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Design and synthesis of redox stable analogues of sunflower trypsin inhibitors (SFTI-1) on solid support, potent inhibitors of matriptase

  1. Author:
    Jiang, S.
    Li, P.
    Lee, S. L.
    Lin, C. Y.
    Long, Y. Q.
    Johnson, M. D.
    Dickson, R. B.
    Roller, P. P.

  2. Author Address

    NCI, Med Chem Lab, NIH, Frederick, MD 21702 USA. Georgetown Univ, Med Ctr, Lombardi Canc Ctr, Washington, DC 20057 USA.;Jiang, S, NCI, Med Chem Lab, NIH, Frederick, MD 21702 USA.;johnsom@georgetown.edu proll@helix.nih.gov
    1. Year: 2007
    2. Date: Jan
  2. Journal: Organic Letters
    1. 9
    2. 1
    3. Pages: 9-12
  4. Type of Article: Article
  5. ISSN: 1523-7060
  1. Abstract:

    Matriptase is a member of the emerging class of type II transmembrane serine proteases. It was found that the sunflower trypsin inhibitor (SFTI-1), isolated from sunflower seeds, inhibits matriptase with a subnanomolar K-i of 0.92 nM. On the basis of this result, we designed and synthesized its proteolytically stable analogues, SFTI-2 and SFTI-3. SFTI-3 exhibited very good binding affinity to matriptase, and it was metabolically stable.

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External Sources

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  2. DOI: 10.1021/ol0621497
  3. View record in Web of Science®
  4. WOS: 000243124900003

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