Design and in Vitro Characterization of Tricyclic Benzodiazepine Derivatives as Potent and Selective Antileukemic Agents.
Animals
Antineoplastic Agents
/ chemistry
Apoptosis
/ drug effects
Benzodiazepines
/ chemistry
Binding Sites
Catalytic Domain
Cell Line
Cell Proliferation
/ drug effects
Crystallography, X-Ray
Drug Design
Drug Screening Assays, Antitumor
Humans
Mice
Molecular Conformation
Phosphoric Diester Hydrolases
/ chemistry
Stereoisomerism
Structure-Activity Relationship
autotaxin inhibition
benzodiazepines
cytotoxic agents
drug design
selectivity
Journal
Chemistry & biodiversity
ISSN: 1612-1880
Titre abrégé: Chem Biodivers
Pays: Switzerland
ID NLM: 101197449
Informations de publication
Date de publication:
Jan 2021
Jan 2021
Historique:
received:
05
09
2020
accepted:
24
11
2020
pubmed:
26
11
2020
medline:
29
6
2021
entrez:
25
11
2020
Statut:
ppublish
Résumé
Currently available chemotherapeutic treatments for blood cancers (leukemia) usually have strong side effects. More selective, efficient, and less toxic anticancer agents are needed. We synthesized seven, new, optically pure (12aS)-1,3,4,12a-tetrahydropyrazino[2,1-c][1,4],12(2H,11H)-dione derivatives and examined their cytotoxicity towards eight cancer cell lines, including urinary bladder (TCC-SUP, UM-UC-3, KU-19-9), colon (LoVo), and breast (MCF-7, MDA-MB-231) cancer representatives, as well as two leukemic cell lines (MV-4-11, CCRF-CEM) and normal murine fibroblasts (Balb/3T3) as reference cell line. Three of the seven newly-obtained compounds ((12aS)-8-bromo-2-(3-phenylbenzoyl)-1,3,4,12a-tetrahydropyrazino[2,1-c][1,4],12(2H,11H)-dione, (12aS)-8,9-dimethoxy-2-(4-phenylbenzoyl)-1,3,4,12a-tetrahydropyrazino[2,1-c][1,4],12(2H,11H)-dione and (12aS)-8-nitro-2-(4-phenylbenzoyl)-1,3,4,12a-tetrahydropyrazino[2,1-c][1,4],12(2H,11H)-dione, showed enhanced activity and selectivity toward the leukemic MV-4-11 cell lines when compared to our previously reported compounds, with IC
Identifiants
pubmed: 33236468
doi: 10.1002/cbdv.202000733
doi:
Substances chimiques
Antineoplastic Agents
0
Benzodiazepines
12794-10-4
Phosphoric Diester Hydrolases
EC 3.1.4.-
alkylglycerophosphoethanolamine phosphodiesterase
EC 3.1.4.39
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2000733Subventions
Organisme : Warsaw University of Technology
Organisme : National Science Center
ID : DEC-2011/01/B/NZ4/03566
Organisme : MAESTRO
ID : DEC-2012/04/A/ST5/00609
Organisme : National Science Center Poland
Informations de copyright
© 2020 Wiley-VHCA AG, Zurich, Switzerland.
Références
G. J. Szebeni, J. A. Balog, A. Demjén, R. Alföldi, V. L. Végi, L. Z. Fehér, I. Mán, E. Kotogány, B. Gubán, P. Batár, L. Hackler Jr., I. Kanizsai, L. G. Puskas, ‘Imidazo[1,2-b]-carboxamides Induce Apoptosis in Human Leukemia Cells at Nanomolar Concentrations’, Molecules 2018, 23, 2845.
C. Salmi-Smail, A. Fabre, F. Deuiedt, A. Restouin, R. Castellano, S. Garbit, P. Roche, X. Morelli, J. M. Brunel, Y. Colette, ‘Modified Cap Group Suberoylanilide Hydroxamic Acid Histone Deacetylase Inhibitor Derivatives Reveal Improved Selective Antileukemic Activity’, J. Med. Chem. 2010, 53, 3038-3047.
Y. Ge, I. Montano, G. Rustici, W. J. Freebern, C. M. Haggerty, W. Cui, D. Ponciano-Jackson, G. V. R. Chandramouli, E. R. Gardner, W. D. Figg, M. Abu-Asab, M. Tsokos, S. H. Jackson, K. Gardner, ‘Selective leukemic-cell killing by a novel functional class of thalidomide analogs’, Blood 2006, 108, 4126-4135.
N. L. Crossnohere, D. R. Richardson, C. Reinhart, B. O'Donoghue, S. M. Love, B. D. Smith, J. F. P. Bridges, ‘Side effects from acute myeloid leukemia treatment: results from a national survey’, Curr. Med. Res. Opin. 2019, 35, 1965-1970.
C. Shanholtz, ‘Acute life-threatening toxicity of cancer treatment’, Crit. Care Clin. 2001, 17, 483-502.
K. K. Ness, S. H. Armenian, N. Kadan-Lottick, J. G. Gurney, ‘Adverse effects of treatment in childhood acute lymphoblastic leukemia: general overview and implications for long-term cardiac health’, Expert Rev. Hematol. 2011, 4, 185-197.
A. Mieczkowski, D. Trzybiński, M. Wilczek, M. Psurski, M. Bagiński, B. Bieszczad, M. Mroczkowska, K. Woźniak, ‘(S)-2-(4-Chlorobenzoyl)-1,2,3,4-tetrahydrobenzo[e][1,2-a][1,4],12(11H,12aH)-dione - Synthesis and Crystallographic Studies’, Molbank 2017, 2017, M964.
A. Mieczkowski, M. Psurski, M. Bagiński, B. Bieszczad, M. Mroczkowska, M. Wilczek, J. Czajkowska, D. Trzybiński, K. Woźniak, J. Wietrzyk, ‘Novel (S)-1,3,4,12a-tetrahydropyrazino[2,1-c][1,4],12(2H,11H)-dione derivatives: Selective inhibition of MV-4-11 biphenotypic B myelomonocytic leukemia cells’ growth is accompanied by reactive oxygen species overproduction and apoptosis’, Bioorg. Med. Chem. Lett. 2018, 28, 618-625.
M. Schultz, K. Schiemann, W. Staehle, ‘Heterocyclic compounds as autotaxin inhibitors’, WO 2011/006569, 2011.
A. L. Parrill, D. L. Baker, ‘Autotaxin inhibition: challenges and progress toward novel anticancer agents’, Anti-Cancer Agents Med. Chem. 2008, 8, 917-923.
C. Ortlepp, C. Steudel, C. Heiderich, S. Koch, A. Jacobi, M. Ryser, S. Brenner, M. Bornhäuser, B. Brors, W. K. Hofman, G. Ehninger, C. Thiede, ‘Autotaxin is expressed in FLT3-ITD positive acute myeloid leukemia and hematopoietic stem cells and promotes cell migration and proliferation’, Exp. Hematol. 2013, 41, 444-461.
M. G. Benesch, Y. M. Ko, T. P. McMullen, D. N. Brindley, ‘Autotaxin in the crosshairs: taking aim at cancer and other inflammatory conditions’, FEBS Lett. 2014, 588, 2712-2727.
A. Masuda, K. Nakamura, K. Izutsu, K. Igarashi, R. Ohkawa, M. Jona, K. Higashi, H. Yokota, S. Okudaira, T. Kishimoto, T. Watanabe, Y. Koike, H. Ikeda, Y. Kozai, M. Kurokawa, J. Aoki, Y. Yatomi, ‘Serum autotaxin measurement in haematological malignancies: a promising marker for follicular lymphoma’, Br. J. Haematol. 2008, 143, 60-70.
F. Salgado-Polo, A. Perrakis, ‘The structural binding mode of the four inhibitor types that differentially affect catalytic and not-catalytic functions’, Cancers 2019, 11, 1577.
A. L. Speck, ‘Structure validation in chemical crystallography’, Acta Crystallogr. Sect. D 2009, 65, 148-155.
E. Barbayianni, E. Kaffe, V. Aidinis, G. Kokotos, ‘Autotaxin, a secreted lysophospholipase D, as a promising therapeutic target in chronic inflammation and cancer’, Prog. Lipid Res. D 2015, 58, 76-96.
Y. Zhao, S. Hasse, C. Zhao, S. G. Bourgoin, ‘Targeting the Autotaxin - Lysophosphatidic Acid Receptor Axis in Cardiovascular Diseases’, Biochem. Pharmacol. 2019, 164, 74-78.
E. Barbayianni, V. Magrioti, P. Moutevelis-Minakakis, G. Kokotos, ‘Autotaxin inhibitors: a patent review’, Expert Opin. Ther. Pat. 2013, 23, 1123-1132.
A. Nikolaou, M. G. Kokotou, D. Limnios, A. Psarra, G. Kokotos, ‘Autotaxin inhibitors: a patent review (2012 - 2016)’, Expert Opin. Ther. Pat. 2017, 27, 815-829.
H. M. H. G. Albert, H. Ovaa, ‘Chemical evolution of autotaxin inhibitors’, Chem. Rev. 2012, 112, 2593-2603.
S. Banerjee, D. D. Norman, S. Deng, S. O. Fakayode, S. C. Lee, A. L. Parrill, W. Lee, D. D. Miller, G. J. Tigyi, ‘Molecular modelling guided design, synthesis and QSAR analysis of new small molecule non-lipid autotaxin inhibitors’, Bioorg. Chem. 2020, 103, 104188.
A. Joncour, N. Desroy, C. Housseman, X. Bock, N. Bienvenu, L. Cherel, V. Labeguere, C. Peixoto, D. Annoot, L. Lepissier, J. Heiermann, W. J. Hengeveld, G. Pilzak, A. Monjardet, E. Wakselman, V. Roncoroni, S. Le Tallec, R. Galien, C. David, N. Vandervoort, T. Christophe, K. Conrath, M. Jans, A. Wohlkonig, S. Soror, J. Steyaert, R. Touitou, D. Fleury, L. Vercheval, P. Mollat, N. Triballeau, E. Van de Aar, R. Brys, B. Heckmann, ‘Discovery, Structure-Activity Relationship, and Binding Mode of an Imidazo[1,2-a]Series of Autotaxin Inhibitors’, J. Med. Chem. 2017, 60, 7371-7392.
T. Mosmann, ‘Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays’, J. Immunol. Methods 1983, 65, 55-63.
M. Psurski, Ł. Janczewski, M. Świtalska, A. Gajda, T. M. Goszczyński, J. Oleksyszyn, J. Wietrzyk, T. Gajda, ‘Novel phosphonate analogs of sulforaphane: Synthesis, In Vitro and In Vivo anticancer activity’, Eur. J. Med. Chem. 2017, 132, 63-80.
CrysAlis CCD and CrysAlis RED, Oxford Diffraction, Oxford Diffraction Ltd., Yarnton, 2008.
R. C. Clark, J. S. Reid, ‘The analytical calculation of absorption in multifaceted crystals’, Acta Crystallogr. Sect. A 1995, 51, 887-897.
G. M. Sheldrick, ‘A short history of SHELX’, Acta Crystallogr. Sect. A 2008, 64, 112-122.
O. V. Dolomanov, L. J. Bourhis, R. J. Gildea, J. A. K. Howard, H. Puschmann, ‘OLEX2: a complete structure solution, refinement and analysis program’, J. Appl. Crystallogr. 2009, 42, 339-341.
L. J. Farrugia, ‘WinGX and ORTEP for Windows: an update’, J. Appl. Crystallogr. 2012, 45, 849-854.
M. V. Shapovalov, R. L. Dunbrack Jr., ‘A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressions’, Structure 2011, 19, 844-858.
E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt, E. C. Meng, T. E. Ferrin, ‘UCSF Chimera - a visualization system for exploratory research and analysis’, J. Comput. Chem. 2004, 25, 1605-1612.
J. A. Maier, C. Martinez, K. Kasavajhala, L. Wickstrom, K. E. Hauser, C. Simmerling, ‘ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB’, J. Chem. Theory Comput. 2015, 11, 3696-3713.
O. Trott, A. J. Olson, ‘AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading’, J. Comput. Chem. 2010, 31, 455-461.
N. M. O'Boyle, M. Banck, C. A. James, C. Morley, T. Vandermeersch, G. R. Hutchison, ‘Open Babel: An open chemical toolbox’, J. Cheminf. 2010, 3, 33.