ArticleInternational journal of biological macromolecules2012
Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthase.
Article in International journal of biological macromolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- Applying nanoemulsions produced from the essential oil mixture of citronella and Coleus Amboinicus to preserve minced chicken meat.PloS one · 2026Article
- Insights into the potential dual-antibacterial mechanism of Kelisha capsule on Escherichia coli.BMC complementary medicine and therapies · 2024Article
- Inhibitors of ATP Synthase as New Antibacterial Candidates.Antibiotics (Basel, Switzerland) · 2023Review
- Evaluation of double expression system for co-expression and co-immobilization of flavonoid glucosylation cascade.Applied microbiology and biotechnology · 2022Article
- Beneficial effect of polyphenols in COVID-19 and the ectopic FJournal of cellular biochemistry · 2022Article
- Inhibition ofSaudi journal of biological sciences · 2022Article
- Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2019Article
- Reversible optical control of FFEBS letters · 2018Article
- A Therapeutic Connection between Dietary Phytochemicals and ATP Synthase.Current medicinal chemistry · 2017Review
- Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase.International journal of biological macromolecules · 2017Article
- Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 2017Article
- Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase.International journal of biological macromolecules · 2016Article
- Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2016Article
- Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase.International journal of biological macromolecules · 2015Article
- Article
- Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Biochemistry · 2014Article
- ATP synthase: the right size base model for nanomotors in nanomedicine.TheScientificWorldJournal · 2014Review
- Resveratrol induced inhibition of Escherichia coli proceeds via membrane oxidation and independent of diffusible reactive oxygen species generation.Redox biology · 2014Article
- ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.Current medicinal chemistry · 2013Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
In this paper we present the inhibitory effect of a variety of structurally modulated/modified polyphenolic compounds on purified F(1) or membrane bound F(1)F(o)Escherichia coli ATP synthase. Structural modulation of polyphenols with two phenolic rings inhibited ATP synthase essentially completely; one or three ringed polyphenols individually or fused together inhibited partially. We found that the position of hydroxyl and nitro groups plays critical role in the degree of binding and inhibition of ATPase activity. The extended positioning of hydroxyl groups on imino diphenolic compounds diminished the inhibition and abridged position enhanced the inhibition potency. This was contrary to the effect by simple single ringed phenolic compounds where extended positioning of hydroxyl group was found to be effective for inhibition. Also, introduction of nitro group augmented the inhibition on molar scale in comparison to the inhibition by resveratrol but addition of phosphate group did not. Similarly, aromatic diol or triol with rigid or planar ring structure and no free rotation poorly inhibited the ATPase activity. The inhibition was identical in both F(1)F(o) membrane preparations as well as in isolated purified F(1) and was reversible in all cases. Growth assays suggested that modulated compounds used in this study inhibited F(1)-ATPase as well as ATP synthesis nearly equally.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.