Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 57, Issue 20, Pages 8664-8670Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm5011397
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Funding
- The Wellcome Trust [087792]
- BBSRC [BB/D02014X/1] Funding Source: UKRI
- EPSRC [EP/K039946/1] Funding Source: UKRI
- MRC [G0900278] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D02014X/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1098649, EP/K039946/1] Funding Source: researchfish
- Medical Research Council [G0900278] Funding Source: researchfish
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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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