Abstract
Apicidin, a natural product recently isolated at Merck, inhibits both mammalian and protozoan histone deacetylases (HDACs). The conversion of apicidin, a nanomolar inhibitor of HDACs, into a series of side-chain analogues that display picomolar enzyme affinity is described within this structure-activity study.
MeSH terms
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Animals
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Antiprotozoal Agents / chemical synthesis*
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Antiprotozoal Agents / pharmacology
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Biological Factors / pharmacology
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Cattle
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Cell Line
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Combinatorial Chemistry Techniques
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Eimeria tenella / drug effects
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / pharmacology
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Fusarium / chemistry
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HeLa Cells
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Histone Deacetylase Inhibitors*
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Humans
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Microbial Sensitivity Tests
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Peptides, Cyclic / chemical synthesis
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Peptides, Cyclic / pharmacology*
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Plasmodium falciparum / drug effects
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Structure-Activity Relationship
Substances
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Antiprotozoal Agents
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Biological Factors
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Enzyme Inhibitors
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Histone Deacetylase Inhibitors
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Peptides, Cyclic
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apicidin