scholarly journals Synthesis, Crystal Structures and Urease Inhibition of 4-Bromo-N’-(1-(pyridin-2-yl)ethylidene)benzohydrazide and Its Dinuclear Copper(II) Complex

2021 ◽  
Vol 68 (4) ◽  
pp. 804-810
Author(s):  
Hui Zhao ◽  
Xiu-Rui Liu ◽  
Xue Wang ◽  
Jing Hu ◽  
Ya-Jun Cai ◽  
...  

A new dinuclear copper(II) complex [Cu2(μ-Br)2L2] · 0.5 MeOH with the benzohydrazone ligand 4-bromo-N’-(1-(pyridin-2-yl)ethylidene)benzohydrazide (HL) has been synthesized and characterized by elemental analysis, IR and UV-Vis spectroscopic studies. Single crystal structures of the complex and the benzohydrazone compound were studied. The Cu atoms in the complex are coordinated by two benzohydrazone ligands and two Br bridging groups, forming square pyramidal coordination. The complex has good inhibitory activity on Jack bean urease, with IC50 value of 1.38 μmol L-1.

1975 ◽  
Vol 5 (3) ◽  
pp. 221-225 ◽  
Author(s):  
S. Cervelli ◽  
P. Nannipieri ◽  
G. Giovannini ◽  
A. Perna

2012 ◽  
Vol 6 (1) ◽  
Author(s):  
Nana Du ◽  
Mingming Chen ◽  
Zhaodi Liu ◽  
Liangquan Sheng ◽  
Huajie Xu ◽  
...  

Drug Research ◽  
2017 ◽  
Vol 67 (10) ◽  
pp. 596-605 ◽  
Author(s):  
Aamer Saeed ◽  
Sajid ur-Rehman ◽  
Pervaiz Channar ◽  
Fayaz Larik ◽  
Qamar Abbas ◽  
...  

AbstractA series of acylthioureas was synthesized and their inhibitory effects on the DPPH and jack bean urease were evaluated. The results showed that all of the synthesized compounds exhibited significant jack bean urease inhibitory activities. Especially, 1-(4-chlorophenyl)-3 palmitoylthiourea 5a bearing 4-chloro substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with an IC50 value 0.0170 μM compared to the IC50 value of 4.720 μM of thiourea used as standard. The inhibition mechanism analyzed by Lineweaver–Burk plots revealed that the type of inhibition of compound 5a on tyrosinase was noncompetitive. The docking study against jack bean urease enzyme was also performed to determine the binding affinity of the compounds. The compounds 4c and 4e showed the highest binding affinity with the active binding site of tyrosinase. The initial structure activity relationships (SARs) analysis suggested that further development of such compounds might be of interest. The statistics of our results endorses that all compounds and particularly 5a may serve as a structural template for the design and development of novel urease inhibitors Graphical Abstract.


PLoS ONE ◽  
2021 ◽  
Vol 16 (10) ◽  
pp. e0258568
Author(s):  
Muhammad Ajmal Rana ◽  
Rashid Mahmood ◽  
Sajid Ali

Urea is the most popular and widely used nitrogenous fertilizer. High soil urease activity rapidly hydrolyses applied urea to ammonia which contributes to soil nitrogen (N) losses and reduces N use efficiency of crop plants. The ammonia losses can be minimized by the inhibition of soil urease activity which has been explored using various potential chemical inhibitors. However, the soil urease activity inhibition potential of plant extracts is rarely explored to date. In the present study, extracts of 35 plant materials were taken and evaluated against jack bean urease. Eleven extracts, showing >50% jack bean urease inhibition, were selected and further investigated in 13 soils collected from various districts of Punjab, Pakistan. Interestingly, except Capsicum annum, Melia azedarach, Citrus reticulata and Quercus infectoria, the plant extracts showed urease inhibition activities in soils, the extent of which was lower as compared to that observed in jack bean urease though. Maximum urea hydrolysis inhibition (70%) was noted with Vachellia nilotica which was 40% more than that of hydroquinone (50%) followed by that of Eucalyptus camaldulensis (24%). The extracts of V. nilotica and E. camaldulensis were coated on urea and applied to soil in the next step. At 21st day, 239% and 116% more urea-N was recovered from soil treated with V. nilotica and E. camaldulensis extracts coated urea, respectively, as compared to uncoated urea. Conclusively, these results indicated that the coating of V. nilotica and E. camaldulensis extracts on urea prills prolonged urea persistence in soil owing to minimum urea hydrolysis, probably, the extracts of V. nilotica and E. camaldulensis showed their urease inhibition potential. The results of this study provide a base line for the identification of new soil urease inhibitor compounds from plant materials in future.


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