belinostat

Ligand id: 7496

Name: belinostat

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Structure and Physico-chemical Properties

2D Structure
Calculated Physico-chemical Properties
Hydrogen bond acceptors 4
Hydrogen bond donors 3
Rotatable bonds 6
Topological polar surface area 103.88
Molecular weight 318.07
XLogP 3.22
No. Lipinski's rules broken 0

Molecular properties generated using the CDK

References
1. Bradner JE, West N, Grachan ML, Greenberg EF, Haggarty SJ, Warnow T, Mazitschek R. (2010)
Chemical phylogenetics of histone deacetylases.
Nat. Chem. Biol.6 (3): 238-243. [PMID:20139990]
2. Buckley MT, Yoon J, Yee H, Chiriboga L, Liebes L, Ara G, Qian X, Bajorin DF, Sun TT, Wu XR et al.. (2007)
The histone deacetylase inhibitor belinostat (PXD101) suppresses bladder cancer cell growth in vitro and in vivo.
J Transl Med5: 49. [PMID:17935615]
3. Khan N, Jeffers M, Kumar S, Hackett C, Boldog F, Khramtsov N, Qian X, Mills E, Berghs SC, Carey N et al.. (2008)
Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors.
Biochem. J.409 (2): 581-9. [PMID:17868033]
4. Plumb JA, Finn PW, Williams RJ, Bandara MJ, Romero MR, Watkins CJ, La Thangue NB, Brown R. (2003)
Pharmacodynamic response and inhibition of growth of human tumor xenografts by the novel histone deacetylase inhibitor PXD101.
Mol. Cancer Ther.2 (8): 721-8. [PMID:12939461]
5. Qian X, LaRochelle WJ, Ara G, Wu F, Petersen KD, Thougaard A, Sehested M, Lichenstein HS, Jeffers M. (2006)
Activity of PXD101, a histone deacetylase inhibitor, in preclinical ovarian cancer studies.
Mol. Cancer Ther.5 (8): 2086-95. [PMID:16928830]
6. Savickiene J, Treigyte G, Valiuliene G, Stirblyte I, Navakauskiene R. (2014)
Epigenetic and molecular mechanisms underlying the antileukemic activity of the histone deacetylase inhibitor belinostat in human acute promyelocytic leukemia cells.
Anticancer Drugs,  [Epub ahead of print]. [PMID:24800886]