118091-50-2Relevant academic research and scientific papers
Synthesis, crystal structures and xanthine oxidase inhibitory activities of two copper(II) complexes with Schiff bases
Cui, Yan-Qin,You, Zhong-Lu,Li, Xiao-Fang,Wang, Xiao-Ling,Ma, Yu-Ping,Wang, Che,Zhang, Cheng-Lu
, p. 159 - 163 (2010)
Two azido-coordinated Schiff base Cu(II) complexes with the formulae [Cu(L1)(N3)]-MeOH and [Cu(L2)(μ1,1-N 3)]n, where L1 is the deprotonated form of 2-chloro-2-[(2- ethylaminoethylimino)methyl]phenol, and L2 is
Bimetallic zirconium amine bis(phenolate) polymerization catalysts: Enhanced activity and tacticity control for polyolefin synthesis
Radlauer, Madalyn R.,Agapie, Theodor
supporting information, p. 3247 - 3250 (2014/08/05)
Binucleating multidentate amine bis(phenolate) ligands with rigid terphenyl backbones were designed to support two zirconium centers locked in close proximity. Polymerizations of propylene or 1-hexene with the synthesized bimetallic precatalysts resulted in polymers with significantly higher isotacticity (up to 79% mmmm) in comparison to the stereoirregular polymers produced with previously reported Cs-symmetric monometallic analogues. The bimetallic precatalysts also display higher activity (up to 124 kg of poly(1-hexene) (mmol of Zr)-1 h-1), in comparison to the monometallic analogues, and among the highest activities reported for nonmetallocene catalysts. The stereocontrol is consistent with a bimetallic mechanism involving remote steric interactions with the ligand sphere of the second metal center.
Synthesis, molecular docking and biological evaluation of Schiff base transition metal complexes as potential urease inhibitors
Chen, Wu,Li, Yuguang,Cui, Yongming,Zhang, Xian,Zhu, Hai-Liang,Zeng, Qingfu
body text, p. 4473 - 4478 (2010/10/19)
Six transition metal compounds of Schiff base ligands were evaluated for the inhibitory activity on jack bean urease, of which compounds 2-6 were determined by single crystal X-ray analysis. It was found that copper(II) complexes 1 and 4 showed strong inhibitory activity against jack bean urease (IC50 = 0.52 and 0.46 μM), compared with acetohydroxamic acid (IC50 = 42.12 μM) as a positive reference. Cobalt(II), nickel(II) and zinc(II) compounds also exhibited potent inhibitory activity (IC 50 = 3.88-25.20 μM). A docking analysis using the AUTODOCK 4.0 program could explain the inhibitory activities of 1 and 4 against urease.
