ArticleInternational journal of biological macromolecules2010
Inhibition of Escherichia coli ATP synthase by amphibian antimicrobial peptides.
Article in International journal of biological macromolecules, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 58 citations in OpenAlex.
- Going Beyond Host Defence Peptides: Horizons of Chemically Engineered Peptides for Multidrug-Resistant Bacteria.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023Review
- Gene drive mosquitoes can aid malaria elimination by retardingScience advances · 2022Article
- Antibiofilm activity of host defence peptides: complexity provides opportunities.Nature reviews. Microbiology · 2021Review
- Potential Inhibitory Effect ofAntibiotics (Basel, Switzerland) · 2020Article
- Automatic construction of molecular similarity networks for visual graph mining in chemical space of bioactive peptides: an unsupervised learning approach.Scientific reports · 2020Article
- Spotlight on the Selected New Antimicrobial Innate Immune Peptides Discovered During 2015-2019.Current topics in medicinal chemistry · 2020Review
- Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.Archives of biochemistry and biophysics · 2019Article
- Dermaseptins, Multifunctional Antimicrobial Peptides: A Review of Their Pharmacology, Effectivity, Mechanism of Action, and Possible Future Directions.Frontiers in pharmacology · 2019Review
- Snake Venom Cathelicidins as Natural Antimicrobial Peptides.Frontiers in pharmacology · 2019Review
- A Therapeutic Connection between Dietary Phytochemicals and ATP Synthase.Current medicinal chemistry · 2017Review
- Improving Phylogeny Reconstruction at the Strain Level Using Peptidome Datasets.PLoS computational biology · 2016Article
- 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
- ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.Current medicinal chemistry · 2013Review
- Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthase.International journal of biological macromolecules · 2012Article
- Trimeric form of intracellular ATP synthase subunit β of Aggregatibacter actinomycetemcomitans binds human interleukin-1β.PloS one · 2011Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Previously melittin, the alpha-helical basic honey bee venom peptide, was shown to inhibit F(1)-ATPase by binding at the beta-subunit DELSEED motif of F(1)F(o)-ATP synthase. Herein, we present the inhibitory effects of the basic alpha-helical amphibian antimicrobial peptides, ascaphin-8, aurein 2.2, aurein 2.3, carein 1.8, carein 1.9, citropin 1.1, dermaseptin, maculatin 1.1, maganin II, MRP, or XT-7, on purified F(1) and membrane bound F(1)F(0)Escherichia coli ATP synthase. We found that the extent of inhibition by amphibian peptides is variable. Whereas MRP-amide inhibited ATPase essentially completely (approximately 96% inhibition), carein 1.8 did not inhibit at all (0% inhibition). Inhibition by other peptides was partial with a range of approximately 13-70%. MRP-amide was also the most potent inhibitor on molar scale (IC(50) approximately 3.25 microM). Presence of an amide group at the c-terminal of peptides was found to be critical in exerting potent inhibition of ATP synthase ( approximately 20-40% additional inhibition). Inhibition was fully reversible and found to be identical in both F(1)F(0) membrane preparations as well as in isolated purified F(1). Interestingly, growth of E. coli was abrogated in the presence of ascaphin-8, aurein 2.2, aurein 2.3, citropin 1.1, dermaseptin, magainin II-amide, MRP, MRP-amide, melittin, or melittin-amide but was unaffected in the presence of carein 1.8, carein 1.9, maculatin 1.1, magainin II, or XT-7. Hence inhibition of F(1)-ATPase and E. coli cell growth by amphibian antimicrobial peptides suggests that their antimicrobial/anticancer properties are in part linked to their actions on ATP synthase.
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