Curcumin inhibits FtsZ assembly: an attractive mechanism for its antibacterial activity

Rai, Dipti; Singh, Jitendra; Roy, Nilanjan; Panda, Dulal

doi:10.1042/bj20070891

Cited by 446 publications

(331 citation statements)

References 41 publications

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“…In agreement with our study, Rai et al, suggested that curcumin might be considered as an important antibacterial drug target. In this study, curcumin has been shown to have a potent antibacterial activity against a number of pathogenic bacteria including Staphylococcus aureus, Staphylococcus epidermidis and Enterococcus (32). Also, Wang et al used microcapsule curcumin against Staphylococcus aureus, Escherichia coli, Yersinia enterocolitica, Bacillus subtilis and Bacillus cereus.…”

Section: Discussionmentioning

confidence: 99%

Curcumin-loaded Chitosan Tripolyphosphate Nanoparticles as a safe,natural and effective antibiotic inhibits the infection of Staphylococcusaureus and Pseudomonas aeruginosa in vivo

Jahromi¹,

Al-Musawi²,

Pirestani³

et al. 2014

Iran J Biotech

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Section: Discussionmentioning

confidence: 99%

Curcumin-loaded Chitosan Tripolyphosphate Nanoparticles as a safe,natural and effective antibiotic inhibits the infection of Staphylococcusaureus and Pseudomonas aeruginosa in vivo

Jahromi¹,

Al-Musawi²,

Pirestani³

et al. 2014

Iran J Biotech

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“…16 This may be due to a direct increase in the GTP hydrolysis reaction, induced by the change in FtsZ secondary structure on curcumin binding. Alternatively, the increase in GTP turnover may be due to a steric hindrance on polymer bundling (which is not explicitly represented in our model).…”

Section: Bacillus Subtilis Cell Cultures Its Mode Of Action Is Via Dmentioning

confidence: 99%

Biological Insights from a Simulation Model of the Critical FtsZ Accumulation Required for Prokaryotic Cell Division

Dow

Berg²,

Roper

et al. 2015

Biochemistry

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Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work of researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-forprofit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. Publisher's statement:This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/acs.biochem.5b00261The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription. FtsZ in vitro as well as on in vivo parameters, is used to integrate critical processes in cell division. According to the model, the cell's ability to divide depends on a "contraction parameter" (χ) that links the force of contraction to the dynamics of FtsZ. This parameter accurately predicts the outcome of division. Evaluating the GTP binding strength, the FtsZ polymerization rate, and the intrinsic GTP hydrolysis/dissociation activity, we find that inhibition of GTP-FtsZ binding is an inefficient anti-bacterial target. Furthermore, simulations indicate that the temperature sensitivity of the ftsZ84 mutation arises from the 2 conversion of FtsZ to a dual-specificity NTPase. Finally, the sensitivity to temperature of the rate of ATP hydrolysis, over the critical temperature range, leads us to conclude that the ftsZ84 mutation affects the turnover rate of the Z-ring much less strongly than previously reported.

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“…The results of GTPase assay indicated that the interaction of curcumin with FtsZ enhanced the GTPase activity but destabilized the FtsZ polymers [81]. Using computational docking, Roy and co-workers identified the possible binding sites of curcumin in E. coli FtsZ and B. subtilis FtsZ.…”

Section: Curcuminmentioning

confidence: 99%

Small molecules targeting at the bacterial cell division protein FtsZ as potential antimicrobial agents

Sun¹,

Wong²

2018

Fighting Antimicrobial Resistance

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Curcumin inhibits FtsZ assembly: an attractive mechanism for its antibacterial activity

Cited by 446 publications

References 41 publications

Curcumin-loaded Chitosan Tripolyphosphate Nanoparticles as a safe,natural and effective antibiotic inhibits the infection of Staphylococcusaureus and Pseudomonas aeruginosa in vivo

Curcumin-loaded Chitosan Tripolyphosphate Nanoparticles as a safe,natural and effective antibiotic inhibits the infection of Staphylococcusaureus and Pseudomonas aeruginosa in vivo

Biological Insights from a Simulation Model of the Critical FtsZ Accumulation Required for Prokaryotic Cell Division

Small molecules targeting at the bacterial cell division protein FtsZ as potential antimicrobial agents

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