Quantitative insights for the design of substrate-based SIRT1 inhibitors

European Journal of Pharmaceutical Sciences

Volumn 59, Issue 1, 2014, Pages 12-19

  Kokkonen, Piia ^a   Mellini, Paolo ^a   Nyrhilä, Olli ^a   Rahnasto Rilla, Minna ^a   Suuronen, Tiina ^a   Kiviranta, Päivi ^a   Huhtiniemi, Tero ^a   Poso, Antti ^a   Jarho, Elina ^a   Lahtela Kakkonen, Maija ^a  

^a UNIVERSITY OF EASTERN FINLAND   (Finland)

Author keywords

CoMFA; Inhibitor; QSAR; SIRT1; Sirtuin

Indexed keywords

HYDROGEN; HYDROLASE INHIBITOR; SIRTUIN 1 INHIBITOR; UNCLASSIFIED DRUG; ENZYME INHIBITOR; SIRT1 PROTEIN, HUMAN; SIRTUIN 1;

ARTICLE; COMPARATIVE MOLECULAR FIELD ANALYSIS; CONTROLLED STUDY; DRUG DESIGN; DRUG DETERMINATION; ENZYME INHIBITION; HYDROGEN BOND; IC 50; MOLECULAR DOCKING; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; QUANTITATIVE STRUCTURE ACTIVITY RELATION; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY;

DRUG DESIGN; ENZYME INHIBITORS; MODELS, MOLECULAR; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; SIRTUIN 1;

EID: 84899893544     PISSN: 09280987     EISSN: 18790720     Source Type: Journal    
DOI: 10.1016/j.ejps.2014.04.003     Document Type: Article

References (27)

1. A. Balcerczyk, and L. Pirola Therapeutic potential of activators and inhibitors of sirtuins Biofactors 36 2010 383 393
2. A. Chalkiadaki, and L. Guarente Sirtuins mediate mammalian metabolic responses to nutrient availability Nat. Rev. Endocrinol. 8 2012 287 296
3. L. Chen Medicinal chemistry of sirtuin inhibitors Curr. Med. Chem. 18 2011 1936 1946
4. N. Chirico, and P. Gramatica Real external predictivity of QSAR models. Part 2. New intercomparable thresholds for different validation criteria and the need for scatter plot inspection J. Chem. Inf. Model 52 2012 2044 2058
5. R.D. Clark, and P.C. Fox Statistical variation in progressive scrambling J. Comput. Aided Mol. Des. 18 2004 563 576
6. R.D. Cramer, D.E. Patterson, and J.D. Bunce Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins J. Am. Chem. Soc. 110 1988 5959 5967
7. D.G. Fatkins, A.D. Monnot, and W. Zheng Nepsilon-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine Nepsilon-deacetylation Bioorg. Med. Chem. Lett. 16 2006 3651 3656 (Pubitemid 44137231)
8. Glide version 5.7, 2011. Schrödinger, LLC, New York, NY.
9. M.C. Haigis, and D.A. Sinclair Mammalian sirtuins: biological insights and disease relevance Annu. Rev. Pathol. 5 2010 253 295
10. W.F. Hawse, K.G. Hoff, D.G. Fatkins, A. Daines, O.V. Zubkova, V.L. Schramm, W. Zheng, and C. Wolberger Structural insights into intermediate steps in the Sir2 deacetylation reaction Structure 10 2008 1368 1377
11. T. Huhtiniemi, T. Suuronen, M. Lahtela-Kakkonen, T. Bruijn, S. Jaaskelainen, A. Poso, A. Salminen, J. Leppanen, and E. Jarho N(epsilon)-modified lysine containing inhibitors for SIRT1 and SIRT2 Bioorg. Med. Chem. 18 2010 5616 5625
12. T. Huhtiniemi, H.S. Salo, T. Suuronen, A. Poso, A. Salminen, J. Leppanen, E. Jarho, and M. Lahtela-Kakkonen Structure-based design of pseudopeptidic inhibitors for SIRT1 and SIRT2 J. Med. Chem. 54 2011 6456 6468
13. L. Jin, W. Wei, Y. Jiang, H. Peng, J. Cai, C. Mao, H. Dai, W. Choy, J.E. Bemis, M.R. Jirousek, J.C. Milne, C.H. Westphal, and R.B. Perni Crystal structures of human SIRT3 displaying substrate-induced conformational changes J. Biol. Chem. 284 2009 24394 24405
14. P.H. Kiviranta, T. Suuronen, E.A. Wallen, J. Leppanen, J. Tervonen, S. Kyrylenko, A. Salminen, A. Poso, and E.M. Jarho N(epsilon)-thioacetyl-lysine- containing tri-, tetra-, and pentapeptides as SIRT1 and SIRT2 inhibitors J. Med. Chem. 52 2009 2153 2156
15. LigPrep version 2.5, 2011. Schrödinger; LLC, New York, NY.
16. Maestro version 9.2, 2011. Schrödinger, LLC, New York, NY.
17. P. Mellini, T. Kokkola, T. Suuronen, H.S. Salo, L. Tolvanen, A. Mai, M. Lahtela-Kakkonen, and E.M. Jarho Screen of pseudopeptidic inhibitors of human sirtuins 1-3: two lead compounds with antiproliferative effects in cancer cells J. Med. Chem. 56 17 2013 6681 6695
18. S. Pagans, A. Pedal, B.J. North, K. Kaehlcke, B.L. Marshall, A. Dorr, C. Hetzer-Egger, P. Henklein, R. Frye, M.W. McBurney, H. Hruby, M. Jung, E. Verdin, and M. Ott SIRT1 regulates HIV transcription via Tat deacetylation PLoS Biol. 3 2005 e41
19. Pearlman, R.S., Concord. 6.1.3.
20. Prime version 3.0, 2011. Schrödinger, LLC, New York, NY.
21. C. Sebastian, F.K. Satterstrom, M.C. Haigis, and R. Mostoslavsky From sirtuin biology to human diseases: an update J. Biol. Chem. 287 2012 42444 42452
22. SYBYL-X 2.0, 2011. Tripos International, 1699 South Hanley Rd., St. Louis, Missouri, 63144, USA.
23. K.C. Tsai, Y.C. Chen, N.W. Hsiao, C.L. Wang, C.L. Lin, Y.C. Lee, M. Li, and B. Wang A comparison of different electrostatic potentials on prediction accuracy in CoMFA and CoMSIA studies Eur. J. Med. Chem. 45 2010 1544 1551
24. Y. Wang, C. Xu, Y. Liang, and P.M. Vanhoutte SIRT1 in metabolic syndrome: where to target matters Pharmacol. Ther. 136 2012 305 318
25. H. Yuan, and R. Marmorstein Structural basis for sirtuin activity and inhibition J. Biol. Chem. 51 2012 42428 42435
26. L. Zhang, K.C. Tsai, L. Du, H. Fang, M. Li, and W. Xu How to generate reliable and predictive CoMFA models Curr. Med. Chem. 18 2011 923 930
27. X. Zhao, D. Allison, B. Condon, F. Zhang, T. Gheyi, A. Zhang, S. Ashok, M. Russell, I. Macewan, Y. Qian, J.A. Jamison, and J.G. Luz The 2.5 a crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD(+)) and an Indole (EX527 Analogue) reveals a novel mechanism of histone deacetylase inhibition J. Med. Chem. 56 2013 963 969