ArticleBiomacromolecules2014
Cationic PAMAM dendrimers as pore-blocking binary toxin inhibitors.
Article in Biomacromolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Dendrimer-Based Drug Delivery Systems for Brain Targeting.Biomolecules · 2019Review
- Exploring the Nature of Cationic Blocker Recognition by the Anthrax Toxin Channel.Biophysical journal · 2019Article
- Inhibition of Pore-Forming Proteins.Toxins · 2019Review
- Analysis of the CDK4/6 Cell Cycle Pathway in Leiomyosarcomas as a Potential Target for Inhibition by Palbociclib.Sarcoma · 2019Article
- Brain Delivery of Multifunctional Dendrimer Protein Bioconjugates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018Article
- Impact of Dendrimer Terminal Group Chemistry on Blockage of the Anthrax Toxin Channel: A Single Molecule Study.Toxins · 2016Article
- Inhibiting bacterial toxins by channel blockage.Pathogens and disease · 2016Review
- Cationic Polyamidoamine Dendrimers as Modulators of EGFR Signaling In Vitro and In Vivo.PloS one · 2015Article
- Multivalent Inhibitors of Channel-Forming Bacterial Toxins.Current topics in microbiology and immunologyReview
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Dendrimers are unique highly branched macromolecules with numerous groundbreaking biomedical applications under development. Here we identified poly(amido amine) (PAMAM) dendrimers as novel blockers for the pore-forming B components of the binary anthrax toxin (PA63) and Clostridium botulinum C2 toxin (C2IIa). These pores are essential for delivery of the enzymatic A components of the internalized toxins from endosomes into the cytosol of target cells. We demonstrate that at low μM concentrations cationic PAMAM dendrimers block PA63 and C2IIa to inhibit channel-mediated transport of the A components, thereby protecting HeLa and Vero cells from intoxication. By channel reconstitution and high-resolution current recording, we show that the PAMAM dendrimers obstruct transmembrane PA63 and C2IIa pores in planar lipid bilayers at nM concentrations. These findings suggest a new potential role for the PAMAM dendrimers as effective polyvalent channel-blocking inhibitors, which can protect human target cells from intoxication with binary toxins from pathogenic bacteria.
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Registered trials
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.