Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1

PLoS One. 2014 Feb 25;9(2):e89465. doi: 10.1371/journal.pone.0089465. eCollection 2014.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caspases / metabolism
  • Chymotrypsin / metabolism
  • Humans
  • Peptides / metabolism
  • Peptides, Cyclic / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Trypsin / metabolism
  • Trypsin Inhibitors / metabolism*
  • Yeasts / metabolism*

Substances

  • Peptides
  • Peptides, Cyclic
  • SFTI-1 peptide, sunflower
  • Trypsin Inhibitors
  • Chymotrypsin
  • Trypsin
  • Caspases
  • 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.