Abstract
Based on the analysis of the crystal structure of MG101 (1) and 20S proteasomes, a new series of peptide aldehyde derivatives were designed and synthesized. Their ability to inhibit 20S proteasome was assayed. Among them, Cbz-Glu(OtBu)-Phe-Leucinal (3c), Cbz-Glu(OtBu)-Leu-Leucinal (3d), and Boc-Ser(OBzl)-Leu-Leucinal (3o) exhibited the most activity, which represented an order of magnitude enhancement compared with MG132 (2). The covalent docking protocol was used to explore the binding mode. The structure-activity relationship of the peptide aldehyde inhibitors is discussed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehydes / chemical synthesis*
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Aldehydes / chemistry
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Amino Acid Motifs
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Binding Sites
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Computer Simulation
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Enzyme Assays
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Models, Molecular
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Oligopeptides / chemical synthesis*
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Oligopeptides / chemistry
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / chemistry
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Proteasome Endopeptidase Complex / chemistry
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Proteasome Inhibitors*
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Protein Binding
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Structure-Activity Relationship
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Surface Properties
Substances
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Aldehydes
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Oligopeptides
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Protease Inhibitors
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Proteasome Inhibitors
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Proteasome Endopeptidase Complex