Abstract
Synthetic methods for the construction of a novel peptidomimetic structure are reported. The structure incorporates a beta-lactam and an azapeptide in a peptide backbone with the intention of generating rationally designed substrate-based protease inhibitors. The beta-lactam is formed by subjecting serine or threonine-azapeptides to Mitsunobu reaction conditions. Importantly, the azapeptidomimetic beta-lactam structure permits extended binding inhibition and the synthetic methods to create tetrapeptidomimetic structures are described.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Aza Compounds / chemical synthesis*
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Aza Compounds / chemistry
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Aza Compounds / pharmacology
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Binding Sites
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Binding, Competitive
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Catalysis
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Combinatorial Chemistry Techniques*
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Drug Design
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Models, Molecular
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Molecular Mimicry
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Molecular Structure
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Oligopeptides / chemical synthesis*
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Oligopeptides / chemistry
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Oligopeptides / pharmacology
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Serine Proteinase Inhibitors / chemical synthesis*
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Serine Proteinase Inhibitors / chemistry
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Serine Proteinase Inhibitors / pharmacology
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Structure-Activity Relationship
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Substrate Specificity
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beta-Lactams / chemical synthesis*
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beta-Lactams / chemistry
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beta-Lactams / pharmacology
Substances
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Aza Compounds
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Oligopeptides
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Serine Proteinase Inhibitors
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beta-Lactams