Identification of small-molecule inhibitors of the human S100B-p53 interaction and evaluation of their activity in human melanoma cells

Bioorganic and Medicinal Chemistry

Volumn 21, Issue 5, 2013, Pages 1109-1115

  Yoshimura, Chihoko ^a,b   Miyafusa, Takamitsu ^a   Tsumoto, Kouhei ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b TAIHO PHARMACEUTICAL CO LTD   (Japan)

Author keywords

Fragment; Inhibitor; p53; Protein protein interaction; S100B; Surface plasomon resonance

Indexed keywords

ANTINEOPLASTIC AGENT; PENTAMIDINE; PROTEIN INHIBITOR; PROTEIN P53; PROTEIN S100B; SMALL MOLECULE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; CANCER INHIBITION; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG DATABASE; DRUG IDENTIFICATION; DRUG MECHANISM; DRUG PROTEIN BINDING; DRUG SCREENING; DRUG STRUCTURE; DRUG TARGETING; HUMAN; HUMAN CELL; IC 50; MELANOMA; MELANOMA CELL; MOLECULAR LIBRARY; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION;

CELL LINE, TUMOR; CELL SURVIVAL; HUMANS; MELANOMA; PROTEIN INTERACTION MAPS; RECOMBINANT PROTEINS; S100 PROTEINS; SMALL MOLECULE LIBRARIES; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84873732098     PISSN: 09680896     EISSN: 14643391     Source Type: Journal    
DOI: 10.1016/j.bmc.2012.12.042     Document Type: Article

References (35)

1. E. Tremante, A. Ginebri, E. Lo Monaco, P. Frascione, F. Di Filippo, I. Terrenato, M. Benevolo, M. Mottolese, E. Pescarmona, P. Visca, P.G. Natali, and P. Giacomini Lancet Oncol. 13 2012 e205
2. J.M. Bonfrer, C.M. Korse, O.E. Nieweg, and E.M. Rankin Br. J. Cancer 77 1998 2210
3. R. Donato Microsc. Res. Tech. 60 2003 540
4. K.H. Vousden Cell 103 2000 691
5. A.J. Levine Cell 88 1997 323
6. P.T. Wilder, J. Lin, C.L. Bair, T.H. Charpentier, D. Yang, M. Liriano, K.M. Varney, A. Lee, A.B. Oppenheim, S. Adhya, F. Carrier, and D.J. Weber Biochim. Biophys. Acta 1763 2006 1284
7. C. Scotto, J.C. Deloulme, D. Rousseau, E. Chambaz, and J. Baudier Mol. Cell. Biol. 18 1998 4272
8. J. Lin, Q. Yang, P. Wilder, and F. Carrier J. Biol. Chem. 285 2010 27487
9. Y. Arendt, A. Bhaumik, R. Del Conte, C. Luchinat, M. Mori, and M. Porcu ChemMedChem 2 2007 1648
10. P. Athri, T. Wenzler, P. Ruiz, R. Brun, D.W. Boykin, R. Tidwell, and W.D. Wilson Bioorg. Med. Chem. 14 2006 3144
11. Z. Zhou, and Y. Li J. Comput. Aided Mol. Des. 23 2009 705
12. T.H. Charpentier, P.T. Wilder, M.A. Liriano, K.M. Varney, S. Zhong, A. Coop, E. Pozharski, A.D. MacKerell, E.A. Toth, and D.J. Weber Biochemistry 48 2009 6202
13. M. Agamennone, L. Cesari, D. Lalli, E. Turlizzi, R. Del Conte, P. Turano, S.P.A. Mangani, M. Agamennone, L. Cesari, D. Lalli, E. Turlizzi, R. Del Conte, P. Turano, S. Mangani, and A. Padova ChemMedChem 5 2010 428
14. J.L. Whitlow, J.F. Varughese, Z. Zhou, L.J. Bartolotti, and Y. Li J. Mol. Graph. Model 27 2009 969
15. J.-J. Lu, and C.-H. Lee J. Formos. Med. Assoc. 107 2008 830
16. P.T. Wilder, T.H. Charpentier, M.A. Liriano, K. Gianni, M. Kristen, E. Pozharski, A. Coop, E.A. Toth, A.D. Mackerell, and J. David Int. J. High Throughput Screening 2010 109
17. T.H. Charpentier, L.E. Thompson, M.A. Liriano, K.M. Varney, T. Wilder, E. Pozharski, E.A. Toth, and D.J. Weber J. Mol. Biol. 396 2010 1227
18. C.W. Murray, M.L. Verdonk, and D.C. Rees Trends Pharm. Sci. 33 2012 224
19. J. Weiss, K. Schwechheimer, W.K. Cavenee, and M.A.K. Herlyn Int. J. Cancer 54 1993 693
20. E. Leclerc, C.W. Heizmann, and S.W. Vetter Gen. Physiol. Biophys. 28 2009 F65
21. T.H. Charpentier, P.T. Wilder, M.A. Liriano, K.M. Varney, E. Pozharski, A.D. MacKerell, A. Coop, E.A. Toth, and D.J. Weber J. Mol. Biol. 382 2008 56
22. A.P. McGrath, K.M. Hilmer, C.A. Collyer, E.M. Shepard, B.O. Elmore, D.E. Brown, D.M. Dooley, and J.M. Guss Biochemistry 48 2009 9810
23. Karen J. Edwards, Terence C. Jenkins, and Stephen Neidle Biochemistry 31 1992 7104
24. T. Sun, and Y. Zhang Nucleic Acids Res. 36 2008 1654
25. B.E. Brooks, K.M. Piro, and R.G. Brennan J. Am. Chem. Soc. 129 2007 8389
26. J.M. Barnard, and G.M. Downs J. Chem. Inf. Comput. Sci. 38 1998 983
27. MOE: Molecular Operating Environment. Chemical Computing Group (CCG) Montreal. http://www.chemcomp.com/software.htm.
28. A.C. Drohat, D.M. Baldisseri, R.R. Rustandi, and D.J. Weber Biochemistry 37 1998 2729
29. W.W. Streicher, M.M. Lopez, and G.I. Makhatadze Biochemistry 48 2009 2788
30. J.-H. Zhang, T.D.Y. Chang, and K.R. Oldenberg J. Biomol. Screen. 4 1999 67
31. Z. Nikolovska-Coleska, R. Wang, X. Fang, H. Pan, Y. Tomita, P. Li, P.P. Roller, K. Krajewski, N.G. Saito, J.A. Stuckey, and S. Wang Anal. Biochem. 332 2004 261
32. i Calculator http://sw16.im.med.umich.edu/software/calc- ki/.
33. B.J. Gentil, C. Delphin, G.O. Mbele, J.C. Deloulme, M. Ferro, J. Garin, and J. Baudier J. Biol. Chem. 276 2001 23253
34. B.J. Sugarman, B.B. Aggarwal, I.S. Figari, M.A. Palladino Jr., P.E. Hass, and H.M. Shepard Science 230 1985 943
35. PyMol http://www.pymol.org/.