Salen-based bifunctional chemosensor for copper (II) ions: Inhibition of copper-induced amyloid-β aggregation
Tài liệu tham khảo
Multhaup, 1996, The amyloid precursor protein of Alzheimer’s disease in the reduction of copper(II) to copper(I), Science, 271, 1406, 10.1126/science.271.5254.1406
Ishida, 2013, Bioavailable copper modulates oxidative phosphorylation and growth of tumors, Proc. Natl. Acad. Sci. U.S.A., 110, 19507, 10.1073/pnas.1318431110
Reddi, 2013, SOD1 integrates signals from oxygen and glucose to repress respiration, Cell, 152, 224, 10.1016/j.cell.2012.11.046
Kohen, 1998, Enzyme Catalysis: beyond classical paradigms, Acc. Chem. Res., 31, 397, 10.1021/ar9701225
Heffern, 2016, In vivo bioluminescence imaging reveals copper deficiency in a murine model of nonalcoholic fatty liver disease, Proc. Natl. Acad. Sci. U.S.A., 113, 14219, 10.1073/pnas.1613628113
McCord, 1969, Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J. Biol. Chem., 244, 6049, 10.1016/S0021-9258(18)63504-5
Lee, 2016, Copper capture in a thioether-functionalized porous polymer applied to the detection of Wilson’s disease, J. Am. Chem. Soc., 138, 7603, 10.1021/jacs.6b02515
Brady, 2014, Copper is required for oncogenic BRAF signalling and tumorigenesis, Nature, 509, 492, 10.1038/nature13180
Kaler, 2011, ATP7A-related copper transport diseases-emerging concepts and future trends, Nat. Rev. Neurol., 7, 15, 10.1038/nrneurol.2010.180
Barnham, 2014, Biological metals and metal-targeting compounds in major neurodegenerative diseases, Chem. Soc. Rev., 43, 6727, 10.1039/C4CS00138A
Lovell, 1998, Copper, iron and zinc in Alzheimer’s disease senile plaques, J. Neurol. Sci., 158, 47, 10.1016/S0022-510X(98)00092-6
DeToma, 2012, Misfolded proteins in Alzheimer’s disease and type II diabetes, Chem. Soc. Rev., 41, 608, 10.1039/C1CS15112F
Beck, 2015, A rationally designed small molecule for identifying an in vivo link between metal–amyloid-β complexes and the pathogenesis of Alzheimer’s disease, Chem. Sci., 6, 1879, 10.1039/C4SC03239J
Barnham, 2004, Neurodegenerative diseases and oxidative stress, Nat. Rev. Drug Discov., 3, 205, 10.1038/nrd1330
Kepp, 2012, Bioinorganic chemistry of Alzheimer’s disease, Chem. Rev., 112, 5193, 10.1021/cr300009x
Savelieff, 2013, Untangling amyloid-beta, tau, and metals in Alzheimer’s disease, ACS Chem. Biol., 8, 856, 10.1021/cb400080f
Lee, 2014, Cholesterol and metal ions in Alzheimer’s disease, Chem. Soc. Rev., 43, 6672, 10.1039/C4CS00005F
Greenough, 2013, Metal dyshomeostasis and oxidative stress in Alzheimer’s disease, Neurochem. Int., 62, 540, 10.1016/j.neuint.2012.08.014
Young, 2014, An integrated study of the affinities of the Abeta16 peptide for Cu(I) and Cu(II): implications for the catalytic production of reactive oxygen species, Metallomics, 6, 505, 10.1039/C4MT00001C
Ayton, 2013, Metallostasis in Alzheimer’s disease, Free Radic. Biol. Med., 62, 76, 10.1016/j.freeradbiomed.2012.10.558
Crouch, 2007, The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer’s disease, FEBS J., 274, 3775, 10.1111/j.1742-4658.2007.05918.x
Ritchie, 2003, Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: a pilot phase 2 clinical trial, Arch. Neurol., 60, 1685, 10.1001/archneur.60.12.1685
Adlard, 2008, Rapid restoration of cognition in Alzheimer’s transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Abeta, Neuron, 59, 43, 10.1016/j.neuron.2008.06.018
Faux, 2010, PBT2 rapidly improves cognition in Alzheimer’s Disease: additional phase II analyses, J. Alzheimer’s Dis., 20, 509, 10.3233/JAD-2010-1390
Bandmann, 2015, Wilson’s disease and other neurological copper disorders, Lancet Neurol., 14, 103, 10.1016/S1474-4422(14)70190-5
Ala, 2007, Wilson’s disease, Lancet, 369, 397, 10.1016/S0140-6736(07)60196-2
Liang, 2015, PET neuroimaging studies of [18F]CABS13 in a double transgenic mouse model of Alzheimer’s disease and non-human primates, ACS Chem. Neurosci., 6, 535, 10.1021/acschemneuro.5b00055
Udhayakumari, 2017, Colorimetric and fluorescent chemosensors for Cu2+. A comprehensive review from the years 2013–15, Anal. Methods, 9, 552, 10.1039/C6AY02416E
Cai, 2019, Free-standing 2D nanorafts by assembly of 1D nanorods for biomolecule sensing, Nanoscale, 11, 12169, 10.1039/C9NR02636C
Ge, 2018, Core–shell HA-AuNPs@SiNPs nanoprobe for sensitive fluorescence hyaluronidase detection and cell imaging, ACS Sustain. Chem. Eng., 6, 16555, 10.1021/acssuschemeng.8b03684
Muthuraj, 2015, Multiple function fluorescein probe performs metal chelation, disaggregation, and modulation of aggregated Abeta and Abeta-Cu complex, ACS Chem. Neurosci., 6, 1880, 10.1021/acschemneuro.5b00205
Mergu, 2015, A novel colorimetric detection probe for copper(II) ions based on a Schiff base, Sens. Actuators B, 210, 408, 10.1016/j.snb.2014.12.130
Venkatesan, 2015, A turn-on fluorescent pyrene-based chemosensor for Cu(ii) with live cell application, RSC Adv., 5, 42591, 10.1039/C5RA05440K
Yadav, 2018, Dicarbohydrazide based chemosensors for copper and cyanide ions via a displacement approach, New J. Chem., 42, 6023, 10.1039/C8NJ00230D
WHO, 2008
You, 2015, A colorimetric sensor for the sequential detection of Cu2+ and CN- in fully aqueous media: practical performance of Cu2+, Dalon Trans, 44, 9120, 10.1039/C5DT00772K
Merle, 2007, Clinical presentation, diagnosis and long-term outcome of Wilson’s disease: a cohort study, Gut, 56, 115, 10.1136/gut.2005.087262
Kumawat, 2017, An easily accessible optical chemosensor for Cu2+ based on novel imidazoazine framework, its performance characteristics and potential applications, Sens. Actuators B, 240, 365, 10.1016/j.snb.2016.08.184
Zhang, 2016, A sensitive fluorescent probe for Cu2+ based on rhodamine B derivatives and its application to drinking water examination and living cells imaging, Sens. Actuators B, 225, 579, 10.1016/j.snb.2015.11.069
Jin, 2018, Dual-functional probe based on rhodamine for sequential Cu2+ and ATP detection in vivo, Spectrochim. Acta, Part A, 204, 657, 10.1016/j.saa.2018.06.094
Jiao, 2019, A highly selective and pH-tolerance fluorescent probe for Cu2+ based on a novel carbazole-rhodamine hybrid dye, Dyes Pigments, 160, 633, 10.1016/j.dyepig.2018.08.060
Jung, 2015, Efficient ensemble system based on the copper binding motif for highly sensitive and selective detection of cyanide ions in 100% aqueous solutions by fluorescent and colorimetric changes, Anal. Chem., 87, 9308, 10.1021/acs.analchem.5b01982
Ren, 2018, Spirohydrazine rhodamine as a fluorescent chemodosimeter for the selective detection of Cu(II) ions and its application in live cell imaging, Sens. Actuators B, 255, 2321, 10.1016/j.snb.2017.09.048
Gu, 2017, A benzothiazole-basedfluorescent probe for distinguishingand bioimaging of Hg2+ and Cu2+, Anal. Chim. Acta, 954, 97, 10.1016/j.aca.2016.11.044
Zhu, 2017, A novel ratiometric fluorescent probe for selective and sensitive detection of Cu2+ in complete aqueous solution, Sens. Actuators B, 252, 134, 10.1016/j.snb.2017.05.141
Yuan, 2015, Highly sensitive and selective turn-on fluorescent probes for Cu2+ based on rhodamine B, J. Mater. Chem. B, 3, 5261, 10.1039/C5TB00423C
Tang, 2019, A coumarin based fluorescent probe for rapidly distinguishing of hypochlorite and copper (II) ion in organisms, Spectrochim. Acta, Part A, 208, 299, 10.1016/j.saa.2018.10.019
Rangachari, 2007, Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate, Biochemistry, 46, 12451, 10.1021/bi701213s
Moore, 2009, Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers, Biochemistry, 48, 11796, 10.1021/bi901571t
Sharma, 2012, Bifunctional compounds for controlling metal-mediated aggregation of the abeta42 peptide, J. Am. Chem. Soc., 134, 6625, 10.1021/ja210588m
Zhang, 2013, Design and synthesis of curcumin analogues for in vivo fluorescence imaging and inhibiting copper-induced cross-linking of amyloid beta species in Alzheimer’s disease, J. Am. Chem. Soc., 135, 16397, 10.1021/ja405239v
Klug, 2003, Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH, Eur. J. Biochem., 270, 4282, 10.1046/j.1432-1033.2003.03815.x
Hindo, 2009, Small molecule modulators of copper-induced Abeta aggregation, J. Am. Chem. Soc., 131, 16663, 10.1021/ja907045h
Tew, 2008, Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer’s disease amyloid-beta peptide, Biophys. J., 94, 2752, 10.1529/biophysj.107.119909
Que, 2008, Metals in neurobiology: probing their chemistry and biology with molecular imaging, Chem. Rev., 108, 1517, 10.1021/cr078203u
Havranek, 2015, Intracerebroventricular oxytocin administration in rats enhances object recognition and increases expression of neurotrophins, microtubule-associated protein 2, and synapsin I, J. Neurosci. Res., 93, 893, 10.1002/jnr.23559
Iwata, 2005, A study of a dendritic marker, microtubule-associated protein 2 (MAP-2), in rats neonatally treated neurosteroids, pregnenolone and dehydroepiandrosterone (DHEA), Neurosci. Lett., 386, 145, 10.1016/j.neulet.2005.06.004
LeVine, 2009, Clioquinol and other hydroxyquinoline derivatives inhibit Abeta(1-42) oligomer assembly, Neurosci. Lett., 465, 99, 10.1016/j.neulet.2009.08.002
Derrick, 2015, A redox-active, compact molecule for cross-linking amyloidogenic peptides into nontoxic, off-pathway aggregates: in vitro and in vivo efficacy and molecular mechanisms, J. Am. Chem. Soc., 137, 14785, 10.1021/jacs.5b10043
Hobart, 2004, Anti-crosslinking properties of carnosine: significance of histidine, Life Sci., 75, 1379, 10.1016/j.lfs.2004.05.002