Tiềm năng của 4-ary-6-morpholino-3(2H)-pyridazinone-2-arylpiperazinylacetamide như một khung mới cho sự ức chế SIRT2: phương pháp in silico được hướng dẫn bởi lập bản đồ pharmacophore và docking phân tử

Du J, Jiang H, Lin H. Investigating the ADP-ribosyltransferase activity of Sirtuins with NAD Analogues and 32P-NAD. Biochemistry. 2009;48:2878–90. https://doi.org/10.1021/bi802093g. Jiang H, Khan S, Wang Y, Charron G, He B, Sebastian C, et al. SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature. 2013;496:110–3. https://doi.org/10.1038/nature12038. Du J, Zhou Y, Su X, Yu JJ, Khan S, Jiang H, et al. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 2011;334:806. https://doi.org/10.1126/science.1207861. Sauve AA, Wolberger C, Schramm VL, Boeke JD. The biochemistry of sirtuins. Annu Rev Biochem 2006;75:435–65. https://doi.org/10.1146/annurev.biochem.74.082803.133500. North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The Human Sir2 Ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003;11:437–44. https://doi.org/10.1016/S1097-2765(03)00038-8. Zhang L, Kim S, Ren X. The clinical significance of SIRT2 in malignancies: a tumor suppressor or an oncogene? Front Oncol. 2020;10:1721. https://doi.org/10.3389/fonc.2020.01721. Zhao Y, Wang L, Yang J, Zhang P, Ma K, Zhou J, et al. Anti-neoplastic activity of the cytosolic FoxO1 results from autophagic cell death. Autophagy. 2010;6:988–90. https://doi.org/10.4161/auto.6.7.13289. Xu Y, Li F, Lv L, Li T, Zhou X, Deng C-X, et al. Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase. Cancer Res. 2014;74:3630. https://doi.org/10.1158/0008-5472.CAN-13-3615. Zhang H, Park S-H, Pantazides BG, Karpiuk O, Warren MD, Hardy CW, et al. SIRT2 directs the replication stress response through CDK9 deacetylation. Proc Natl Acad Sci USA. 2013;110:13546. https://doi.org/10.1073/pnas.1301463110. Beirowski B, Gustin J, Armour SM, Yamamoto H, Viader A, North BJ, et al. Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling. Proc Natl Acad Sci USA. 2011;108:E952. https://doi.org/10.1073/pnas.1104969108. Wang Y-P, Zhou L-S, Zhao Y-Z, Wang S-W, Chen L-L, Liu L-X, et al. Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress. EMBO J. 2014;33:1304–20. https://doi.org/10.1002/embj.201387224. Lagunas-Rangel FA. Current role of mammalian sirtuins in DNA repair. DNA Repair. 2019;80:85–92. https://doi.org/10.1016/j.dnarep.2019.06.009. Ng F, Tang BL. Sirtuins’ modulation of autophagy. J Cell Physiol. 2013;228:2262–70. https://doi.org/10.1002/jcp.24399. Seung Min J, Haigis MC. Sirtuins in cancer: a balancing act between genome stability and metabolism. Mol Cells. 2015;38:750–8. https://doi.org/10.14348/molcells.2015.0167. Carafa V, Rotili D, Forgione M, Cuomo F, Serretiello E, Hailu GS, et al. Sirtuin functions and modulation: from chemistry to the clinic. Clin Epigenetics. 2016;8:61. https://doi.org/10.1186/s13148-016-0224-3. Zhang Y, Anoopkumar-Dukie S, Arora D, Davey AK. Review of the anti-inflammatory effect of SIRT1 and SIRT2 modulators on neurodegenerative diseases. Eur J Pharmacol. 2020;867:172847. https://doi.org/10.1016/j.ejphar.2019.172847. Jing H, Hu J, He B, Negrón Abril YL, Stupinski J, Weiser K, et al. A SIRT2-selective inhibitor Promotes c-Myc oncoprotein degradation and exhibits broad anticancer activity. Cancer Cell. 2016;29:297–310. https://doi.org/10.1016/j.ccell.2016.02.007. Shah AA, Ito A, Nakata A, Yoshida M. Identification of a selective SIRT2 inhibitor and its anti-breast cancer activity. Biol Pharm Bull. 2016;39:1739–42. https://doi.org/10.1248/bpb.b16-00520. Moniot S, Forgione M, Lucidi A, Hailu GS, Nebbioso A, Carafa V, et al. Development of 1,2,4-oxadiazoles as potent and selective inhibitors of the human deacetylase sirtuin 2: structure–activity relationship, x-ray crystal structure, and anticancer activity. J Med Chem. 2017;60:2344–60. https://doi.org/10.1021/acs.jmedchem.6b01609. Rumpf T, Schiedel M, Karaman B, Roessler C, North BJ, Lehotzky A, et al. Selective Sirt2 inhibition by ligand-induced rearrangement of the active site. Nat Commun. 2015;6:6263. https://doi.org/10.1038/ncomms7263. Quinti L, Casale M, Moniot S, Pais Teresa F, Van Kanegan Michael J, Kaltenbach Linda S, et al. SIRT2- and NRF2-targeting thiazole-containing compound with therapeutic activity in huntington’s disease models. Cell Chem Biol. 2016;23:849–61. https://doi.org/10.1016/j.chembiol.2016.05.015. Outeiro TF, Kontopoulos E, Altmann SM, Kufareva I, Strathearn KE, Amore AM, et al. Sirtuin 2 inhibitors rescue α-Synuclein-mediated toxicity in models of parkinson’s disease. Science. 2007;317:516–9. https://doi.org/10.1126/science.1143780. Taylor DM, Balabadra U, Xiang Z, Woodman B, Meade S, Amore A, et al. A brain-permeable small molecule reduces neuronal cholesterol by inhibiting activity of sirtuin 2 deacetylase. ACS Chem Biol. 2011;6:540–6. https://doi.org/10.1021/cb100376q. Ai T, Wilson DJ, More SS, Xie J, Chen L. 5-((3-Amidobenzyl)oxy)nicotinamides as sirtuin 2 inhibitors. J Med Chem. 2016;59:2928–41. https://doi.org/10.1021/acs.jmedchem.5b01376. Seifert T, Malo M, Kokkola T, Engen K, Fridén-Saxin M, Wallén EAA, et al. Chroman-4-one- and chromone-based sirtuin 2 inhibitors with antiproliferative properties in cancer cells. J Med Chem. 2014;57:9870–88. https://doi.org/10.1021/jm500930h. Wang L, Li C, Chen W, Song C, Zhang X, Yang F, et al. Discovery of (5-phenylfuran-2-yl)methanamine derivatives as new human sirtuin 2 inhibitors. Molecules. 2019;24:2724. https://doi.org/10.3390/molecules24152724. Radwan MO, Ciftci HI, Ali TFS, Koga R, Tateishi H, Nakata A, et al. Structure activity study of S-trityl-cysteamine dimethylaminopyridine derivatives as SIRT2 inhibitors: Improvement of SIRT2 binding and inhibition. Bioorg Med Chem Lett. 2020;30:127458. https://doi.org/10.1016/j.bmcl.2020.127458. Khalil NA, Ahmed EM, Zaher AF, El-Zoghbi MS, Sobh EA. Synthesis of certain benzothieno[3,2-d]pyrimidine derivatives as a selective SIRT2 inhibitors. Eur J Med Chem. 2020;187:111926. https://doi.org/10.1016/j.ejmech.2019.111926. Eren G, Bruno A, Guntekin-Ergun S, Cetin-Atalay R, Ozgencil F, Ozkan Y, et al. Pharmacophore modeling and virtual screening studies to identify novel selective SIRT2 inhibitors. J Mol Graph Model. 2019;89:60–73. https://doi.org/10.1016/j.jmgm.2019.02.014. Yagci S, Gozelle M, Kaya SG, Ozkan Y, Aksel AB, Bakar-Ates F, et al. Hit-to-lead optimization on aryloxybenzamide derivative virtual screening hit against SIRT. Bioorg Med Chem. 2021;30:115961. https://doi.org/10.1016/j.bmc.2020.115961. Akhtar W, Shaquiquzzaman M, Akhter M, Verma G, Khan MF, Alam MM. The therapeutic journey of pyridazinone. Eur J Med Chem. 2016;123:256–81. https://doi.org/10.1016/j.ejmech.2016.07.061. Süküroglu M, Küpeli E, Banoglu E, Ünlü S, Yesilada E, Sahin MF. Synthesis and analgesic activity of some 4,6-disubstituted-3(2h)-pyridazinone derivatives. Arzneimittelforschung. 2006;56:337–45. https://doi.org/10.1055/s-0031-1296731. Ochiai K, Takita S, Eiraku T, Kojima A, Iwase K, Kishi T, et al. Phosphodiesterase inhibitors. Part 3: Design, synthesis and structure–activity relationships of dual PDE3/4-inhibitory fused bicyclic heteroaromatic-dihydropyridazinones with anti-inflammatory and bronchodilatory activity. Bioorg Med Chem. 2012;20:1644–58. https://doi.org/10.1016/j.bmc.2012.01.033. Abouzid K, Bekhit SA. Novel anti-inflammatory agents based on pyridazinone scaffold; design, synthesis and in vivo activity. Bioorg Med Chem. 2008;16:5547–56. https://doi.org/10.1016/j.bmc.2008.04.007. Sharma D, Bansal R. Synthesis of 2-substituted-4-aryl-6-phenylpyridazin-3(2H)-ones as potential anti-inflammatory and analgesic agents with cardioprotective and ulcerogenic sparing effects. Med Chem Res. 2016;25:1574–89. https://doi.org/10.1007/s00044-016-1588-9. Asano T, Yamazaki H, Kasahara C, Kubota H, Kontani T, Harayama Y, et al. Identification, Synthesis, and biological evaluation of 6-[(6R)-2-(4-fluorophenyl)-6-(hydroxymethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidin-3-yl]-2-(2-methylphenyl)pyridazin-3(2H)-one (AS1940477), a potent p38 MAP Kinase inhibitor. J Med Chem. 2012;55:7772–85. https://doi.org/10.1021/jm3008008. Yue Q, Zhao Y, Hai L, Zhang T, Guo L, Wu Y. First synthesis of novel 3,3′-bipyridazine derivatives as new potent antihepatocellular carcinoma agents. Tetrahedron. 2015;71:7670–5. https://doi.org/10.1016/j.tet.2015.07.063. Zhou S, Liao H, He C, Dou Y, Jiang M, Ren L, et al. Design, synthesis and structure–activity relationships of novel 4-phenoxyquinoline derivatives containing pyridazinone moiety as potential antitumor agents. Eur J Med Chem. 2014;83:581–93. https://doi.org/10.1016/j.ejmech.2014.06.068. Csókás D, Zupkó I, Károlyi BI, Drahos L, Holczbauer T, Palló A, et al. Synthesis, spectroscopy, X-ray analysis and in vitro antiproliferative effect of ferrocenylmethylene-hydrazinylpyridazin-3(2H)-ones and related ferroceno[d]pyridazin-1(2H)-ones. J Organomet Chem. 2013;743:130–8. https://doi.org/10.1016/j.jorganchem.2013.06.040. Al-Tel TH. Design and synthesis of novel tetrahydro-2H-pyrano[3,2-c]pyridazin-3(6H)-one derivatives as potential anticancer agents. Eur J Med Chem. 2010;45:5724–31. https://doi.org/10.1016/j.ejmech.2010.09.029. Zimmerman G, Soreq H. Termination and beyond: acetylcholinesterase as a modulator of synaptic transmission. Cell Tissue Res. 2006;326:655–69. https://doi.org/10.1007/s00441-006-0239-8. Lin H, Fang H, Wang J, Meng Q, Dai X, Wu S, et al. Discovery of a novel 2,3,11,11a-tetrahydro-1H-pyrazino[1,2-b]isoquinoline-1,4(6H)-dione series promoting neurogenesis of human neural progenitor cells. Bioorg Med Chem Lett. 2015;25:3748–53. https://doi.org/10.1016/j.bmcl.2015.05.084. Boukharsa Y, Meddah B, Tiendrebeogo RY, Ibrahimi A, Taoufik J, Cherrah Y, et al. Synthesis and antidepressant activity of 5-(benzo[b]furan-2-ylmethyl)-6-methylpyridazin-3(2H)-one derivatives. Med Chem Res. 2016;25:494–500. https://doi.org/10.1007/s00044-015-1490-x. Schiedel M, Rumpf T, Karaman B, Lehotzky A, Oláh J, Gerhardt S, et al. Aminothiazoles as potent and selective Sirt2 inhibitors: a structure–activity relationship study. J Med Chem. 2016;59:1599–612. https://doi.org/10.1021/acs.jmedchem.5b01517. Fagbohun OF, Olawoye B, Ademakinwa AN, Oriyomi OV, Fagbohun OS, Fadare OA, et al. UHPLC/GC-TOF-MS metabolomics, MTT assay, and molecular docking studies reveal physostigmine as a new anticancer agent from the ethyl acetate and butanol fractions of Kigelia africana (Lam.) Benth. fruit extracts. Biomed Chromatogr. 2021;35:e4979. https://doi.org/10.1002/bmc.4979. Fagbohun OF, Oriyomi OV, Adekola MB, Msagati TAM. Biochemical applications of Kigelia africana (Lam.) Benth. fruit extracts in diabetes mellitus. Comp Clin Path. 2020;29:1251–64. https://doi.org/10.1007/s00580-020-03179-9. Friesner RA, Murphy RB, Repasky MP, Frye LL, Greenwood JR, Halgren TA, et al. Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein−ligand complexes. J Med Chem. 2006;49:6177–96. https://doi.org/10.1021/jm051256o.