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

Jiang S, Li P, Lee SL, Lin CY, Long YQ, Johnson MD, Dickson RB, Roller PP

Laboratory of Medicinal Chemistry, NCI, NIH, Frederick, Maryland 21702, USA.

[structure: see text] 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 Ki 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.

Published 28 December 2006 in Org Lett, 9(1): 9-12.
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