肽基α-酮-β-醛作为组织蛋白酶L新抑制剂的开发——与组织蛋白酶B的效力和选择性概况比较
Development of peptidyl alpha-keto-beta-aldehydes as new inhibitors of cathepsin L--comparisons of potency and selectivity profiles with cathepsin B.
作者信息
Lynas J F, Hawthorne S J, Walker B
机构信息
Division of Biomedicinal Chemistry, School of Pharmacy, Queen's University Belfast, Medical Biology Centre, Northern Ireland, UK.
出版信息
Bioorg Med Chem Lett. 2000 Aug 7;10(15):1771-3. doi: 10.1016/s0960-894x(00)00340-1.
We have utilized previously known substrate and inhibitor specificity profiles for the lysosomal cysteine protease, cathepsin L, to design a new series of putative inhibitors of this enzyme, based on di- and tri-peptidyl alpha-keto-beta-aldehydes. Kinetic evaluation of these compounds revealed Z-Phe-Tyr(OBut)-COCHO, with a Ki 0.6 nM, to be the most potent, synthetic reversible inhibitor of cathepsin L reported to date.
我们利用先前已知的溶酶体半胱氨酸蛋白酶组织蛋白酶L的底物和抑制剂特异性谱，基于二肽基和三肽基α-酮-β-醛设计了一系列该酶的新型推定抑制剂。对这些化合物的动力学评估表明，Ki为0.6 nM的Z-Phe-Tyr(OBut)-COCHO是迄今为止报道的组织蛋白酶L最有效的合成可逆抑制剂。
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