Urease Inhibitors of Agricultural Interest Inspired by Structures of Plant Phenolic Aldehydes

Horta, Lívia P.; Mota, Yane C. C.; Barbosa, Gisele Maria; Braga, Taniris Cafiero; Marriel, I. E.; Fátima, Ângelo de; Modolo, Luzia V.

doi:10.21577/0103-5053.20160208

Cited by 23 publications

(32 citation statements)

References 33 publications

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“…Urease is a metalloenzyme capable of hydrolyzing urea initially into carbondioxide and carbamate which ultimately collapses into ammonia gas . By releasing ammonia in excess amount it paves the way for the Helicobacter pylori to survive in stomach.…”

Section: Introductionmentioning

confidence: 99%

Hybrid Pharmacophoric Approach in the Design and Synthesis of Coumarin Linked Pyrazolinyl as Urease Inhibitors, Kinetic Mechanism and Molecular Docking

Saeed

Mahesar

Channar

et al. 2017

Chemistry & Biodiversity

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The current research article reports the synthesis of coumarinyl pyrazolinyl thioamide derivatives and their biological activity as inhibitors of jack bean urease. The coumarinyl pyrazolinyl thioamides were synthesized by reacting thiosemicarbazide with newly synthesized chalcones to afford the products in good yields and the synthesized compounds were purified by recrystallization. Coumarinyl pyrazolinyl thioamide derivatives 5a - 5q showed significant activity against Urease enzyme and also exhibited good antioxidant potential. The compound 3-(2-oxo-2H-chromen-3-yl)-5-phenyl-4,5-dihydro-1H-pyrazole-1-carbothioamide (5n) was found to be superior agent in the series with an IC = 0.358 ± 0.017 μm compared to standard thiourea with an IC = 4720 ± 174 μm. To undermine the binding mode of inhibition kinetic studies were performed for most potent derivative and it was found that compound 5n inhibits urease enzyme by non-competitive mode of inhibition. Molecular docking studies were carried out to delineate the binding affinity of the synthesized derivatives.

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Section: Introductionmentioning

confidence: 99%

Hybrid Pharmacophoric Approach in the Design and Synthesis of Coumarin Linked Pyrazolinyl as Urease Inhibitors, Kinetic Mechanism and Molecular Docking

Saeed

Mahesar

Channar

et al. 2017

Chemistry & Biodiversity

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“…Urease (EC 3.5.1.5; urea amidohydrolase) is a metal containing enzyme possess dual harmful effects on human health and fertile soil [1][2][3]. Urease enzymes are found in nature, ranging from miniatures to highly complex organism such as invertebrates and plants.…”

Section: Introductionmentioning

confidence: 99%

Jack Bean Urease Inhibitors, and Antioxidant Activity Based on Palmitic acid Derived 1-acyl-3- Arylthioureas: Synthesis, Kinetic Mechanism and Molecular Docking Studies

et al. 2017

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A 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 bearing 4-chloro substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with an IC value 0.0170 μM compared to the IC 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 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 may serve as a structural template for the design and development of novel urease inhibitors Graphical Abstract.

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“…Also, the lines in the double reciprocal plot intersect one another in the second quadrant ( Figure 3c). Other natural products such as protocatechuic aldehyde, syringaldehyde and vanillin were shown to be mixed inhibitors towards urease 22 . Competitive inhibitors compete with the substrate for the enzyme active site and are related to the formation of EI (enzyme-inhibitor) complexes whose equilibrium dissociation constant (or inhibitor constant) is defined as K i .…”

Section: Effect Of Lichen Secondary Metabolites On Urease Activitymentioning

confidence: 99%

In vitroinhibition ofHelicobacter pyloriand interaction studies of lichen natural products with jack bean urease

et al. 2018

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Urease Inhibitors of Agricultural Interest Inspired by Structures of Plant Phenolic Aldehydes

Cited by 23 publications

References 33 publications

Hybrid Pharmacophoric Approach in the Design and Synthesis of Coumarin Linked Pyrazolinyl as Urease Inhibitors, Kinetic Mechanism and Molecular Docking

Hybrid Pharmacophoric Approach in the Design and Synthesis of Coumarin Linked Pyrazolinyl as Urease Inhibitors, Kinetic Mechanism and Molecular Docking

Jack Bean Urease Inhibitors, and Antioxidant Activity Based on Palmitic acid Derived 1-acyl-3- Arylthioureas: Synthesis, Kinetic Mechanism and Molecular Docking Studies

In vitroinhibition ofHelicobacter pyloriand interaction studies of lichen natural products with jack bean urease

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