ArticleInternational journal of biological macromolecules2016
Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase.
Article in International journal of biological macromolecules, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025Review
- Gold nanorods as biocompatible nano-agents for the enhanced photothermal therapy in skin disorders.Journal of biomedical research · 2024Article
- Inhibitors of ATP Synthase as New Antibacterial Candidates.Antibiotics (Basel, Switzerland) · 2023Review
- Past, Present, and Future of Naturally Occurring Antimicrobials Related to Snake Venoms.Animals : an open access journal from MDPI · 2023Review
- Review
- Potential Inhibitory Effect ofAntibiotics (Basel, Switzerland) · 2020Article
- Review
- Antimicrobial Activity of Protein Fraction fromMolecules (Basel, Switzerland) · 2020Article
- Snake Venom Cathelicidins as Natural Antimicrobial Peptides.Frontiers in pharmacology · 2019Review
- LyeTxI-b, a Synthetic Peptide Derived FromFrontiers in microbiology · 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
- Systemic Responses of Multidrug-ResistantFrontiers in cellular and infection microbiology · 2017Article
- Improving Phylogeny Reconstruction at the Strain Level Using Peptidome Datasets.PLoS computational biology · 2016Article
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Authors and funding
6 authors.
Funding
Abstract
Venom peptides are known to have strong antimicrobial activity and anticancer properties. King cobra cathelicidin or OH-CATH (KF-34), banded krait cathelicidin (BF-30), wolf spider lycotoxin I (IL-25), and wolf spider lycotoxin II (KE-27) venom peptides were found to strongly inhibit Escherichia coli membrane bound F1Fo ATP synthase. The potent inhibition of wild-type E. coli in comparison to the partial inhibition of null E. coli by KF-34, BF-30, Il-25, or KE-27 clearly links the bactericidal properties of these venom peptides to the binding and inhibition of ATP synthase along with the possibility of other inhibitory targets. The four venom peptides KF-34, BF-30, IL-25, and KE-27, caused ≥85% inhibition of wild-type membrane bound E.coli ATP synthase. Venom peptide induced inhibition of ATP synthase and the strong abrogation of wild-type E. coli cell growth in the presence of venom peptides demonstrates that ATP synthase is a potent membrane bound molecular target for venom peptides. Furthermore, the process of inhibition was found to be fully reversible.
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