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Bioorg Med Chem Lett. 2013 Jun 15;23(12):3551-5. doi: 10.1016/j.bmcl.2013.04.035. Epub 2013 Apr 24.

Development of a triclosan scaffold which allows for adaptations on both the A- and B-ring for transport peptides.

Author information

1
School of Biomedical Sciences, University of Leeds, Leeds, UK. s.p.muench@leeds.ac.uk

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.

PMID:
23664871
PMCID:
PMC3683578
DOI:
10.1016/j.bmcl.2013.04.035
[Indexed for MEDLINE]
Free PMC Article
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