Synthesis, molecular docking and kinetic properties of β-hydroxy-β-phenylpropionyl-hydroxamic acids as Helicobacter pylori urease inhibitors

Xiao, Zhu‐Ping; Peng, Zhiyuan; Dong, Jing-Jun; Deng, Rui-Cheng; Wang, Xudong; Ouyang, Hongwei; Yang, Po Chih; He, Juan; Wang, Yuanfeng; Zhu, Man; Peng, Xiaochun; Peng, Wanxi; Zhu, Hai‐Liang

doi:10.1016/j.ejmech.2013.07.047

Cited by 81 publications

(24 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…From these plots, and under the conditions employed, the Km value for xanthine was calculated to be 6.7 µmol L -1 . The plots also showed that the inhibition mechanism of pyrogallol and purpurogallin were of the same mixed type, this indicated that the molecular interactions between the XO-inhibitors and XO itself may occur in the active site of XO, including the region around the molybdopterin cofactor (the catalytic site of XO)[27].Recently, developed molecular docking software emerged as a useful tool for theoretical drug design. Computer-based simulations of small molecule (ligand)-protein interactions, including interactions occurring between enzymes and their inhibitors provide insight into the stability of such complex and also provide direct simulated images of the interaction sites by enabling visualizations of simulation results.…”

mentioning

confidence: 90%

Conversion to purpurogallin, a key step in the mechanism of the potent xanthine oxidase inhibitory activity of pyrogallol

Honda

Fukuyama

Nishiwaki

et al. 2017

Free Radical Biology and Medicine

View full text Add to dashboard Cite

In this study, the mechanism of the xanthine oxidase (XO) inhibitory activity of pyrogallol, the main inhibitor found in roasted coffee, was investigated. Pyrogallol was unstable and readily converted to purpurogallin in a pH 7.4 solution, a physiological model of human body fluids. The XO inhibitory activity of the produced purpurogallin was higher than that of pyrogallol, as evidenced by comparing their IC values (0.2µmolL for purpurogallin, 1.6µmolL for pyrogallol). The XO activity of pyrogallol was enhanced by pre-incubation in pH 7.4 solution. Although the initial XO inhibitory activity of 4-methylpyrogallol was weak (IC 33.3µmolL), its XO inhibitory activity was also enhanced by pre-incubation in the pH 7.4 solution. In contrast, 5-methylpyrogallol, which could not be transformed into corresponding purpurogallin derivatives, did not show XO inhibitory activity before or after incubation in pH 7.4 solution. Molecular docking simulations clarified that purpurogallins have stronger affinities for XO than corresponding pyrogallols. These results revealed that the potent XO inhibitory activity seemingly observed in pyrogallol is actually derived from its chemical conversion, under alkaline conditions, into purpurogallin.

show abstract

mentioning

confidence: 90%

Conversion to purpurogallin, a key step in the mechanism of the potent xanthine oxidase inhibitory activity of pyrogallol

Honda

Fukuyama

Nishiwaki

et al. 2017

Free Radical Biology and Medicine

View full text Add to dashboard Cite

show abstract

“…It contributes in urinary tract and gastrointestinal infections, probably augmenting the severity of several pathological conditions like peptic ulcers and stomach cancer as in the case of H. pylori. Ureases are also involved in the development of different human and animal pathogenicity of urolithiasis, pyelonephritis, hepatic encephalopathy, hepatic coma, and urinary catheter encrustation [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Urease Inhibitory Activity of Aerial Parts of Artemisia scoparia: Exploration in an In Vitro Study

Khan

Tariq

et al. 2014

Ulcers

View full text Add to dashboard Cite

Artimisia scoparia has been used in the treatment of different disorders including ulcers. The current study was therefore designed to investigate the aerial parts of Artemisia scoparia (crude extract, total sterol and flavonoidal contents, and aqueous fraction) for its urease inhibitory potential. The crude of the plant evoked marked attenuation on urease activity, when tested in various concentrations with IC50 values of 4.06 mg/ml. The inhibitory potential was further augmented in the aqueous fraction (IC50: 2.30 mg/ml) of the plant. When the total sterol and flavonoidal contents were challenged against urease, both showed concentration dependent activity; the latter showed maximum potency with IC50 values of 8.04 and 2.10 mg/ml, respectively. In short, the aerial parts of the plant demonstrated marked antagonism on urease and thus our study validated the traditional use of Artemisia scoparia in the treatment of ulcer.

show abstract

“…Lineweaver–Burk plots of 1/absorbance versus 1/ l -DOPA and 1/absorbance versus 1/Urea were used to determine the type of enzyme inhibition. A series of experiments were performed to determine the inhibition kinetics by following method 18 , 28 , 29 . Different inhibitor concentrations of compound 8b with 0, 15, 30, 61, 123 and 247 μM, 8j with 0, 14, 28 and 55.8 μM, respectively were used in case of mushroom tyrosinase inhibition.…”

Section: Kinetic Studymentioning

confidence: 99%

“…Urease (EC 3.5.1.5) is a nickel containing enzyme that catalyzes the hydrolysis of urea to ammonia and carbon dioxide or carbamate by at least 10 14 over the spontaneous reaction 18 . It is of our interest to focus on the discovery of novel urease inhibitors as it is already known that these compounds play a crucial part in the therapies both human and plants disorders.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of chiral pyrazolo[4,3-e][1,2,4]triazine sulfonamides with tyrosinase and urease inhibitory activity

Tarasiuk

Kotwica-Mojzych

Rafiq

et al. 2016

Journal of Enzyme Inhibition and Medicinal Chemistry

View full text Add to dashboard Cite

A new series of sulfonamide derivatives of pyrazolo[4,3-e][1,2,4]triazine with chiral amino group has been synthesized and characterized. The compounds were tested for their tyrosinase and urease inhibitory activity. Evaluation of prepared derivatives demonstrated that compounds (8b) and (8j) are most potent mushroom tyrosinase inhibitors whereas all of the obtained compounds showed higher urease inhibitory activity than the standard thiourea. The compounds (8a), (8f) and (8i) exhibited excellent enzyme inhibitory activity with IC50 0.037, 0.044 and 0.042 μM, respectively, while IC50 of thiourea is 20.9 μM.

show abstract

Synthesis, molecular docking and kinetic properties of β-hydroxy-β-phenylpropionyl-hydroxamic acids as Helicobacter pylori urease inhibitors

Cited by 81 publications

References 32 publications

Conversion to purpurogallin, a key step in the mechanism of the potent xanthine oxidase inhibitory activity of pyrogallol

Conversion to purpurogallin, a key step in the mechanism of the potent xanthine oxidase inhibitory activity of pyrogallol

Urease Inhibitory Activity of Aerial Parts of Artemisia scoparia: Exploration in an In Vitro Study

Synthesis of chiral pyrazolo[4,3-e][1,2,4]triazine sulfonamides with tyrosinase and urease inhibitory activity

Contact Info

Product

Resources

About