Abstract
The preparation of a Syringolin A/Glidobactin A hybrid (SylA-GlbA) consisting of a SylA macrocycle connected to the GlbA side chain and its potent proteasome targeting of all three proteasomal subsites is reported. The influence of the syrbactin macrocycle moiety on subsite selectivity is demonstrated.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites / drug effects
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Biological Products / chemistry*
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Models, Molecular
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Molecular Conformation
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Peptides, Cyclic / chemical synthesis
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / pharmacology*
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Protease Inhibitors / chemical synthesis
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Protease Inhibitors / chemistry
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Protease Inhibitors / pharmacology*
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Proteasome Inhibitors*
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Biological Products
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Peptides, Cyclic
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Protease Inhibitors
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Proteasome Inhibitors
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syringolin A
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glidobactin A