School of Pharmacy, Fudan University, Shanghai 201203, China.
Bioorg Med Chem. 2012 Aug 1;20(15):4774-80. doi: 10.1016/j.bmc.2012.05.077. Epub 2012 Jun 7.
The linear depsipeptide grassystatin A, a valuable probe for the study of cathepsin E function, has been synthesized by a [4+6] strategy. It exhibited specific inhibitory activity against cathepsin E with an IC(50) value of 0.8 nM. Our studies indicated that inhibition of cathepsin E did not have an impact on ovalbumin antigen processing and peptide presentation, unique from studies of other aspartic protease inhibitors.
线性二肽草抑素 A 是研究组织蛋白酶 E 功能的有价值的探针，已通过 [4+6] 策略合成。它对组织蛋白酶 E 表现出特异性抑制活性，IC 50 值为 0.8 nM。我们的研究表明，组织蛋白酶 E 的抑制作用不会影响卵清蛋白抗原加工和肽呈递，这与其他天冬氨酸蛋白酶抑制剂的研究不同。
