INSERM U761, Biostructures and Drug Discovery, France; Faculté de Pharmacie, Univ Lille Nord de France, 3 rue du Pr Laguesse, Lille F-59006, France; Institut Pasteur de Lille, IFR 142, Lille F-59021, France; PRIM, Lille F-59006, France.
Eur J Med Chem. 2013 Nov;69:244-61. doi: 10.1016/j.ejmech.2013.08.027. Epub 2013 Aug 30.
Osteoarthritis is a disabling disease characterized by the articular cartilage breakdown. Aggrecanases are potential therapeutic targets for the treatment of this pathology. At the starting point of this project, an acylthiosemicarbazide was discovered to inhibit aggrecanase-2. The acylthiosemicarbazide Zn binding group is also a convenient linker for library synthesis. A focused library of 920 analogs was thus prepared and screened to establish structure-activity relationships. The modification of the acylthiosemicarbazide was also explored. This strategy combining library design and discrete compounds synthesis yielded inhibitor 35, that is highly selective for aggrecanases over a panel of metalloproteases and inhibits the degradation of native fully glycosylated aggrecan. A docking study generated binding conformations explaining the structure-activity relationships.
骨关节炎是一种致残性疾病,其特征为关节软骨的破坏。聚集酶是治疗这种病理的潜在治疗靶点。在这个项目的开始阶段,发现一种酰基硫代缩氨基脲抑制聚集酶-2。酰基硫代缩氨基脲 Zn 结合基团也是文库合成的便利连接物。因此,制备并筛选了一个重点 920 个类似物文库,以建立构效关系。还探索了酰基硫代缩氨基脲的修饰。这种结合文库设计和离散化合物合成的策略产生了抑制剂 35,它对一组金属蛋白酶具有高度的聚集酶选择性,并抑制天然完全糖基化聚集蛋白的降解。对接研究生成了结合构象,解释了构效关系。