Abstract
The structure-based design, chemical synthesis and in vitro activity evaluation of various falcipain inhibitors derived from 2-pyridone are reported. These compounds contain a peptidomimetic binding determinant and a Michael acceptor terminal moiety capable of deactivating the cysteine protease active site.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antimalarials / pharmacology
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Chemistry, Pharmaceutical / methods*
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Cysteine Endopeptidases / chemistry*
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Cysteine Proteinase Inhibitors / chemical synthesis*
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Cysteine Proteinase Inhibitors / pharmacology*
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Drug Design
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Humans
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Inhibitory Concentration 50
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Malaria / drug therapy
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Models, Chemical
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Molecular Conformation
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Plasmodium falciparum / metabolism
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Pyridones / chemistry*
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Structure-Activity Relationship
Substances
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Antimalarials
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Cysteine Proteinase Inhibitors
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Pyridones
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Cysteine Endopeptidases
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falcipain 2
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falcipain 3