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

  1. Author:
    Long, Y. Q.
    Lee, S. L.
    Lin, C. Y.
    Enyedy, I. J.
    Wang, S. M.
    Li, P.
    Dickson, R. B.
    Roller, P. P.

  2. Author Address

    NCI, Med Chem Lab, FCRDC, 376-208, POB B, Frederick, MD 21702 USA. NCI, Med Chem Lab, FCRDC, Frederick, MD 21702 USA. Georgetown Univ, Med Ctr, Lombardi Canc Ctr, Washington, DC 20007 USA. Roller PP NCI, Med Chem Lab, FCRDC, 376-208, POB B, Frederick, MD 21702 USA.
    1. Year: 2001
  2. Journal: Bioorganic & Medicinal Chemistry Letters
    1. 11
    2. 18
    3. Pages: 2515-2519
  4. Type of Article: Article
  1. 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 0.92 nM, of the recently identified epithelial serine protease, termed 'matriptase'. Published by Elsevier Science Ltd.

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