Identification of FDA-approved Drugs that Computationally Bind to MDM2

Chemical Biology and Drug Design

Volumn 80, Issue 4, 2012, Pages 631-637

  Warner, Wayne A ^a   Sanchez, Ricardo ^a   Dawoodian, Alex ^a   Li, Esther ^a   Momand, Jamil ^a  

^a CALIFORNIA STATE UNIVERSITY   (United States)

Author keywords

Cancer; Drugs; FDA; MDM2; Nutlin; P53; Repositioning; Repurposing

Indexed keywords

ANTINEOPLASTIC AGENT; AZARIBINE; AZELASTINE; AZLOCILLIN; BEPRIDIL; CARAMIPHEN; DOXAPRAM; FEPRAZONE; LIGASE INHIBITOR; LORCAINIDE; MEPHENOXALONE; MIDAZOLAM; NAFTIDROFURYL; NANDROLONE PHENPROPIONATE; NUTLIN 2; NUTLIN 3; PHENYLBUTAZONE; PROTEIN MDM2; PROTEIN P53; PROTIRELIN;

ARTICLE; COMPUTATIONAL CONFORMER SELECTION; COMPUTER ANALYSIS; COMPUTER MODEL; CONTROLLED STUDY; DRUG APPROVAL; DRUG IDENTIFICATION; DRUG PROTEIN BINDING; DRUG SCREENING; FOOD AND DRUG ADMINISTRATION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN STRUCTURE;

BEPRIDIL; COMPUTER-AIDED DESIGN; DRUG APPROVAL; DRUG DESIGN; HUMANS; IMIDAZOLES; MOLECULAR CONFORMATION; MOLECULAR DOCKING SIMULATION; PIPERAZINES; PROTO-ONCOGENE PROTEINS C-MDM2; UNITED STATES; UNITED STATES FOOD AND DRUG ADMINISTRATION;

EID: 84866609418     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2012.01428.x     Document Type: Article

References (37)

1. Vogelstein B., Lane D., Levine A.J. (2000) Surfing the p53 network. Nature;408:307-310.
2. Olivier M., Hollstein M., Hainaut P. (2010) TP53 mutations in human cancers: origins, consequences, and clinical use. Cold Spring Harb Perspect Biol;2:a001008.
3. Levine A.J., Hu W., Feng Z. (2006) The P53 pathway: what questions remain to be explored? Cell Death Differ;13:1027-1036.
4. Oliner J.D., Kinzler K.W., Meltzer P.S., George D.L., Vogelstein B. (1992) Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature;358:80-83.
5. Momand J., Jung D., Wilczynski S., Niland J. (1998) The MDM2 gene amplification database. Nucleic Acids Res;26:3453-3459.
6. Bond G.L., Hirshfield K.M., Kirchhoff T., Alexe G., Bond E.E., Robins H., Bartel F. et al. (2006) MDM2 SNP309 accelerates tumor formation in a gender-specific and hormone-dependent manner. Cancer Res;66:5104-5110.
7. Araki S., Eitel J.A., Batuello C.N., Bijangi-Vishehsaraei K., Xie X.J., Danielpour D., Pollok K.E. et al. (2010) TGF-beta1-induced expression of human Mdm2 correlates with late-stage metastatic breast cancer. J Clin Invest;120:290-302.
8. Haupt Y., Maya R., Kazaz A., Oren M. (1997) Mdm2 promotes the rapid degradation of p53. Nature;387:296-299.
9. Kubbutat M.H., Jones S.N., Vousden K.H. (1997) Regulation of p53 stability by Mdm2. Nature;387:299-303.
10. Honda R., Tanaka H., Yasuda H. (1997) Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett;420:25-27.
11. Wu X., Bayle J.H., Olson D., Levine A.J. (1993) The p53-mdm-2 autoregulatory feedback loop. Genes Dev;7:1126-1132.
12. Kastan M.B., Onyekwere O., Sidransky D., Vogelstein B., Craig R.W. (1991) Participation of p53 protein in the cellular response to DNA damage. Cancer Res;51:6304-6311.
13. Chen L., Agrawal S., Zhou W., Zhang R., Chen J. (1998) Synergistic activation of p53 by inhibition of MDM2 expression and DNA damage. Proc Natl Acad Sci USA;95:195-200.
14. Vassilev L.T., Vu B.T., Graves B., Carvajal D., Podlaski F., Filipovic Z., Kong N. et al. (2004) In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science;303:844-848.
15. Cheok C.F., Verma C.S., Baselga J., Lane D.P. (2011) Translating p53 into the clinic. Nat Rev Clin Oncol;8:25-37.
16. Tovar C., Rosinski J., Filipovic Z., Higgins B., Kolinsky K., Hilton H., Zhao X. et al. (2006) Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy. Proc Natl Acad Sci USA;103:1888-1893.
17. Shangary S., Wang S. (2009) Small-molecule inhibitors of the MDM2-p53 protein-protein interaction to reactivate p53 function: a novel approach for cancer therapy. Annu Rev Pharmacol Toxicol;49:223-241.
18. Weber L. (2010) Patented inhibitors of p53-Mdm2 interaction (2006-2008). Expert Opin Ther Pat;20:179-191.
19. Duenas-Gonzalez A., Garcia-Lopez P., Herrera L.A., Medina-Franco J.L., Gonzalez-Fierro A., Candelaria M. (2008) The prince and the pauper. A tale of anticancer targeted agents. Mol Cancer;7:82.
20. Trott O., Olson A.J. (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem;31:455-461.
21. Irwin J.J., Shoichet B.K. (2005) ZINC - a free database of commercially available compounds for virtual screening. J Chem Inf Model;45:177-182.
22. Hawkins P.C., Skillman A.G., Warren G.L., Ellingson B.A., Stahl M.T. (2010) Conformer generation with OMEGA: algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database. J Chem Inf Model;50:572-584.
23. Rush T.S. III, Grant J.A., Mosyak L., Nicholls A. (2005) A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction. J Med Chem;48:1489-1495.
24. Bostrom J., Greenwood J.R., Gottfries J. (2003) Assessing the performance of OMEGA with respect to retrieving bioactive conformations. J Mol Graph Model;21:449-462.
25. Wallace A.C., Laskowski R.A., Thornton J.M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng;8:127-134.
26. Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., Ferrin T.E. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem;25:1605-1612.
27. Kussie P.H., Gorina S., Marechal V., Elenbaas B., Moreau J., Levine A.J., Pavletich N.P. (1996) Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science;274:948-953.
28. Halgren T.A. (1996) Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J Comb Chem;17:490-519.
29. Kirchmair J., Wolber G., Laggner C., Langer T. (2006) Comparative performance assessment of the conformational model generators omega and catalyst: a large-scale survey on the retrieval of protein-bound ligand conformations. J Chem Inf Model;46:1848-1861.
30. Riedinger C., Noble M.E., Wright D.J., Mulks F., Hardcastle I.R., Endicott J.A., McDonnell J.M. (2011) Understanding small-molecule binding to MDM2: insights into structural effects of isoindolinone inhibitors from NMR spectroscopy. Chem Biol Drug Des;77:301-308.
31. Solaro R.J., Bousquet P., Johnson J.D. (1986) Stimulation of cardiac myofilament force, ATPase activity and troponin C Ca++ binding by bepridil. J Pharmacol Exp Ther;238:502-507.
32. MacLachlan L.K., Reid D.G., Mitchell R.C., Salter C.J., Smith S.J. (1990) Binding of a calcium sensitizer, bepridil, to cardiac troponin C. A fluorescence stopped-flow kinetic, circular dichroism, and proton nuclear magnetic resonance study. J Biol Chem;265:9764-9770.
33. Li Y., Love M.L., Putkey J.A., Cohen C. (2000) Bepridil opens the regulatory N-terminal lobe of cardiac troponin C. Proc Natl Acad Sci USA;97:5140-5145.
34. Dudley J.T., Deshpande T., Butte A.J. (2011) Exploiting drug-disease relationships for computational drug repositioning. Brief Bioinform;12:303-311.
35. Grese T.A., Sluka J.P., Bryant H.U., Cullinan G.J., Glasebrook A.L., Jones C.D., Matsumoto K. et al. (1997) Molecular determinants of tissue selectivity in estrogen receptor modulators. Proc Natl Acad Sci USA;94:14105-14110.
36. Koul H.K., Koul S., Meacham R.B. (2012) New role for an established drug? Bisphosphonates as potential anticancer agents. Prostate Cancer Prostatic Dis;15:111-119.
37. Keiser M.J., Setola V., Irwin J.J., Laggner C., Abbas A.I., Hufeisen S.J., Jensen N.H. et al. (2009) Predicting new molecular targets for known drugs. Nature;462:175-181.