Synthesis and evaluation of isatin derivatives as effective SARS coronavirus 3CL protease inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 15, Issue 12, 2005, Pages 3058-3062

  Chen, Li Rung ^a   Wang, Yu Chin ^a   Yi, Wen Lin ^a   Chou, Shan Yen ^a   Chen, Shyh Fong ^a   Lee, Tai Liu ^a   Wu, Ying Ta ^b   Kuo, Chih Jung ^b   Chen, Tom Shieh Shung ^a   Juang, Shin Hun ^a  

^a DEVELOPMENT CENTER FOR BIOTECHNOLOGY   (Taiwan)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

Isatin; SARS CoV protease inhibitor

Indexed keywords

BROMINE DERIVATIVE; CHYMOTRYPSIN; ISATIN DERIVATIVE; PAPAIN; PROTEINASE; PROTEINASE INHIBITOR; TRYPSIN;

ARTICLE; CONTROLLED STUDY; DRUG ACTIVITY; DRUG POTENCY; DRUG SCREENING; DRUG SYNTHESIS; IC 50; IN VITRO STUDY; NONHUMAN; SARS CORONAVIRUS; SUBSTITUTION REACTION;

BINDING SITES; CHYMOTRYPSIN; COMPUTER SIMULATION; CYSTEINE ENDOPEPTIDASES; ENDOPEPTIDASES; ENZYME ACTIVATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; ISATIN; MOLECULAR STRUCTURE; PAPAIN; PROTEASE INHIBITORS; SARS VIRUS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRYPSIN; VIRAL PROTEINS;

SARS CORONAVIRUS; SARS COV;

EID: 19944378080     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2005.04.027     Document Type: Article

References (23)

1. N. Lee, D. Hui, A. Wu, P. Chan, P. Cameron, G.M. Joynt, A. Ahuja, M.Y. Yung, C.B. Leung, K.F. To, S.F. Lui, C.C. Szeto, S. Chung, and J.J.Y. Sung N. Engl. J. Med. 348 2003 1986
2. C. Drosten, S. Günther, W. Preiser, S. van der Werf, H.-R. Brodt, S. Becker, H. Rabenau, M. Panning, L. Kolesnikova, R.A.M. Fouchier, A. Berger, A.M. Burguière, J. Cinatl, M. Eickmann, N. Escriou, K. Grywna, S. Kramme, J.-C. Manuguerra, S. Müller, V. Rickerts, M. Stürmer, S. Vieth, H.-D. Klenk, A.D.M.E. Osterhaus, H. Schmitz, and H.W. Doerr N. Engl. J. Med. 348 2003 1967
3. L.K.-Y. So, A.C.W. Lau, L.Y.C. Yam, T.M.T. Cheung, E. Poon, R.W.H. Yung, and K.Y. Yuen Lancet 361 2003 1615
4. K.L.E. Hon, C.W. Leung, W.T.F. Cheng, P.K.S. Chan, W.C.W. Chu, Y.W. Kwan, A.M. Li, N.C. Fong, P.C. Ng, M.C. Chiu, C.K. Li, J.S. Tam, and T.F. Fok Lancet 361 2003 1701
5. N. Yamamoto, R. Yang, Y. Yoshinaka, S. Amari, T. Nakano, J. Cinatl, H. Rabenau, H.W. Doerr, G. Hunsmann, A. Otaka, H. Tamamura, N. Fujii, and N. Yamamoto Biochem. Biophys. Res. Commun. 318 2004 719
6. K. Anand, J. Ziebuhr, P. Wadhwani, J.R. Mesters, and R. Hilgenfeld Science 300 2003 1763
7. E.J. Snijder, P.J. Bredenbeek, J.C. Dobbe, V. Thiel, J. Ziebuhr, L.L.M. Poon, Y. Guan, M. Rozanov, W.J.M. Spaan, and A.E. Gorbalenya J. Mol. Biol. 331 2003 991
8. E. Jenwitheesuk, and R. Samudrala Bioorg. Med. Chem. Lett. 13 2003 3989
9. C.-Y. Wu, J.-T. Jan, S.-H. Ma, C.-J. Kuo, H.-F. Juan, Y.-S.E. Cheng, H.-H. Hsu, H.-C. Huang, D. Wu, A. Brik, F.-S. Liang, R.-S. Liu, J.-M. Fang, S.-T. Chen, P.-H. Liang, and C.-H. Wong PNAS 101 2004 10012
10. R.P. Jain, H.I. Pettersson, J. Zhang, K.D. Aull, P.D. Fortin, C. Huitema, L.D. Eltis, J.C. Parrish, M.N.G. James, D.S. Wishart, and J.C. Vederas J. Med. Chem. 47 2004 6113
11. J.H. Toney, S. Navas-Martin, S.R. Weiss, and A. Koeller J. Med. Chem. 47 2004 1079
12. U. Bacha, J. Barrila, A. Velazquez-Campoy, S.A. Leavitt, and E. Freire Biochemistry 43 2004 4906
13. J.E. Blanchard, N.H. Elowe, P.D. Fortin, C. Huitema, J.D. Cechetto, L.D. Eltis, and E.D. Brown Chem. Biol. 43 2004 1445
14. R.Y. Kao, W.H.W. Tsui, T.S.W. Lee, J.A. Tanner, R.M. Watt, J.-D. Huang, L. Hu, G. Chen, Z. Chen, L. Zhang, T. He, K.-H. Chan, H. Tse, A.P.C. To, L.W.Y. Ng, B.C.W. Wong, H.-W. Tsoi, D. Yang, D.D. Ho, and K.-Y. Yuen Chem. Biol. 43 2004 1293
15. J.T.-A. Hsu, C.-J. Kuo, H.-P. Hsieh, Y.-C. Wang, K.-K. Huang, C.P.-C. Lin, P.-F. Huang, X. Chen, and P.-H. Liang FEBS Lett. 574 2004 116
16. S.E. Webber, J. Tikhe, S.T. Worland, S.A. Fuhrman, T.F. Hendrickson, D.A. Matthews, R.A. Love, A.K. Patick, J.W. Meador, R.A. Ferre, E.L. Brown, D.M. DeLisle, C.E. Ford, and S.L. Binford J. Med. Chem. 39 1996 5072
17. +
18. C.-J. Kuo, Y.-H. Chi, J.T.-A. Hsu, and P.-H. Liang Biochem. Biophys. Res. Commun. 318 2004 862
19. J.E. Blanchard, N.H. Elowe, C. Huitema, P.D. Fortin, J.D. Cechetto, L.D. Eltis, and E.D. Brown Chem. Biol. 11 2004 1445
20. Substrate (Dabcyl-KTSAVLQSGFRKME-Edans) and the fragments (Dabcyl-KTSAVLQ, Edans-EMKRFGS) were analyzed by HPLC: Photodiarray detector monitored at UV 300 and 500 nm; reversed phase column COSMOSIL 5C18-MS 4.5 mm × 150 mm; 0.1% trifluoroacetic acid in acetonitrile/0.1% trifluoroacetic acid in water (10/90, v/v) for 20 min followed by a linear gradient to 0.1% trifluoroacetic acid in acetonitrile/0.1% trifluoroacetic acid in water (45/55, v/v) at the flow rate of 1.0 mL/min. A similar result has been reported during our research: K. Fan, P. Wei, Q. Feng, S. Chen, C. Huang, L. Ma, B. Lai, J. Pei, Y. Liu, J. Chen, and L. Lai J. Biol. Chem. 279 2004 1637
21. 16 merge non-polar H atoms, and defined torsions. Autogrid tool in Autodock3.0.5 was applied to compute energy grids (60 × 60 × 70 in xyz directions with 0.375 Å spacing) of various compound atoms. Grip maps were centered at the active site. Solis and Wets' local search method with LGA was applied to generate available conformations of compound structures within the active site. During docking experiments, each compound was kept flexible (except for the rings and amide bonds) and the protein was rigid
22. G.M. Morris, D.S. Goodsell, R.S. Halliday, R. Huey, W.E. Hart, R.K. Belew, and A.J. Olson J. Comput. Chem. 19 1998 1639
23. J. Gasteiger, and M. Marsili Tetrahedron 36 1980 3219