Abstract
The design, chemical synthesis, and enzymatic activity evaluation of a set of falcipain-2 inhibitors are reported. These compounds contain a proven peptidomimetic recognition motif based on a benzo[1,4]diazepin-2-one (1,4-BDZ) framework built on a dipeptide sequence, and a Michael acceptor terminal moiety capable of deactivating the cysteine protease active site. Our goal is to modify the P(3) site of this motif in order to identify the structural requirements for the interaction with the target.
Copyright © 2011 Elsevier Masson SAS. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Benzodiazepinones / chemical synthesis
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Benzodiazepinones / chemistry
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Benzodiazepinones / pharmacology*
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Cysteine Endopeptidases / metabolism*
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Cysteine Proteinase Inhibitors / chemical synthesis
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Cysteine Proteinase Inhibitors / chemistry
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Cysteine Proteinase Inhibitors / pharmacology*
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Drug Design
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Enzyme Activation / drug effects
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Humans
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Models, Molecular
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Molecular Structure
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Peptidomimetics*
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Stereoisomerism
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Structure-Activity Relationship
Substances
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Benzodiazepinones
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Cysteine Proteinase Inhibitors
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Peptidomimetics
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benzo(1,4)diazepin-2-one
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Cysteine Endopeptidases
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falcipain 2