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Structure-based design of potent and selective leishmania N-myristoyltransferase inhibitors

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JournalJOURNAL OF MEDICINAL CHEMISTRY
DatePublished - 19 Sep 2014
Issue number20
Volume57
Number of pages7
Pages (from-to)8664-8670
Original languageEnglish

Abstract

Inhibitors of Leishmania N-myristoyltransferase (NMT), a potential target for the treatment of leishmaniasis, obtained from a high-throughput screen, were resynthesized to validate activity. Crystal structures bound to Leishmania major NMT were obtained, and the active diastereoisomer of one of the inhibitors was identified. On the basis of structural insights, enzyme inhibition was increased 40-fold through hybridization of two distinct binding modes, resulting in novel, highly potent Leishmania donovani NMT inhibitors with good selectivity over the human enzyme.

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