Abstract
Proteasomes are responsible for the cytoplasmic turnover of the vast majority of proteins including regulatory proteins. We have synthesized lipopeptides a new class of non-covalent inhibitors of the 20S proteasome and assayed their inhibitory capacities. Their ability to inhibit at micromolar concentrations chymotrypsin-like and post-acid activities depends on peptide length (3 or 6 amino acids), sequence (presence of a positively or negatively charged amino acid), and alkyl chain length (C6-C18). These structural features could be varied to selectively inhibit one or more of the three proteasome activities.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Lipoproteins / chemical synthesis
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Lipoproteins / chemistry*
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Lipoproteins / pharmacology*
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Molecular Structure
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Peptide Hydrolases / metabolism
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Peptides / chemical synthesis
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Peptides / chemistry*
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Peptides / pharmacology*
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Proteasome Endopeptidase Complex / metabolism
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Proteasome Inhibitors*
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Structure-Activity Relationship
Substances
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Enzyme Inhibitors
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Lipoproteins
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Peptides
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Proteasome Inhibitors
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semen liquefaction factor
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Peptide Hydrolases
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Proteasome Endopeptidase Complex