在固体支持物上设计并合成向日葵胰蛋白酶抑制剂（SFTI-1）的氧化还原稳定类似物，即matriptase的强效抑制剂。
Design and synthesis of redox stable analogues of sunflower trypsin inhibitors (SFTI-1) on solid support, potent inhibitors of matriptase.
作者信息
Jiang Sheng, Li Peng, Lee Sheau-Ling, Lin Cheng Yong, Long Ya-Qiu, Johnson Michael D, Dickson Robert B, Roller Peter P
机构信息
Laboratory of Medicinal Chemistry, NCI, NIH, Frederick, Maryland 21702, USA.
出版信息
Org Lett. 2007 Jan 4;9(1):9-12. doi: 10.1021/ol0621497.
[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.
[结构：见正文] 胃蛋白酶原激活酶是新出现的II型跨膜丝氨酸蛋白酶家族的一员。研究发现，从向日葵种子中分离出的向日葵胰蛋白酶抑制剂（SFTI-1）对胃蛋白酶原激活酶具有抑制作用，其抑制常数（Ki）为0.92 nM，属于亚纳摩尔级别。基于这一结果，我们设计并合成了其蛋白水解稳定类似物SFTI-2和SFTI-3。SFTI-3对胃蛋白酶原激活酶表现出非常好的结合亲和力，并且其代谢稳定。
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