Fluorimetric urease inhibition assay on a multilayer microfluidic chip with immunoaffinity immobilized enzyme reactors

Zhang, Qin; Tang, Xiaoyong; Hou, Fenghua; Yang, Jianping; Xie, Zefeng; Cheng, Zhen

doi:10.1016/j.ab.2013.06.003

Cited by 8 publications

(8 citation statements)

References 33 publications

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“…There are many proposed technological application of ureases [195] , [196] , [197] , [198] , [199] , [200] all of which explore exclusively the enzyme’s catalytic activity. There are though certainly much more to be explored with these proteins, starting with the biotechnological use of ureases (and of urease-derived peptides) as transgenes to protect crops against insect herbivory and disease-causing fungi, or as ecofriendly insecticides to control insect borne diseases.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Ureases: Historical aspects, catalytic, and non-catalytic properties – A review

Kappaun

Piovesan

Carlini

et al. 2018

Journal of Advanced Research

176

145

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Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Ureases: Historical aspects, catalytic, and non-catalytic properties – A review

Kappaun

Piovesan

Carlini

et al. 2018

Journal of Advanced Research

176

145

View full text Add to dashboard Cite

show abstract

“…To construct the HTS assay, we compared three reported protocols for determination of the activity of JBU by using salicylic acid-hypochlorite and Nessler detection reagent, as well as phenol red(20,26,27), which undergo the indophenol and Nessler’s reaction with NH 3 , respectively. Salicylic acid-hypochlorite and Nessler’s reagents could dose-dependently and time-dependently monitor the activity of JBU at various concentrations (Figures S1A and B); however, the phenol red failed to detect it (Figure S1C).…”

Section: Resultsmentioning

confidence: 99%

“…The current assay to determine the activity of urease mainly relies on colorimetric reactions to determine the concentration of NH 3 using indophenol or Nessler's reaction [20]. Recently, a microfluidic chip-based fluorometric assay has been developed to monitor the activity of urease [21,22]. In addition, a cell-based assay for H. pylori urease has been reported lately, and validated by known inhibitors of urease, but it has not been employed to screen new inhibitors for urease yet [23].…”

Section: Introductionmentioning

confidence: 99%

High-throughput tandem-microwell assay for ammonia repositions FDA-Approved drugs to Helicobacter pylori infection

Liu

Zhang

et al. 2021

Preprint

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To date, little attempt has been made to develop new treatments for Helicobacter pylori (H. pylori), although the community is aware of the shortage of treatments for H. pylori. In this study, we developed a 192-tandem-microwell-based high-throughput-assay for ammonia that is a known virulence factor of H. pylori and a product of urease. We could identify few drugs, i.e. panobinostat, dacinostat, ebselen, captan and disulfiram, to potently inhibit the activity of ureases from bacterial or plant species. These inhibitors suppress the activity of urease via substrate-competitive or covalent-allosteric mechanism, but all except captan prevent the antibiotic-resistant H. pylori strain from infecting human gastric cells, with a more pronounced effect than acetohydroxamic acid, a well-known urease inhibitor and clinically used drug for the treatment of bacterial infection. This study offers several bases for the development of new treatments for urease-containing pathogens and to study the mechanism responsible for the regulation of urease activity.

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“…The current assay to determine the activity of urease mainly relies on colorimetric reactions to determine the concentration of NH 3 using indophenol or Nessler's reaction 21 . Recently, a microfluidic chip‐based fluorometric assay has been developed to monitor the activity of urease 22,23 . In addition, a cell‐based assay for H .…”

Section: Introductionmentioning

confidence: 99%

High‐throughput tandem‐microwell assay for ammonia repositions FDA‐Approved drugs to inhibit Helicobacter pylori urease

Liu

Zhang

et al. 2021

The FASEB Journal

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To date, little attempt has been made to develop new treatments for Helicobacter pylori (H. pylori), although the community is aware of the shortage of treatments for H. pylori. In this study, we developed a 192-tandem-microwell-based highthroughput assay for ammonia that is a known virulence factor of H. pylori and a product of urease. We could identify few drugs, that is, panobinostat, dacinostat, ebselen, captan, and disulfiram, to potently inhibit the activity of ureases from bacterial or plant species. These inhibitors suppress the activity of urease via substrate-competitive or covalent-allosteric mechanism, but all except captan prevent the antibiotic-resistant H. pylori strain from killing human gastric cells, with a more pronounced effect than acetohydroxamic acid, a well-known urease inhibitor and clinically used drug for the treatment of bacterial infection.This study offers several bases for the development of new treatments for ureasecontaining pathogens and to study the mechanism responsible for the regulation of urease activity.

show abstract

Fluorimetric urease inhibition assay on a multilayer microfluidic chip with immunoaffinity immobilized enzyme reactors

Cited by 8 publications

References 33 publications

Ureases: Historical aspects, catalytic, and non-catalytic properties – A review

Ureases: Historical aspects, catalytic, and non-catalytic properties – A review

High-throughput tandem-microwell assay for ammonia repositions FDA-Approved drugs to Helicobacter pylori infection

High‐throughput tandem‐microwell assay for ammonia repositions FDA‐Approved drugs to inhibit Helicobacter pylori urease

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