A comparative reverse docking strategy to identify potential antineoplastic targets of tea functional components and binding mode

International Journal of Molecular Sciences

Volumn 12, Issue 8, 2011, Pages 5200-5212

  Zheng, Rong ^a   Chen, Tuan sheng ^b   Lu, Tun ^a,c  

^a FUZHOU UNIVERSITY   (China)

^b FUJIAN AGRICULTURE AND FORESTRY UNIVERSITY   (China)

^c Fujian Supercomputing Center   (China)

Author keywords

Binding mode; Reverse docking; Target protein; Tea polyphenols; Virtual screening

Indexed keywords

CATALASE; EPICATECHIN; EPICATECHIN GALLATE; EPIGALLOCATECHIN; EPIGALLOCATECHIN GALLATE; GLUTATHIONE REDUCTASE; LEUKOTRIENE A4 HYDROLASE; ANTINEOPLASTIC AGENT; CATECHIN; EPOXIDE HYDROLASE; POLYPHENOL; PROTEIN BINDING; TEA;

ANTINEOPLASTIC ACTIVITY; ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DATA ANALYSIS SOFTWARE; DRUG RECEPTOR BINDING; DRUG STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; GENE; HUMAN; HYDROGEN BOND; INTERMETHOD COMPARISON; LEUKOTRIENE A4 HYDOLASE GENE; LIGAND BINDING; MOLECULAR DOCKING; MOLECULARLY TARGETED THERAPY; PROTEIN TARGETING; STRUCTURE ANALYSIS; TEA; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; CONFORMATION; DRUG DEVELOPMENT; METABOLISM; QUANTITATIVE STRUCTURE ACTIVITY RELATION;

ANTINEOPLASTIC AGENTS; CATECHIN; COMPUTER SIMULATION; DRUG DISCOVERY; EPOXIDE HYDROLASES; HUMANS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR DOCKING SIMULATION; POLYPHENOLS; PROTEIN BINDING; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; TEA;

EID: 80052148863     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12085200     Document Type: Article

References (29)

1. Wang, H.Y.; Ding, J.; Yang, F. Cell signal transduction and development of targeted anti-tumor agent. Chin. J. Cancer Biother. 2007, 14, 401-404.
2. Tachibana, H.; Koga, K.; Fujimura, Y.; Yamada, K. A receptor for green tea polyphenol EGCG. Nat. Struct. Mol. Biol. 2004, 11, 380-381.
3. Umeda, D.; Yano, S.; Yamada, K.; Tachibana, H. Green tea polyphenol epigallocatechin-3-gallate signaling pathway through 67-kDa laminin receptor. J. Biol. Chem. 2008, 283, 3050-3058.
4. Adachi, S.; Nagao, T.; To, S.; Joe, A.K.; Shimizu, M.; Matsushima-Nishiwaki, R.; Kozawa, O.; Moriwaki, H.; Maxfield, F.R.; Weinstein, I.B. (-)-Epigallocatechin gallate causes internalization of the epidermal growth factor receptor in human colon cancer cells. Carcinogenesis 2008, 29, 1986-1993.
5. Hajduk, P.J.; Huth, J.R.; Tse, C. Predicting protein druggability. Drug Discov. Today 2005, 10, 1675-1682.
6. Huang, C.M.; Elmets, C.A.; Tang, D.C.; Li, F.; Yusuf, N. Proteomics reveals that proteins expressed during the early stage of Bacillus anthracis infection are potential targets for the development of vaccines and drugs. Genomics Proteomics Bioinforma. 2004, 3, 143-151.
7. Persidis, A. Proteomics: An ambitious drug development platform attempts to link gene sequence to expressed phenotype under various physiological states. Nat. Biotechnol. 1998, 16, 393-394.
8. Lin, J.H.; Lu, A.Y. Role of pharmacokinetics and metabolism in drug discovery and development. Pharmacol. Rev. 1997, 49, 403-449.
9. Chen, Y.Z.; Ung, C.Y. Prediction of potential toxicity and side effect protein targets of a small molecule by a ligand-protein inverse docking approach. J. Mol. Graph. Model. 2001, 20, 199-218.
10. Li, H.; Gao, Z.; Kang, L.; Zhang, H.; Yang, K.; Yu, K.; Luo, X.; Zhu, W.; Chen, K.; Shen, J.; et al. TarFisDock: A web server for identifying drug targets with docking approach. Nucleic Acids Res. 2006, 34, W219-W224.
11. Ewing, T.J.A.; Kuntz, I.D. Critical evaluation of search algorithms for automated molecular docking and database screening. J. Comput. Chem. 1997, 18, 1175-1189.
12. Morris, G.M.; Goodsell, D.S.; Halliday, R.S.; Huey, R.; Hart, W.E.; Belew, R.K.; Olson, A.J. Automated docking using a lamarckian genetic algorithm and and empirical binding free energy function. J. Comput. Chem. 1998, 19, 1639-1662.
13. Smith, D.M.; Daniel, K.G.; Wang, Z.; Guida, W.C.; Chan, T.H.; Dou, Q.P. Docking studies and model development of tea polyphenol proteasome inhibitors: Applications to rational drug design. Proteins 2004, 54, 58-70.
14. Rao, M.S.; Olson, A.J. Modelling of factor Xa-inhibitor complexes: A computational flexible docking approach. Proteins 1999, 34, 173-183.
15. Dym, O.; Xenarios, I.; Ke, H.; Colicelli, J. Molecular docking of competitive phosphodiesterase inhibitors. Mol. Pharmacol. 2002, 61, 20-25.
16. Harriman, D.J.; Deslongchamps, G. Reverse-docking as a computational tool for the study of asymmetric organocatalysis. J. Comput. Aided Mol. Des. 2004, 18, 303-308.
17. Gao, Z.; Li, H.; Zhang, H.; Liu, X.; Kang, L.; Luo, X.; Zhu, W.; Chen, K.; Wang, X.; Jiang, H. PDTD: A web-accessible protein database for drug target identification. BMC Bioinforma. 2008, 9, 104-110.
18. Yamaguchi, K.; Honda, M.; Ikigai, H.; Hara, Y.; Shimamura, T. Inhibitory effects of (-)-epigallocatechin gallate on the life cycle of human immunodeficiency virus type 1 (HIV-1). Antivir. Res. 2002, 53, 19-34.
19. Ramirez-Mares, M.V.; de Mejia, E.G. Comparative study of the antioxidant effect of ardisin and epigallocatechin gallate in rat hepatocytes exposed to benomyl and 1-nitropyrene. Food Chem. Toxicol. 2003, 41, 1527-1535.
20. Ahmed, I.; John, A.; Vijayasarathy, C.; Robin, M.A.; Raza, H. Differential modulation of growth and glutathione metabolism in cultured rat astrocytes by 4-hydroxynonenal and green tea polyphenol, epigallocatechin-3-gallate. Neurotoxicology 2002, 23, 289-300.
21. Raederstorff, D.G.; Schlachter, M.F.; Elste, V.; Weber, P. Effect of EGCG on lipid absorption and plasma lipid levels in rats. J. Nutr. Biochem. 2003, 14, 326-332.
22. Zigman, S. Do tea polyphenols protect dogfish lens (mustelus canis) catalase against UV damage? Biol. Bull. 1997, 193, 253-254.
23. Lee, W.J.; Shim, J.Y.; Zhu, B.T. Mechanisms for the inhibition of DNA methyltransferases by tea catechins and bioflavonoids. Mol. Pharmacol. 2005, 68, 1018-1030.
24. Shim, J.H.; Choi H.S.; Pugliese, A.; Lee, S.Y.; Chae, J.I.; Choi, B.I.; Bode, A.M.; Dong, Z. (-)-Epigallocatechin gallate regulates CD3-mediated T cell receptor signaling in leukemia through the inhibition of ZAP-70 kinase. J. Biol. Chem. 2008, 283, 28370-28379.
25. He, Z.; Tang, F.; Ermakova, S.; Li, M.; Zhao, Q.; Cho, Y.-Y.; Ma, W.-Y.; Choi, H.-S.; Bode, A.M.; Yang, C.S.; et al. Fyn is a novel target of (-)-epigallocatechin gallate in the inhibition of JB6 Cl41 cell transformation. Mol. Carcinog. 2008, 47, 172-183.
26. Okamoto, T. NSAID zaltoprofen improves the decrease in body weight in rodent sickness behavior models: Proposed new applications of NSAIDs (Review). Int. J. Mol. Med. 2002, 9, 369-372.
27. Daniel, L.; Lechevallier, E.; Giorgi, R.; Sichez, H.; Zattara-Cannoni, H. Pax-2 expression in adult renal tumors. Hum. Pathol. 2001, 32, 282-287.
28. Huey, R.; Morris, G.M.; Olson, A.J.; Goodsell, D.S. A semiempirical free energy force field with charge-based desolvation. J. Comput. Chem. 2007, 28, 1145-1152.
29. Hakonarson, H.; Thorvaldsson, S.; Helgadottir, A.; Gudbjartsson, D.; Zink, F.; Andresdottir, M.; Manolescu, A.; Arnar, D.O.; Andersen, K.; Sigurdsson, A.; et al. Effects of a 5-lipoxygenase-activating protein inhibitor on biomarkers associated with risk of myocardial infarction: a randomized trial. JAMA 2005, 293, 2245-2256.