Muench, S.P., Stec, J., Zhou, Y. et al. (9 more authors) (2013) Development of a triclosan scaffold which allows for adaptations on both the A- and B-ring for transport peptides. Bioorganic and Medicinal Chemistry Letters, 23 (12). pp. 3551-3555. ISSN 0960-894X
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2013 Elsevier. This is an author produced version of a paper subsequently published in Bioorganic and Medicinal Chemistry Letters. Uploaded in accordance with the publisher's self-archiving policy. Article available under the terms of the CC-BY-NC-ND licence (https://creativecommons.org/licenses/by-nc-nd/4.0/) |
Keywords: | Enoyl reductase; Triclosan; Toxoplasma; Plasmodium |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 20 Feb 2017 12:30 |
Last Modified: | 02 Apr 2018 06:31 |
Published Version: | https://doi.org/10.1016/j.bmcl.2013.04.035 |
Status: | Published |
Publisher: | Elsevier |
Refereed: | Yes |
Identification Number: | 10.1016/j.bmcl.2013.04.035 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:110836 |