Abstract
Starting from the primary structure of sunflower trypsin inhibitor SFTI-1, we designed novel non-covalent inhibitors of human and yeast 20S proteasomes. Peptides with Arg residue in P1 position and two basic amino acid residues (Lys or/and Arg) in P2' and P3' positions strongly inhibited chymotrypsin-like and caspase-like activities, while trypsin-like activity was poorly modified. We found that some SFTI-1 analogues up-regulated exclusively the chymotrypsin-like activity of latent yeast 20S proteasome.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Caspases / metabolism
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Chymotrypsin / metabolism
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Humans
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Peptides / metabolism
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Peptides, Cyclic / metabolism*
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Proteasome Endopeptidase Complex / metabolism*
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Trypsin / metabolism
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Trypsin Inhibitors / metabolism*
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Yeasts / metabolism*
Substances
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Peptides
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Peptides, Cyclic
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SFTI-1 peptide, sunflower
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Trypsin Inhibitors
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Chymotrypsin
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Trypsin
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Caspases
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Proteasome Endopeptidase Complex
Grants and funding
This work was supported by Polish National Science Center (grant No. UMO-2011/01/D/ST5/02778). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.