ArticleBioorganic & medicinal chemistry letters2013
Development of a triclosan scaffold which allows for adaptations on both the A- and B-ring for transport peptides.
Article in Bioorganic & medicinal chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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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Who cites it
4 citing papers in PubMed, 14 citations in OpenAlex.
- Triclosan inhibits the growth of Neospora caninum in vitro and in vivo.Parasitology research · 2019Article
- Drugs in development for toxoplasmosis: advances, challenges, and current status.Drug design, development and therapy · 2017Review
- A Multilayer Network Approach for Guiding Drug Repositioning in Neglected Diseases.PLoS neglected tropical diseases · 2016Article
- The benzimidazole based drugs show good activity against T. gondii but poor activity against its proposed enoyl reductase enzyme target.Bioorganic & medicinal chemistry letters · 2014Article
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
Abstract
The enoyl acyl-carrier protein reductase (ENR) enzyme is harbored within the apicoplast of apicomplexan parasites providing a significant challenge for drug delivery, which may be overcome through the addition of transductive peptides, which facilitates crossing the apicoplast membranes. The binding site of triclosan, a potent ENR inhibitor, is occluded from the solvent making the attachment of these linkers challenging. Herein, we have produced 3 new triclosan analogs with bulky A- and B-ring motifs, which protrude into the solvent allowing for the future attachment of molecular transporters for delivery.
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Registered trials
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