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

Stephen P. Muench, Jozef Stec, Ying Zhou, Gustavo A. Afanador, Martin J. McPhillie, Mark R. Hickman, Patty J. Lee, Susan E. Leed, Jennifer M. Auschwitz, Sean T. Prigge, David W. Rice, Rima McLeod

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)3551-3555
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Volume23
Issue number12
DOIs
StatePublished - Jun 15 2013

Keywords

  • Enoyl reductase Triclosan Toxoplasma Plasmodium

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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  • Cite this

    Muench, S. P., Stec, J., Zhou, Y., Afanador, G. A., McPhillie, M. J., Hickman, M. R., Lee, P. J., Leed, S. E., Auschwitz, J. M., Prigge, S. T., Rice, D. W., & McLeod, R. (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), 3551-3555. https://doi.org/10.1016/j.bmcl.2013.04.035