Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.
basic_science · Level V
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- Record sourced from PubMed, PMID 24586798.
- Also identified by DOI 10.1371/journal.pone.0089465 and PMC identifier 3934894.
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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.
Medical subject headings
- Peptides, Cyclic
- Proteasome Endopeptidase Complex
- Trypsin Inhibitors
- Yeasts