Selected article for: "active site and nucleophilic residue"

Author: Shie, Jiun-Jie; Fang, Jim-Min; Kuo, Chih-Jung; Kuo, Tun-Hsun; Liang, Po-Huang; Huang, Hung-Jyun; Yang, Wen-Bin; Lin, Chun-Hung; Chen, Jiun-Ling; Wu, Yin-Ta; Wong, Chi-Huey
Title: Discovery of potent anilide inhibitors against the severe acute respiratory syndrome 3CL protease.
  • Cord-id: cb3e3wna
  • Document date: 2005_1_1
  • ID: cb3e3wna
    Snippet: A diversified library of peptide anilides was prepared, and their inhibition activities against the SARS-CoV 3CL protease were examined by a fluorogenic tetradecapeptide substrate. The most potent inhibitor is an anilide derived from 2-chloro-4-nitroaniline, l-phenylalanine and 4-(dimethylamino)benzoic acid. This anilide is a competitive inhibitor of the SARS-CoV 3CL protease with K(i) = 0.03 muM. The molecular docking experiment indicates that the P1 residue of this anilide inhibitor is distant
    Document: A diversified library of peptide anilides was prepared, and their inhibition activities against the SARS-CoV 3CL protease were examined by a fluorogenic tetradecapeptide substrate. The most potent inhibitor is an anilide derived from 2-chloro-4-nitroaniline, l-phenylalanine and 4-(dimethylamino)benzoic acid. This anilide is a competitive inhibitor of the SARS-CoV 3CL protease with K(i) = 0.03 muM. The molecular docking experiment indicates that the P1 residue of this anilide inhibitor is distant from the nucleophilic SH of Cys145 in the active site.

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