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Mini-Reviews in Medicinal Chemistry

Mini-Reviews in Medicinal Chemistry

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ISSN (Print): 1389-5575
ISSN (Online): 1875-5607

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Mini-Review Article

Insight in Quinazoline-based HDAC Inhibitors as Anti-cancer Agents

Author(s): Elena Martinoorcid of author, Shruti Thakur, Arun Kumar, Ashok Kumar Yadav, Donatella Boschiorcid of author, Deepak Kumar*orcid of author and Marco Lolliauthors OrcID

Volume 24, Issue 22, 2024

Published on: 07 June, 2024

Page: [1983 - 2007] Pages: 25

DOI: 10.2174/0113895575303614240527093106

Price: $65

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Abstract

Cancer remains a primary cause of death globally, and effective treatments are still limited. While chemotherapy has notably enhanced survival rates, it brings about numerous side effects. Consequently, the ongoing challenge persists in developing potent anti-cancer agents with minimal toxicity. The versatile nature of the quinazoline moiety has positioned it as a pivotal component in the development of various antitumor agents, showcasing its promising role in innovative cancer therapeutics. This concise review aims to reveal the potential of quinazolines in creating anticancer medications that target histone deacetylases (HDACs).

Keywords: Quinazoline, HDAC inhibitors, cancer, anti-proliferative agents, hybrid HDAC inhibitors, multitarget approach.

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Graphical Abstract

Graphical abstract illustrating key findings of the study

[1]
Kouzarides, T. Chromatin modifications and their function. Cell, 2007, 128(4), 693-705.
[http://dx.doi.org/10.1016/j.cell.2007.02.005] [PMID: 17320507]
[2]
Smalley, J.P.; Cowley, S.M.; Hodgkinson, J.T. Bifunctional HDAC therapeutics: One drug to rule them al. Molecules, 2020, 25(19), 4394.
[http://dx.doi.org/10.3390/molecules25194394] [PMID: 32987782]
[3]
Lin, Z.; Bishop, K.S.; Sutherland, H.; Marlow, G.; Murray, P.; Denny, W.A.; Ferguson, L.R. A quinazoline-based HDAC inhibitor affects gene expression pathways involved in cholesterol biosynthesis and mevalonate in prostate cancer cells. Mol. Biosyst., 2016, 12(3), 839-849.
[http://dx.doi.org/10.1039/C5MB00554J] [PMID: 26759180]
[4]
Gregoretti, I.; Lee, Y.M.; Goodson, H.V. Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis. J. Mol. Biol., 2004, 338(1), 17-31.
[http://dx.doi.org/10.1016/j.jmb.2004.02.006] [PMID: 15050820]
[5]
Aldana-Masangkay, G.I.; Sakamoto, K.M. The role of HDAC6 in cancer. J. Biomed. Biotechnol., 2011, 2011, 1-10.
[http://dx.doi.org/10.1155/2011/875824] [PMID: 21076528]
[6]
Glozak, M.A.; Seto, E. Histone deacetylases and cancer. Oncogene, 2007, 26(37), 5420-5432.
[http://dx.doi.org/10.1038/sj.onc.1210610] [PMID: 17694083]
[7]
Bieliauskas, A.V.; Pflum, M.K.H. Isoform-selective histone deacetylase inhibitors. Chem. Soc. Rev., 2008, 37(7), 1402-1413.
[http://dx.doi.org/10.1039/b703830p] [PMID: 18568166]
[8]
Hesham, H.M.; Lasheen, D.S.; Abouzid, K.A.M. Chimeric HDAC inhibitors: Comprehensive review on the HDAC‐based strategies developed to combat cancer. Med. Res. Rev., 2018, 38(6), 2058-2109.
[http://dx.doi.org/10.1002/med.21505] [PMID: 29733427]
[9]
Bolden, J.E.; Peart, M.J.; Johnstone, R.W. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov., 2006, 5(9), 769-784.
[http://dx.doi.org/10.1038/nrd2133] [PMID: 16955068]
[10]
Li, G.; Tian, Y.; Zhu, W.G. The roles of histone deacetylases and their inhibitors in cancer therapy. Front. Cell Dev. Biol., 2020, 8, 576946.
[http://dx.doi.org/10.3389/fcell.2020.576946] [PMID: 33117804]
[11]
Zhang, Q.; Li, Y.; Zhang, B.; Lu, B.; Li, J. Design, synthesis and biological evaluation of novel histone deacetylase inhibitors incorporating 4-aminoquinazolinyl systems as capping groups. Bioorg. Med. Chem. Lett., 2017, 27(21), 4885-4888.
[http://dx.doi.org/10.1016/j.bmcl.2017.09.036] [PMID: 28947154]
[12]
Yang, Z.; Wang, T.; Wang, F.; Niu, T.; Liu, Z.; Chen, X.; Long, C.; Tang, M.; Cao, D.; Wang, X.; Xiang, W.; Yi, Y.; Ma, L.; You, J.; Chen, L. Discovery of selective histone deacetylase 6 inhibitors using the quinazoline as the cap for the treatment of cancer. J. Med. Chem., 2016, 59(4), 1455-1470.
[http://dx.doi.org/10.1021/acs.jmedchem.5b01342] [PMID: 26443078]
[13]
Dhuguru, J.; Ghoneim, O.A. Quinazoline based HDAC dual inhibitors as potential anti-cancer agents. Molecules, 2022, 27(7), 2294.
[http://dx.doi.org/10.3390/molecules27072294] [PMID: 35408693]
[14]
Sun, L.; Han, L.; Zhang, L.; Chen, C.; Zheng, C. Design, synthesis, and antitumor activity evaluation of carbazole derivatives with potent HDAC inhibitory activity. Med. Chem. Res., 2023, 32(8), 1677-1689.
[http://dx.doi.org/10.1007/s00044-023-03084-0]
[15]
Liu, G.; Mondal, P.; Sang, N.; Li, Z.; Ding, W.; Yang, L.; Liu, Y.; Birar, V.C.; Gomm, A.; Tanzi, R.E.; Zhang, C.; Shen, S.; Wang, C.; Lu, X.; Bai, P. Design, synthesis, and anti-inflammatory activity characterization of novel brain-permeable HDAC6 inhibitors. Eur. J. Med. Chem., 2023, 254, 115327.
[http://dx.doi.org/10.1016/j.ejmech.2023.115327] [PMID: 37098307]
[16]
Zhao, Y.; Yao, Z.; Ren, W.; Yang, X.; Hou, X.; Cao, S.; Fang, H. Design, synthesis and bioactivity evaluations of 8-substituted-quinoline-2-carboxamide derivatives as novel histone deacetylase (HDAC) inhibitors. Bioorg. Med. Chem., 2023, 85, 117242.
[http://dx.doi.org/10.1016/j.bmc.2023.117242] [PMID: 37079967]
[17]
Xiong, S.; Wang, X.; Zhu, M.; Song, K.; Li, Y.; Yang, J.; Liu, X.; Liu, M.; Dong, H.; Chen, M.; Chen, D.; Xiang, H.; Luo, G. Structural optimization of tetrahydroisoquinoline-hydroxamate hybrids as potent dual ERα degraders and HDAC inhibitors. Bioorg. Chem., 2023, 134, 106459.
[http://dx.doi.org/10.1016/j.bioorg.2023.106459] [PMID: 36924653]
[18]
Zhao, M.; Yang, K.; Zhu, X.; Gao, T.; Yu, W.; Liu, H.; You, Z.; Liu, Z.; Qiao, X.; Song, Y. Design, synthesis and biological evaluation of dual Topo II/HDAC inhibitors bearing pyrimido[5,4-b]indole and pyrazolo[3,4-d]pyrimidine motifs. Eur. J. Med. Chem., 2023, 252, 115303.
[http://dx.doi.org/10.1016/j.ejmech.2023.115303] [PMID: 36996717]
[19]
Kong, S.J.; Nam, G.; Boggu, P.R.; Park, G.M.; Kang, J.E.; Park, H.J.; Jung, Y.H. Synthesis and biological evaluation of novel N-benzyltriazolyl-hydroxamate derivatives as selective histone deacetylase 6 inhibitors. Bioorg. Med. Chem., 2023, 79, 117154.
[http://dx.doi.org/10.1016/j.bmc.2023.117154] [PMID: 36645952]
[20]
Dong, J.; Zhu, X.; Yu, W.; Hu, X.; Zhang, Y.; Yang, K.; You, Z.; Liu, Z.; Qiao, X.; Song, Y. Pyrazolo[3,4-d]pyrimidine-based dual HDAC/Topo II inhibitors: Design, synthesis, and biological evaluation as potential antitumor agents. J. Mol. Struct., 2023, 1272, 134221.
[http://dx.doi.org/10.1016/j.molstruc.2022.134221]
[21]
Omidkhah, N.; Hadizadeh, F.; Zarghi, A.; Ghodsi, R. Synthesis, cytotoxicity, Pan-HDAC inhibitory activity and docking study of new N-(2-aminophenyl)-2-methylquinoline-4-carboxamide and (E)-N-(2-aminophenyl)-2-styrylquinoline-4-carboxamide derivatives as anticancer agents. Med. Chem. Res., 2023, 32(3), 506-524.
[http://dx.doi.org/10.1007/s00044-023-03018-w]
[22]
Moi, D.; Citarella, A.; Bonanni, D.; Pinzi, L.; Passarella, D.; Silvani, A.; Giannini, C.; Rastelli, G. Synthesis of potent and selective HDAC6 inhibitors led to unexpected opening of a quinazoline ring. RSC Advances, 2022, 12(18), 11548-11556.
[http://dx.doi.org/10.1039/D2RA01753A] [PMID: 35425078]
[23]
Bass, A.K.A.; El-Zoghbi, M.S.; Nageeb, E.S.M.; Mohamed, M.F.A.; Badr, M.; Abuo-Rahma, G.E.D.A. Comprehensive review for anticancer hybridized multitargeting HDAC inhibitors. Eur. J. Med. Chem., 2021, 209, 112904.
[http://dx.doi.org/10.1016/j.ejmech.2020.112904] [PMID: 33077264]
[24]
Undheim, K.; Benneche, T. Benneche, pyrimidines and their benzo derivatives. In: Comprehensive Heterocyclic Chemistry II.
[25]
Yao, D.; Li, C.; Jiang, J.; Huang, J.; Wang, J.; He, Z.; Zhang, J. Design, synthesis and biological evaluation of novel HDAC inhibitors with improved pharmacokinetic profile in breast cancer. Eur. J. Med. Chem., 2020, 205, 112648.
[http://dx.doi.org/10.1016/j.ejmech.2020.112648] [PMID: 32791401]
[26]
Chen, J.; Sang, Z.; Jiang, Y.; Yang, C.; He, L. Design, synthesis, and biological evaluation of quinazoline derivatives as dual HDAC 1 and HDAC 6 inhibitors for the treatment of cancer. Chem. Biol. Drug Des., 2019, 93(3), 232-241.
[http://dx.doi.org/10.1111/cbdd.13405] [PMID: 30251407]
[27]
Hieu, D.T.; Anh, D.T.; Hai, P.T.; Huong, L.T.T.; Park, E.J.; Choi, J.E.; Kang, J.S.; Dung, P.T.P.; Han, S.B.; Nam, N.H. Quinazoline‐based hydroxamic acids: Design, synthesis, and evaluation of histone deacetylase inhibitory effects and cytotoxicity. Chem. Biodivers., 2018, 15(6), e1800027.
[http://dx.doi.org/10.1002/cbdv.201800027] [PMID: 29667768]
[28]
Hieu, D.T.; Anh, D.T.; Tuan, N.M.; Hai, P.T.; Huong, L.T.T.; Kim, J.; Kang, J.S.; Vu, T.K.; Dung, P.T.P.; Han, S.B.; Nam, N.H.; Hoa, N.D. Design, synthesis and evaluation of novel N -hydroxybenzamides/ N -hydroxypropenamides incorporating quinazolin-4(3 H )-ones as histone deacetylase inhibitors and antitumor agents. Bioorg. Chem., 2018, 76, 258-267.
[http://dx.doi.org/10.1016/j.bioorg.2017.12.007] [PMID: 29223029]
[29]
Anh, D.T.; Hai, P.T.; Huy, L.D.; Ngoc, H.B.; Ngoc, T.T.M.; Dung, D.T.M.; Park, E.J.; Song, I.K.; Kang, J.S.; Kwon, J.H.; Tung, T.T.; Han, S.B.; Nam, N.H. Novel 4-oxoquinazoline-based N -hydroxypropenamides as histone deacetylase inhibitors: Design, synthesis, and biological evaluation. ACS Omega, 2021, 6(7), 4907-4920.
[http://dx.doi.org/10.1021/acsomega.0c05870] [PMID: 33644598]
[30]
Yu, C.W.; Chang, P.T.; Hsin, L.W.; Chern, J.W. Quinazolin-4-one derivatives as selective histone deacetylase-6 inhibitors for the treatment of Alzheimer’s disease. J. Med. Chem., 2013, 56(17), 6775-6791.
[http://dx.doi.org/10.1021/jm400564j] [PMID: 23905680]
[31]
Yu, C.W.; Hung, P.Y.; Yang, H.T.; Ho, Y.H.; Lai, H.Y.; Cheng, Y.S.; Chern, J.W. Quinazolin-2,4-dione-based hydroxamic acids as selective histone deacetylase-6 inhibitors for treatment of non-small cell lung cancer. J. Med. Chem., 2019, 62(2), 857-874.
[http://dx.doi.org/10.1021/acs.jmedchem.8b01590] [PMID: 30525585]
[32]
Du, Z.; Lovly, C.M. Mechanisms of receptor tyrosine kinase activation in cancer. Mol. Cancer, 2018, 17(1), 58.
[http://dx.doi.org/10.1186/s12943-018-0782-4] [PMID: 29455648]
[33]
Lohrisch, C.; Piccart, M. An overview of HER2. Semin. Oncol., 2001, 28(6)(Suppl. 18), 3-11.
[http://dx.doi.org/10.1016/S0093-7754(01)90103-4] [PMID: 11774200]
[34]
Wang, J.; Pursell, N.W.; Samson, M.E.S.; Atoyan, R.; Ma, A.W.; Selmi, A.; Xu, W.; Cai, X.; Voi, M.; Savagner, P.; Lai, C.J. Potential advantages of CUDC-101, a multitargeted HDAC, EGFR, and HER2 inhibitor, in treating drug resistance and preventing cancer cell migration and invasion. Mol. Cancer Ther., 2013, 12(6), 925-936.
[http://dx.doi.org/10.1158/1535-7163.MCT-12-1045] [PMID: 23536719]
[35]
Galloway, T.J.; Wirth, L.J.; Colevas, A.D.; Gilbert, J.; Bauman, J.E.; Saba, N.F.; Raben, D.; Mehra, R.; Ma, A.W.; Atoyan, R.; Wang, J.; Burtness, B.; Jimeno, A. A phase I study of CUDC-101, a multitarget inhibitor of HDACs, EGFR, and HER2, in combination with chemoradiation in patients with head and neck squamous cell carcinoma. Clin. Cancer Res., 2015, 21(7), 1566-1573.
[http://dx.doi.org/10.1158/1078-0432.CCR-14-2820] [PMID: 25573383]
[36]
Hynes, N.E.; Lane, H.A. ERBB receptors and cancer: The complexity of targeted inhibitors. Nat. Rev. Cancer, 2005, 5(5), 341-354.
[http://dx.doi.org/10.1038/nrc1609] [PMID: 15864276]
[37]
Bali, P.; Pranpat, M.; Swaby, R.; Fiskus, W.; Yamaguchi, H.; Balasis, M.; Rocha, K.; Wang, H.G.; Richon, V.; Bhalla, K. Activity of suberoylanilide hydroxamic Acid against human breast cancer cells with amplification of her-2. Clin. Cancer Res., 2005, 11(17), 6382-6389.
[http://dx.doi.org/10.1158/1078-0432.CCR-05-0344] [PMID: 16144943]
[38]
Zhang, X.; Su, M.; Chen, Y.; Li, J.; Lu, W. The design and synthesis of a new class of RTK/HDAC dual-targeted inhibitors. Molecules, 2013, 18(6), 6491-6503.
[http://dx.doi.org/10.3390/molecules18066491] [PMID: 23736786]
[39]
LaBonte, M.J.; Wilson, P.M.; Fazzone, W.; Russell, J.; Louie, S.G.; El-Khoueiry, A.; Lenz, H.J.; Ladner, R.D. The dual EGFR/HER2 inhibitor lapatinib synergistically enhances the antitumor activity of the histone deacetylase inhibitor panobinostat in colorectal cancer models. Cancer Res., 2011, 71(10), 3635-3648.
[http://dx.doi.org/10.1158/0008-5472.CAN-10-2430] [PMID: 21464044]
[40]
Poole, R.M. Belinostat: First global approval. Drugs, 2014, 74(13), 1543-1554.
[http://dx.doi.org/10.1007/s40265-014-0275-8] [PMID: 25134672]
[41]
Cai, X.; Zhai, H.X.; Wang, J.; Forrester, J.; Qu, H.; Yin, L.; Lai, C.J.; Bao, R.; Qian, C. Discovery of 7-(4(3-Ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide (CUDC-101) as a potent multi-acting HDAC, EGFR, and HER2 inhibitor for the treatment of cancer. J. Med. Chem., 2010, 53, 2000-2009.
[http://dx.doi.org/10.1021/jm901453q] [PMID: 20143778]
[42]
Stamos, J.; Sliwkowski, M.X.; Eigenbrot, C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem., 2002, 277(48), 46265-46272.
[http://dx.doi.org/10.1074/jbc.M207135200] [PMID: 12196540]
[43]
Wang, D.F.; Helquist, P.; Wiech, N.L.; Wiest, O. Toward selective histone deacetylase inhibitor design: homology modeling, docking studies, and molecular dynamics simulations of human class I histone deacetylases. J. Med. Chem., 2005, 48(22), 6936-6947.
[http://dx.doi.org/10.1021/jm0505011] [PMID: 16250652]
[44]
Kéri, G.; Orfi, L.; Eros, D.; Hegymegi-Barakonyi, B.; Szantai-Kis, C.; Horvath, Z.; Waczek, F.; Marosfalvi, J.; Szabadkai, I.; Pato, J.; Greff, Z.; Hafenbradl, D.; Daub, H.; Muller, G.; Klebl, B.; Ullrich, A. Signal transduction therapy with rationally designed kinase inhibitors. Curr. Signal Transduct. Ther., 2006, 1(1), 67-95.
[http://dx.doi.org/10.2174/157436206775269190]
[45]
Zhang, T.; Ma, D.; Wei, D.; Lu, T.; Yu, K.; Zhang, Z.; Wang, W.; Fang, Q.; Wang, J. CUDC-101 overcomes arsenic trioxide resistance via caspase-dependent promyelocytic leukemia-retinoic acid receptor alpha degradation in acute promyelocytic leukemia. Anticancer Drugs, 2020, 31(2), 158-168.
[http://dx.doi.org/10.1097/CAD.0000000000000847] [PMID: 31584454]
[46]
Ding, C.; Chen, S.; Zhang, C.; Hu, G.; Zhang, W.; Li, L.; Chen, Y.Z.; Tan, C.; Jiang, Y. Synthesis and investigation of novel 6-(1,2,3-triazol-4-yl)-4-aminoquinazolin derivatives possessing hydroxamic acid moiety for cancer therapy. Bioorg. Med. Chem., 2017, 25(1), 27-37.
[http://dx.doi.org/10.1016/j.bmc.2016.10.006] [PMID: 27769671]
[47]
Ding, C.; Li, D.; Wang, Y.W.; Han, S.S.; Gao, C.M.; Tan, C.Y.; Jiang, Y.Y. Discovery of ErbB/HDAC inhibitors by combining the core pharmacophores of HDAC inhibitor vorinostat and kinase inhibitors vandetanib, BMS-690514, neratinib, and TAK-285. Chin. Chem. Lett., 2017, 28(6), 1220-1227.
[http://dx.doi.org/10.1016/j.cclet.2017.01.003]
[48]
Zhao, L.; Fan, T.; Shi, Z.; Ding, C.; Zhang, C.; Yuan, Z.; Sun, Q.; Tan, C.; Chu, B.; Jiang, Y. Design, synthesis and evaluation of novel ErbB/HDAC multitargeted inhibitors with selectivity in EGFRT790M mutant cell lines. Eur. J. Med. Chem., 2021, 213, 113173.
[http://dx.doi.org/10.1016/j.ejmech.2021.113173] [PMID: 33493830]
[49]
van Meerbeeck, J.P.; Fennell, D.A.; De Ruysscher, D.K.M. Thelancet. Com, 2011, 378
[http://dx.doi.org/10.1016/S0140]
[50]
Ferrara, N.; Kerbel, R.S. Angiogenesis as a therapeutic target. Nature, 2005, 438(7070), 967-974.
[http://dx.doi.org/10.1038/nature04483] [PMID: 16355214]
[51]
Liotta, L.A.; Steeg, P.S.; Stetler-Stevenson, W.G. Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation. Cell, 1991, 64(2), 327-336.
[http://dx.doi.org/10.1016/0092-8674(91)90642-C] [PMID: 1703045]
[52]
Kiselyov, A.; Balakin, K.V.; Tkachenko, S.E. VEGF/VEGFR signalling as a target for inhibiting angiogenesis. Expert Opin. Investig. Drugs, 2007, 16(1), 83-107.
[http://dx.doi.org/10.1517/13543784.16.1.83] [PMID: 17155856]
[53]
Ellis, L.M.; Hicklin, D.J. VEGF-targeted therapy: Mechanisms of anti-tumour activity. Nat. Rev. Cancer, 2008, 8(8), 579-591.
[http://dx.doi.org/10.1038/nrc2403] [PMID: 18596824]
[54]
Ellis, L.M.; Hicklin, D.J. Pathways mediating resistance to vascular endothelial growth factor-targeted therapy. Clin. Cancer Res., 2008, 14(20), 6371-6375.
[http://dx.doi.org/10.1158/1078-0432.CCR-07-5287] [PMID: 18927275]
[55]
Curtin, M.L.; Frey, R.R.; Heyman, H.R.; Soni, N.B.; Marcotte, P.A.; Pease, L.J.; Glaser, K.B.; Magoc, T.J.; Tapang, P.; Albert, D.H.; Osterling, D.J.; Olson, A.M.; Bouska, J.J.; Guan, Z.; Preusser, L.C.; Polakowski, J.S.; Stewart, K.D.; Tse, C.; Davidsen, S.K.; Michaelides, M.R. Thienopyridine ureas as dual inhibitors of the VEGF and Aurora kinase families. Bioorg. Med. Chem. Lett., 2012, 22(9), 3208-3212.
[http://dx.doi.org/10.1016/j.bmcl.2012.03.035] [PMID: 22465635]
[56]
Nakagawa, T.; Matsushima, T.; Kawano, S.; Nakazawa, Y.; Kato, Y.; Adachi, Y.; Abe, T.; Semba, T.; Yokoi, A.; Matsui, J.; Tsuruoka, A.; Funahashi, Y. Lenvatinib in combination with golvatinib overcomes hepatocyte growth factor pathway‐induced resistance to vascular endothelial growth factor receptor inhibitor. Cancer Sci., 2014, 105(6), 723-730.
[http://dx.doi.org/10.1111/cas.12409] [PMID: 24689876]
[57]
Shi, L.; Wu, T.T.; Wang, Z.; Xue, J.Y.; Xu, Y.G. Discovery of quinazolin-4-amines bearing benzimidazole fragments as dual inhibitors of c-Met and VEGFR-2. Bioorg. Med. Chem., 2014, 22(17), 4735-4744.
[http://dx.doi.org/10.1016/j.bmc.2014.07.008] [PMID: 25082515]
[58]
Peng, F.W.; Xuan, J.; Wu, T.T.; Xue, J.Y.; Ren, Z.W.; Liu, D.K.; Wang, X.Q.; Chen, X.H.; Zhang, J.W.; Xu, Y.G.; Shi, L. Design, synthesis and biological evaluation of N-phenylquinazolin-4-amine hybrids as dual inhibitors of VEGFR-2 and HDAC. Eur. J. Med. Chem., 2016, 109, 1-12.
[http://dx.doi.org/10.1016/j.ejmech.2015.12.033] [PMID: 26741358]
[59]
Peng, F.W.; Wu, T.T.; Ren, Z.W.; Xue, J.Y.; Shi, L. Hybrids from 4-anilinoquinazoline and hydroxamic acid as dual inhibitors of vascular endothelial growth factor receptor-2 and histone deacetylase. Bioorg. Med. Chem. Lett., 2015, 25(22), 5137-5141.
[http://dx.doi.org/10.1016/j.bmcl.2015.10.006] [PMID: 26475519]
[60]
Commander, H.; Whiteside, G.; Perry, C. Vandetanib. Drugs, 2011, 71(10), 1355-1365.
[http://dx.doi.org/10.2165/11595310-000000000-00000] [PMID: 21770481]
[61]
Tachibana, M.; Ueda, J.; Fukuda, M.; Takeda, N.; Ohta, T.; Iwanari, H.; Sakihama, T.; Kodama, T.; Hamakubo, T.; Shinkai, Y. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes Dev., 2005, 19(7), 815-826.
[http://dx.doi.org/10.1101/gad.1284005] [PMID: 15774718]
[62]
Greer, E.L.; Shi, Y. Histone methylation: A dynamic mark in health, disease and inheritance. Nat. Rev. Genet., 2012, 13(5), 343-357.
[http://dx.doi.org/10.1038/nrg3173] [PMID: 22473383]
[63]
Hu, Y.; Zheng, Y.; Dai, M.; Wang, X.; Wu, J.; Yu, B.; Zhang, H.; Cui, Y.; Kong, W.; Wu, H.; Yu, X. G9a and histone deacetylases are crucial for Snail2‐mediated E‐cadherin repression and metastasis in hepatocellular carcinoma. Cancer Sci., 2019, 110(11), 3442-3452.
[http://dx.doi.org/10.1111/cas.14173] [PMID: 31432592]
[64]
Zheng, H.; Dai, Q.; Yuan, Z.; Fan, T.; Zhang, C.; Liu, Z.; Chu, B.; Sun, Q.; Chen, Y.; Jiang, Y. Quinazoline-based hydroxamic acid derivatives as dual histone methylation and deacetylation inhibitors for potential anticancer agents. Bioorg. Med. Chem., 2022, 53, 116524.
[http://dx.doi.org/10.1016/j.bmc.2021.116524] [PMID: 34847495]
[65]
Cantley, L.C. The phosphoinositide 3-kinase pathway. Science, 2002, 296(5573), 1655-1657.
[http://dx.doi.org/10.1126/science.296.5573.1655] [PMID: 12040186]
[66]
Vivanco, I.; Sawyers, C.L. The phosphatidylinositol 3-Kinase–AKT pathway in human cancer. Nat. Rev. Cancer, 2002, 2(7), 489-501.
[http://dx.doi.org/10.1038/nrc839] [PMID: 12094235]
[67]
Liu, P.; Cheng, H.; Roberts, T.M.; Zhao, J.J. Targeting the phosphoinositide 3-kinase pathway in cancer. Nat. Rev. Drug Discov., 2009, 8(8), 627-644.
[http://dx.doi.org/10.1038/nrd2926] [PMID: 19644473]
[68]
Millis, S.Z.; Ikeda, S.; Reddy, S.; Gatalica, Z.; Kurzrock, R. Landscape of phosphatidylinositol-3-kinase pathway alterations across 19 784 diverse solid tumors. JAMA Oncol., 2016, 2(12), 1565-1573.
[http://dx.doi.org/10.1001/jamaoncol.2016.0891] [PMID: 27388585]
[69]
Yoshioka, T.; Yogosawa, S.; Yamada, T.; Kitawaki, J.; Sakai, T. Combination of a novel HDAC inhibitor OBP-801/YM753 and a PI3K inhibitor LY294002 synergistically induces apoptosis in human endometrial carcinoma cells due to increase of Bim with accumulation of ROS. Gynecol. Oncol., 2013, 129(2), 425-432.
[http://dx.doi.org/10.1016/j.ygyno.2013.02.008] [PMID: 23403163]
[70]
Younes, A.; Berdeja, J.G.; Patel, M.R.; Flinn, I.; Gerecitano, J.F.; Neelapu, S.S.; Kelly, K.R.; Copeland, A.R.; Akins, A.; Clancy, M.S.; Gong, L.; Wang, J.; Ma, A.; Viner, J.L.; Oki, Y. Safety, tolerability, and preliminary activity of CUDC-907, a first-in-class, oral, dual inhibitor of HDAC and PI3K, in patients with relapsed or refractory lymphoma or multiple myeloma: an open-label, dose-escalation, phase 1 trial. Lancet Oncol., 2016, 17(5), 622-631.
[http://dx.doi.org/10.1016/S1470-2045(15)00584-7] [PMID: 27049457]
[71]
Qian, C.; Lai, C.J.; Bao, R.; Wang, D.G.; Wang, J.; Xu, G.X.; Atoyan, R.; Qu, H.; Yin, L.; Samson, M.; Zifcak, B.; Ma, A.W.S.; DellaRocca, S.; Borek, M.; Zhai, H.X.; Cai, X.; Voi, M. Cancer network disruption by a single molecule inhibitor targeting both histone deacetylase activity and phosphatidylinositol 3-kinase signaling. Clin. Cancer Res., 2012, 18(15), 4104-4113.
[http://dx.doi.org/10.1158/1078-0432.CCR-12-0055] [PMID: 22693356]
[72]
Zhang, K.; Lai, F.; Lin, S.; Ji, M.; Zhang, J.; Zhang, Y.; Jin, J.; Fu, R.; Wu, D.; Tian, H.; Xue, N.; Sheng, L.; Zou, X.; Li, Y.; Chen, X.; Xu, H. Design, synthesis, and biological evaluation of 4-Methyl quinazoline derivatives as anticancer agents simultaneously targeting phosphoinositide 3-kinases and histone deacetylases. J. Med. Chem., 2019, 62(15), 6992-7014.
[http://dx.doi.org/10.1021/acs.jmedchem.9b00390] [PMID: 31117517]
[73]
Thakur, A.; Tawa, G.J.; Henderson, M.J.; Danchik, C.; Liu, S.; Shah, P.; Wang, A.Q.; Dunn, G.; Kabir, M.; Padilha, E.C.; Xu, X.; Simeonov, A.; Kharbanda, S.; Stone, R.; Grewal, G. Design, synthesis, and biological evaluation of quinazolin-4-one-based hydroxamic acids as dual PI3K/HDAC inhibitors. J. Med. Chem., 2020, 63(8), 4256-4292.
[http://dx.doi.org/10.1021/acs.jmedchem.0c00193] [PMID: 32212730]
[74]
Bosshart, H.; Heinzelmann, M. THP-1 cells as a model for human monocytes. Ann. Transl. Med., 2016, 4(21), 438.
[http://dx.doi.org/10.21037/atm.2016.08.53] [PMID: 27942529]
[75]
Ramachandran, R.P.; Madhivanan, S.; Sundararajan, R.; Wan-Ying Lin, C.; Sankaranarayanan, K. An in vitro study of electroporation of leukemia and cervical cancer cells. In: Electroporation-Based Therapies for Cancer: From Basics to Clinical Applications; Elsevier, 2014; pp. 161-183.
[http://dx.doi.org/10.1533/9781908818294.161]
[76]
Bondarev, A.D.; Attwood, M.M.; Jonsson, J.; Chubarev, V.N.; Tarasov, V.V.; Schiöth, H.B. Recent developments of HDAC inhibitors: Emerging indications and novel molecules. Br. J. Clin. Pharmacol., 2021, 87(12), 4577-4597.
[http://dx.doi.org/10.1111/bcp.14889] [PMID: 33971031]
[77]
McClure, J.J.; Li, X.; Chou, C.J. Advances and challenges of HDAC inhibitors in cancer therapeutics. In: Adv Cancer Res; Academic Press Inc., 2018; pp. 183-211.
[http://dx.doi.org/10.1016/bs.acr.2018.02.006]

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