Zhou Lu, Liu Ying, Zhang Weilin, Wei Ping, Huang Changkang, Pei Jianfeng, Yuan Yaxia, Lai Luhua
State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
J Med Chem. 2006 Jun 15;49(12):3440-3. doi: 10.1021/jm0602357.
A series of isatin derivatives were synthesized and tested against SARS CoV 3C-like protease. Substitutions at the N-1 and C-5 positions were examined to elucidate the differences in substrate binding sites of the rhinovirus 3C protease and SARS CoV 3C-like protease. Compound 5f shows significant inhibition with an IC(50) of 0.37 microM. Further study showed that, unlike the irreversible covalent binding of isatin derivatives to human rhinovirus 3C protease, the compounds tested in this study are all noncovalent reversible inhibitors.
合成了一系列异吲哚酮衍生物，并针对严重急性呼吸综合征冠状病毒（SARS-CoV）3C样蛋白酶进行了测试。研究了N-1和C-5位的取代情况，以阐明鼻病毒3C蛋白酶和SARS-CoV 3C样蛋白酶底物结合位点的差异。化合物5f表现出显著抑制作用，IC50为0.37微摩尔。进一步研究表明，与异吲哚酮衍生物与人鼻病毒3C蛋白酶的不可逆共价结合不同，本研究中测试的化合物均为非共价可逆抑制剂。
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