Author: 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
Title: Synthesis, crystal structure, structure-activity relationships, and antiviral activity of a potent SARS coronavirus 3CL protease inhibitor. Cord-id: s9jrsz91 Document date: 2006_1_1
ID: s9jrsz91
Snippet: A potent SARS coronavirus (CoV) 3CL protease inhibitor (TG-0205221, Ki = 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 microM) for SARS CoV and 5.2 log (at 1.25 microM) 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 c
Document: A potent SARS coronavirus (CoV) 3CL protease inhibitor (TG-0205221, Ki = 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 microM) for SARS CoV and 5.2 log (at 1.25 microM) 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.
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