898264-61-4Relevant academic research and scientific papers
A Quick Route to Multiple Highly Potent SARS-CoV-2 Main Protease Inhibitors**
Yang, Kai S.,Ma, Xinyu R.,Ma, Yuying,Alugubelli, Yugendar R.,Scott, Danielle A.,Vatansever, Erol C.,Drelich, Aleksandra K.,Sankaran, Banumathi,Geng, Zhi Z.,Blankenship, Lauren R.,Ward, Hannah E.,Sheng, Yan J.,Hsu, Jason C.,Kratch, Kaci C.,Zhao, Baoyu,Hayatshahi, Hamed S.,Liu, Jin,Li, Pingwei,Fierke, Carol A.,Tseng, Chien-Te K.,Xu, Shiqing,Liu, Wenshe Ray
supporting information, p. 942 - 948 (2020/12/15)
The COVID-19 pathogen, SARS-CoV-2, requires its main protease (SC2MPro) to digest two of its translated long polypeptides to form a number of mature proteins that are essential for viral replication and pathogenesis. Inhibition of this vital pr
Synthesis, crystal structure, structure-activity relationships, and antiviral activity of a potent SARS coronavirus 3CL protease inhibitor
Yang, Syaulan,Chen, Shu-Jen,Hsu, Min-Feng,Wu, Jen-Dar,Tseng, Chien-Te K.,Liu, Yu-Fan,Chen, Hua-Chien,Kuo, Chun-Wei,Wu, Chi-Shen,Chang, Li-Wen,Chen, Wen-Chang,Liao, Shao-Ying,Chang, Teng-Yuan,Hung, Hsin-Hui,Shr, Hui-Lin,Liu, Cheng-Yuan,Huang, Yu-An,Chang, Ling-Yin,Hsu, Jen-Chi,Peters, Clarence J.,Wang, Andrew H.-J.,Hsu, Ming-Chu
, p. 4971 - 4980 (2007/10/03)
A potent SARS coronavirus (CoV) 3CL protease inhibitor (TG-0205221, K i = 53 nM) has been developed. TG-0205221 showed remarkable activity against SARS CoV and human coronavirus (HCoV) 229E replications by reducing the viral titer by 4.7 log (at 5 μM) for SARS CoV and 5.2 log (at 1.25 μM) for HCoV 229E. The crystal structure of TG-0205221 (resolution = 1.93 A?) has revealed a unique binding mode comprising a covalent bond, hydrogen bonds, and numerous hydrophobic interactions. Structural comparisons between TG-0205221 and a natural peptide substrate were also discussed. This information may be applied toward the design of other 3CL protease inhibitors.
