References
- Alzheimer's Association. Alzheimer's disease facts and figures. Alzheimers Dement 2020;16:391–460.
- Sengoku R. Aging and Alzheimer's disease pathology. Neuropathology 2020;40:22–9.
- Busche MA, Hyman BT. Synergy between amyloid-β and tau in Alzheimer's disease. Nat Neurosci 2020;23:1183–93.
- Arriagada PV, Growdon JH, Hedley-Whyte ET, et al. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 1992;42:631–9.
- Ingelsson M, Fukumoto H, Newell KL, et al. Early Abeta accumulation and progressive synaptic loss, gliosis, and tangle formation in AD brain. Neurology 2004;62:925–31.
- Scheltens P, Blennow K, Breteler MMB, et al. Alzheimer's disease. Lancet 2016;388:505–17.
- Ghosh AK, Osswald HL. BACE1 (β-secretase) inhibitors for the treatment of Alzheimer's disease. Chem Soc Rev 2014;43:6765–813.
- Rosini M, Simoni E, Milelli A, et al. Oxidative stress in Alzheimer's disease: are we connecting the dots? J Med Chem 2014;57:2821–31.
- Perry EK, Tomlinson BE, Blessed G, et al. Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia. Br Med J 1978;2:1457–9.
- Bartus RT. On neurodegenerative diseases, models, and treatment strategies: lessons learned and lessons forgotten a generation following the cholinergic hypothesis. Exp Neurol 2000;163:495–529.
- Massoulié J, Pezzementi L, Bon S, et al. Molecular and cellular biology of cholinesterases. Prog Neurobiol 1993;41:31–91.
- Mesulam MM, Geula C. Acetylcholinesterase-rich neurons of the human cerebral cortex: cytoarchitectonic and ontogenetic patterns of distribution. J Comp Neurol 1991;306:193–220.
- Kandiah N, Pai MC, Senanarong V, et al. Rivastigmine: the advantages of dual inhibition of acetylcholinesterase and butyrylcholinesterase and its role in subcortical vascular dementia and Parkinson's disease dementia. Clin Interv Aging 2017;12:697–707.
- Greig NH, Utsuki T, Ingram DK, et al. Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer beta-amyloid peptide in rodent. Proc Natl Acad Sci USA 2005;102:17213–8.
- Perry EK, Perry RH, Blessed G, et al. Changes in brain cholinesterases in senile dementia of Alzheimer type. Neuropathol Appl Neurobiol 1978;4:273–7.
- Mesulam MM, Guillozet A, Shaw P, et al. Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 2002;110:627–39.
- Nordberg A, Ballard C, Bullock R, et al. A review of butyrylcholinesterase as a therapeutic target in the treatment of Alzheimer’s disease. Prim Care Companion CNS Disord 2013;15:1–30.
- Hartmann J, Kiewert C, Duysen EG, et al. Excessive hippocampal acetylcholine levels in acetylcholinesterase-deficient mice are moderated by butyrylcholinesterase activity. J Neurochem 2007;100:1421–9.
- Furukawa-Hibi Y, Alkam T, Nitta A, et al. Butyrylcholinesterase inhibitors ameliorate cognitive dysfunction induced by amyloid-β peptide in mice. Behav Brain Res 2011;225:222–9.
- Maurice T, Strehaiano M, Siméon N, et al. Learning performances and vulnerability to amyloid toxicity in the butyrylcholinesterase knockout mouse. Behav Brain Res 2016;296:351–60.
- Ferreira-Vieira TH, Guimaraes IM, Silva FR, et al. Alzheimer's disease: targeting the cholinergic system. Curr Neuropharmacol 2016;14:101–15.
- Kumar V, Saha A, Roy K. In silico modeling for dual inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) enzymes in Alzheimer's disease. Comput Biol Chem 2020;88:107355.
- Bortolami M, Pandolfi F, De Vita D, et al. New deferiprone derivatives as multi-functional cholinesterase inhibitors: design, synthesis and in vitro evaluation. Eur J Med Chem 2020;198:112350.
- Xu M, Peng Y, Zhu L, et al. Triazole derivatives as inhibitors of Alzheimer's disease: current developments and structure-activity relationships. Eur J Med Chem 2019;180:656–72.
- Mesulam MM, Geula C. Butyrylcholinesterase reactivity differentiates the amyloid plaques of aging from those of dementia. Ann Neurol 1994;36:722–7.
- Guillozet AL, Smiley JF, Mash DC, et al. Butyrylcholinesterase in the life cycle of amyloid plaques. Ann Neurol 1997;42:909–18.
- Contestabile A. The history of the cholinergic hypothesis. Behav Brain Res 2011;221:334–40.
- Li Q, He S, Chen Y, et al. Donepezil-based multi-functional cholinesterase inhibitors for treatment of Alzheimer's disease. Eur J Med Chem 2018;158:463–77.
- Li Q, Xing S, Chen Y, et al. Discovery and biological evaluation of a novel highly potent selective butyrylcholinsterase inhibitor. J Med Chem 2020;63:10030–44.
- Li Q, Xing S, Chen Y, et al. Discovery and biological evaluation of a novel highly potent selective butyrylcholinsterase inhibitor. J Med Chem 2020;63:10030–44.
- Lotfi S, Rahmani T, Hatami M, et al. Design, synthesis and biological assessment of acridine derivatives containing 1,3,4-thiadiazole moiety as novel selective acetylcholinesterase inhibitors. Bioorg Chem 2020;105:104457.
- Wang C, Cai Z, Wang W, et al. Piperine attenuates cognitive impairment in an experimental mouse model of sporadic Alzheimer's disease. J Nutr Biochem 2019;70:147–55.
- Wang L, Cai X, Shi M, et al. Identification and optimization of piperine analogues as neuroprotective agents for the treatment of Parkinson's disease via the activation of Nrf2/keap1 pathway. Eur J Med Chem 2020;199:112385.
- Scott JD, Li SW, Brunskill AP, et al. Discovery of the 3-imino-1,2,4-thiadiazinane 1,1-dioxide derivative verubecestat (MK-8931)-A β-site amyloid precursor protein cleaving enzyme 1 inhibitor for the treatment of Alzheimer's disease. J Med Chem 2016;59:10435–50.
- Wu M, Ma J, Ji L, et al. Design, synthesis, and biological evaluation of rutacecarpine derivatives as multitarget-directed ligands for the treatment of Alzheimer's disease. Eur J Med Chem 2019;177:198–211.
- Prati F, Bottegoni G, Bolognesi ML, et al. BACE-1 inhibitors: from recent single-target molecules to multitarget compounds for Alzheimer's disease. J Med Chem 2018;61:619–37.
- Di Martino RMC, De Simone A, Andrisano V, et al. Versatility of the curcumin scaffold: discovery of potent and balanced dual BACE-1 and GSK-3β inhibitors. J Med Chem 2016;59:531–44.
- Dong J, Krasnova L, Finn MG, et al. Sulfur(VI) fluoride exchange (SuFEx): another good reaction for click chemistry. Angew Chem Int Ed Engl 2014;53:9430–48.
- Qin HL, Zheng Q, Bare GAL, et al. A Heck-Matsuda process for the synthesis of β-arylethenesulfonyl fluorides: selectively addressable Bis-electrophiles for SuFEx click chemistry. Angew Chem Int Ed Engl 2016;55:14155–8.
- Barrow AS, Smedley CJ, Zheng Q, et al. The growing applications of SuFEx click chemistry. Chem Soc Rev 2019;48:4731–58.
- Zhang X, Fang WY, Lekkala R, et al. An easy, general and practical method for the construction of alkyl sulfonyl fluorides. Adv Synth Catal 2020;362:3358–63.
- Gao B, Zhang L, Zheng Q, et al. Bifluoride-catalysed sulfur(VI) fluoride exchange reaction for the synthesis of polysulfates and polysulfonates. Nat Chem 2017;9:1083–8.
- Li Q, Chen Q, Klauser PC, et al. Developing covalent protein drugs via proximity-enabled reactive therapeutics. Cell 2020;182:85–97.
- Zha GF, Wang SM, Rakesh KP, et al. Discovery of novel arylethenesulfonyl fluorides as potential candidates against methicillin-resistant of Staphylococcus aureus (MRSA) for overcoming multidrug resistance of bacterial infections. Eur J Med Chem 2019;162:364–77.
- Zhang ZW, Wang SM, Fang WY, et al. Protocol for stereoselective construction of highly functionalized dienyl sulfonyl fluoride warheads. J Org Chem 2020;85:13721–34.
- Chen X, Zha GF, Wang JQ, et al. Ethenesulfonyl fluoride derivatives as telomerase inhibitors: structure-based design, SAR, and anticancer evaluation in vitro. J Enzyme Inhib Med Chem 2018;33:1266–70.
- Brouwer AJ, Herrero Álvarez N, Ciaffoni A, et al. Proteasome inhibition by new dual warhead containing peptido vinyl sulfonyl fluorides. Bioorg Med Chem 2016;24:3429–35.
- Fahrney DE, Gold AM. Sulfonyl fluorides as inhibitors of esterases. I. rates of reaction with acetylcholinesterase, α-chymotrypsin, and trypsin. J Am Chem Soc 1963;85:997–1000.
- Dighe SN, Deora GS, De la Mora E, et al. Discovery and structure-activity relationships of a highly selective butyrylcholinesterase inhibitor by structure-based virtual screening. J Med Chem 2016;59:7683–79.
- Qiu GL, He SS, Chen SC, et al. Design, synthesis and biological evaluation of tricyclic pyrazolo[1,5-C][1,3]benzoxazin-5(5h)-one scaffolds as selective buche inhibitors. J Enzyme Inhib Med Chem 2018;33:1506–15.
- Zhang ZW, Min JL, Chen MD, et al. The structure-based optimization of δ-sultone-fused pyrazoles as selective BuChE inhibitors. Eur J Med Chem 2020;201:112273.
- Park JW, Ha YM, Moon KM, et al. De novo tyrosinase inhibitor: 4-(6,7-dihydro-5h-indeno[5,6-D]thiazol-2-yl)benzene-1,3-diol (Mhy1556). Bioorg Med Chem Lett 2013;23:4172–6.
- Tada H, Shiho O, Kuroshima K, et al. An improved colorimetric assay for interleukin 2. J Immunol Methods 1986;93:157–65.
- Xu YY, Zhang ZW, Jiang X, et al. Discovery of δ-sultone-fused pyrazoles for treating alzheimer's disease: design, synthesis, biological evaluation and sar studies. Eur J Med Chem 2019;181:111598.
- Chen SC, Qiu GL, Li B, et al. Tricyclic pyrazolo[1,5-D][1,4]benzoxazepin-5(6h)-one scaffold derivatives: synthesis and biological evaluation as selective BuChE inhibitors. Eur J Med Chem 2018;147:194–204.
- Di L, Kerns EH, Fan K, et al. High throughput artificial membrane permeability assay for blood-brain barrier. Eur J Med Chem 2003;38:223–32.
- Dolles D, Hoffmann M, Gunesch S, et al. Structure-activity relationships and computational investigations into the development of potent and balanced dual-acting butyrylcholinesterase inhibitors and human cannabinoid receptor 2 ligands with pro-cognitive in vivo profiles. J Med Chem 2018;61:1646–63.
- Maurice T, Lockhart BP, Privat A. Amnesia induced in mice by centrally administered beta-amyloid peptides involves cholinergic dysfunction. Brain Res 1996;706:181–93.
- Lahmy V, Meunier J, Malmström S, et al. Blockade of Tau hyperphosphorylation and Aβ1−42 generation by the aminotetrahydrofuran derivative ANAVEX2-73, a mixed muscarinic and σ-receptor agonist, in a nontransgenic mouse model of Alzheimer's disease. Neuropsychopharmacology 2013;38:1706–23.
- Chen Y, Zhu J, Mo J, et al. Synthesis and bioevaluation of new tacrine-cinnamic acid hybrids as cholinesterase inhibitors against Alzheimer's disease. J Enzyme Inhib Med Chem 2018;33:290–302.
- Vorhees CV, Williams MT. Morris water maze: procedures for assessing spatial and related forms of learning and memory. Nat Protoc 2006;1:848–58.