Synthesis and evaluation of the sunflower derived trypsin inhibitor as a potent inhibitor of the type II transmembrane serine protease, matriptase

Bioorg Med Chem Lett. 2001 Sep 17;11(18):2515-9. doi: 10.1016/s0960-894x(01)00493-0.

Abstract

We report here the synthesis of a 14-amino acid long bicyclic peptide, previously isolated from sunflower seeds. This peptide, termed sunflower trypsin inhibitor (SFTI-1), is one of the most potent naturally occurring small-molecule trypsin inhibitors. In addition to inhibiting trypsin, the synthetic SFTI-1 is also a very potent inhibitor, with a K(i) of 0.92nM, of the recently identified epithelial serine protease, termed 'matriptase'.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biochemistry / methods
  • Helianthus / chemistry
  • Models, Molecular
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology*
  • Protein Conformation
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / drug effects*
  • Serine Proteinase Inhibitors / chemistry*
  • Serine Proteinase Inhibitors / pharmacology*
  • Trypsin / chemistry
  • Trypsin / drug effects*
  • Trypsin / pharmacology

Substances

  • Peptides, Cyclic
  • SFTI-1 peptide, sunflower
  • Serine Proteinase Inhibitors
  • Serine Endopeptidases
  • matriptase
  • Trypsin