 1x. A surface plasmon resonance analysis confirmed in vitro binding of A22 to Cat K. Molecular docking studies indicated several favourable interaction sites for A22 within the active pocket of Cat K. Furthermore, A22 also blocked active osteoclasts in vitro and increased spinal bone density in zebrafish, in which it showed an activity that was higher than that of the marketed therapeutic bone metabolizer etidronate disodium. A22 represents a very promising lead compound for the development of novel antiresorptive agents functioning as orthosteric inhibitors of Cat K.