{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T01:48:08Z","timestamp":1791856088506,"version":"4.3.4"},"reference-count":235,"publisher":"SAGE Publications","issue":"s1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JAD"],"published-print":{"date-parts":[[2021,6,22]]},"abstract":"<jats:p>\u00a0Alzheimer\u2019s disease (AD) is the most common neurodegenerative disease affecting more than 50 million people worldwide. The pathology of this multifactorial disease is primarily characterized by the formation of amyloid-\u03b2 (A\u03b2) aggregates; however, other etiological factors including metal dyshomeostasis, specifically copper (Cu), zinc (Zn), and iron (Fe), play critical role in disease progression. Because these transition metal ions are important for cellular function, their imbalance can cause oxidative stress that leads to cellular death and eventual cognitive decay. Importantly, these transition metal ions can interact with the amyloid-\u03b2 protein precursor (A\u03b2PP) and A\u03b242 peptide, affecting A\u03b2 aggregation and increasing its neurotoxicity. Considering how metal dyshomeostasis may substantially contribute to AD, this review discusses polyphenols and the underlying chemical principles that may enable them to act as natural chelators. Furthermore, polyphenols have various therapeutic effects, including antioxidant activity, metal chelation, mitochondrial function, and anti-amyloidogenic activity. These combined therapeutic effects of polyphenols make them strong candidates for a moderate chelation-based therapy for AD.<\/jats:p>","DOI":"10.3233\/jad-200185","type":"journal-article","created":{"date-parts":[[2020,6,19]],"date-time":"2020-06-19T12:10:50Z","timestamp":1592568650000},"page":"S335-S357","source":"Crossref","is-referenced-by-count":172,"title":["Polyphenols as Potential Metal Chelation Compounds Against Alzheimer\u2019s Disease"],"prefix":"10.1177","volume":"82","author":[{"given":"Johant","family":"Lakey-Beitia","sequence":"first","affiliation":[{"name":"Centre for Biodiversity and Drug Discovery, Instituto de Investigaciones Cient\u00edficas y Servicios de Alta Tecnolog\u00eda (INDICASAT AIP), Clayton, City of Knowledge, Panama"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea M.","family":"Burillo","sequence":"additional","affiliation":[{"name":"Centre for Biodiversity and Drug Discovery, Instituto de Investigaciones Cient\u00edficas y 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binds copper ions","volume":"367","author":"Kong","year":"2007","journal-title":"J Mol Biol"},{"key":"10.3233\/JAD-200185_ref37","doi-asserted-by":"crossref","first-page":"183","DOI":"10.3233\/JAD-2011-110281","article-title":"Oxidative genome damage and its repair in neurodegenerative diseases: Function of transition metals as a double-edged sword","volume":"24","author":"Hegde","year":"2011","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-200185_ref38","doi-asserted-by":"crossref","first-page":"3751","DOI":"10.1074\/jbc.M116.754101","article-title":"Zinc and copper differentially modulate amyloid precursor protein processing by \u03b3-secretase and amyloid-\u03b2 peptide production","volume":"292","author":"Gerber","year":"2017","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-200185_ref39","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.freeradbiomed.2013.01.017","article-title":"Targeting dysregulation of brain iron homeostasis in Parkinson\u2019s 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novel curcumin derivative, guards dopamine neurons in MPTP model of Parkinson\u2019s disease","volume":"2014","author":"Jayaraj","year":"2014","journal-title":"Biomed Res Int"},{"key":"10.3233\/JAD-200185_ref49","doi-asserted-by":"crossref","first-page":"76","DOI":"10.2174\/138161212798919093","article-title":"Curcumin-glucoside, a novel synthetic derivative of curcumin, inhibits alpha-synuclein oligomer formation: Relevance to Parkinson\u2019s disease","volume":"18","author":"Gadad","year":"2012","journal-title":"Curr Pharm Des"},{"key":"10.3233\/JAD-200185_ref50","first-page":"2174","article-title":"Plant polyphenols as neuroprotective agents in Parkinson\u2019s disease targeting oxidative stress","volume":"20","author":"Hor","year":"2019","journal-title":"Curr Drug Targets"},{"key":"10.3233\/JAD-200185_ref51","doi-asserted-by":"crossref","first-page":"5385","DOI":"10.1007\/s12035-016-0048-3","article-title":"Comparative mitochondrial-based protective effects of resveratrol and nicotinamide in Huntington\u2019s disease models","volume":"54","author":"Naia","year":"2017","journal-title":"Mol Neurobiol"},{"key":"10.3233\/JAD-200185_ref52","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.expneurol.2011.08.014","article-title":"Neuroprotective and metabolic effects of resveratrol: Therapeutic implications for Huntington\u2019s disease and other neurodegenerative disorders","volume":"232","author":"Pasinetti","year":"2011","journal-title":"Exp Neurol"},{"key":"10.3233\/JAD-200185_ref53","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1002\/biof.1441","article-title":"Comparative binding of kaempferol and kaempferide on inhibiting the aggregate formation of mutant (G85R) SOD1 protein in familial amyotrophic lateral sclerosis: A quantum chemical and molecular mechanics 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\u2018metal-protein attenuating compounds\u2019 for the treatment of Alzheimer\u2019s disease: A proof-of-concept based on the study of the interactions between zinc (II) and pyridine-2-carboxaldehyde isonicotinoyl hydrazon","volume":"23","author":"Cukierman","year":"2018","journal-title":"J Biol Inorg Chem"},{"key":"10.3233\/JAD-200185_ref57","doi-asserted-by":"crossref","first-page":"719","DOI":"10.3390\/ijms20030719","article-title":"Novel approaches for the treatment of Alzheimer\u2019s and Parkinson\u2019s disease","volume":"20","author":"Van Bulck","year":"2019","journal-title":"Int J Mol Sci"},{"key":"10.3233\/JAD-200185_ref58","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/j.tips.2018.10.001","article-title":"Copper and zinc dysregulation in Alzheimer\u2019s disease","volume":"39","author":"Sensi","year":"2018","journal-title":"Trends Pharmacol Sci"},{"key":"10.3233\/JAD-200185_ref59","first-page":"31","volume-title":"Biological Inorganic Chemistry: Structure and Reactivity","author":"Bertini","year":"2007"},{"key":"10.3233\/JAD-200185_ref60","first-page":"1","author":"Crichton","year":"2018","journal-title":"Biological Inorganic Chemistry: A New Introduction to Molecular Structure and Function"},{"key":"10.3233\/JAD-200185_ref61","doi-asserted-by":"crossref","first-page":"4628","DOI":"10.1074\/jbc.R117.000176","article-title":"Copper signaling in the brain and beyond","volume":"293","author":"Ackerman","year":"2018","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-200185_ref62","doi-asserted-by":"crossref","first-page":"678","DOI":"10.3390\/biom4030678","article-title":"New perspectives on oxidized genome damage and repair inhibition by pro-oxidant metals in neurological diseases","volume":"4","author":"Mitra","year":"2014","journal-title":"Biomolecules"},{"key":"10.3233\/JAD-200185_ref63","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1021\/cr300009x","article-title":"Bioinorganic chemistry of Alzheimer\u2019s disease","volume":"112","author":"Kepp","year":"2012","journal-title":"Chem Rev"},{"key":"10.3233\/JAD-200185_ref64","doi-asserted-by":"crossref","first-page":"311","DOI":"10.2174\/156720506778249399","article-title":"Role of metals in neuronal apoptosis: Challenges associated with neurodegeneration","volume":"3","author":"Bharathi","year":"2006","journal-title":"Curr Alzheimer Res"},{"key":"10.3233\/JAD-200185_ref65","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3389\/fnins.2017.00003","article-title":"Metal dyshomeostasis and their pathological role in prion and prion-like diseases: The basis for a nutritional approach","volume":"11","author":"Toni","year":"2017","journal-title":"Front Neurosci"},{"key":"10.3233\/JAD-200185_ref66","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1039\/c1mt90005f","article-title":"Metals in neurodegenerative 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Divers"},{"key":"10.3233\/JAD-200185_ref89","doi-asserted-by":"crossref","first-page":"2164","DOI":"10.1016\/j.ccr.2012.03.037","article-title":"Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-\u03b2 peptides involved in Alzheimer disease. Part 1: An overview","volume":"256","author":"Hureau","year":"2012","journal-title":"Coord Chem Rev"},{"key":"10.3233\/JAD-200185_ref90","doi-asserted-by":"crossref","first-page":"S379","DOI":"10.3233\/JAD-179944","article-title":"Iron and Alzheimer\u2019s disease: An update on emerging mechanisms","volume":"64","author":"Lane","year":"2018","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-200185_ref91","first-page":"1070","volume-title":"Chemistry of the Elements","author":"Greenwood","year":"1997"},{"key":"10.3233\/JAD-200185_ref92","doi-asserted-by":"crossref","first-page":"2234","DOI":"10.1016\/j.ccr.2012.03.036","article-title":"Metal ions and protons compete for ligand atoms in disordered peptides: Examples from computer simulations of copper binding to the prion tandem repeat","volume":"256","author":"Furlan","year":"2012","journal-title":"Coord Chem 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Lett"},{"key":"10.3233\/JAD-200185_ref96","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1126\/science.271.5254.1406","article-title":"The amyloid precursor protein of Alzheimer\u2019s disease in the reduction of copper(II) to Copper(I)","volume":"271","author":"Multhaup","year":"1996","journal-title":"Science"},{"key":"10.3233\/JAD-200185_ref97","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/alzrt258","article-title":"Truncated and modified amyloid-beta species","volume":"6","author":"Kummer","year":"2014","journal-title":"Alzheimers Res Ther"},{"key":"10.3233\/JAD-200185_ref98","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/j.bbrc.2012.07.010","article-title":"Activation of \u03b1-secretase by curcumin-aminoacid conjugates","volume":"424","author":"Narasingapa","year":"2012","journal-title":"Biochem Biophys Res 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assembly","volume":"290","author":"Barritt","year":"2015","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-200185_ref105","doi-asserted-by":"crossref","first-page":"23223","DOI":"10.1074\/jbc.274.33.23223","article-title":"Aqueous dissolution of Alzheimer\u2019s disease A\u03b2 amyloid deposits by biometal depletion","volume":"274","author":"Cherny","year":"1999","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-200185_ref106","doi-asserted-by":"crossref","first-page":"17401","DOI":"10.1074\/jbc.M300629200","article-title":"Structure of the Alzheimer\u2019s disease amyloid precursor protein copper binding domain","volume":"278","author":"Barnham","year":"2003","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-200185_ref107","doi-asserted-by":"crossref","first-page":"9273","DOI":"10.1002\/anie.200904567","article-title":"Pulse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-\u03b2 Peptide: A key role of the first two N-terminus residues","volume":"48","author":"Dorlet","year":"2009","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.3233\/JAD-200185_ref108","doi-asserted-by":"crossref","first-page":"8760","DOI":"10.1021\/ja903669a","article-title":"Alanine-2 carbonyl is an oxygen ligand in Cu2+ coordination of Alzheimer\u2019s disease amyloid-\u03b2 peptide - relevance to N-terminally truncated forms","volume":"131","author":"Drew","year":"2009","journal-title":"J Am Chem Soc"},{"key":"10.3233\/JAD-200185_ref109","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1007\/s00249-005-0041-7","article-title":"Metal binding in amyloid \u03b2-peptides shows intra- and inter-peptide coordination modes","volume":"35","author":"Stellato","year":"2006","journal-title":"Eur Biophys J"},{"key":"10.3233\/JAD-200185_ref110","doi-asserted-by":"crossref","first-page":"10784","DOI":"10.1074\/jbc.M707109200","article-title":"Identifying the minimal copper- and zinc-binding site sequence in amyloid-\u03b2 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initio study","volume":"109","author":"Rickard","year":"2005","journal-title":"J Phys Chem A"},{"key":"10.3233\/JAD-200185_ref114","doi-asserted-by":"crossref","first-page":"16455","DOI":"10.1021\/jp410046w","article-title":"Identifying, by first-principles simulations, Cu[amyloid-\u03b2] species making fenton-type reactions in Alzheimer\u2019s disease","volume":"117","author":"La Penna","year":"2013","journal-title":"J Phys Chem B"},{"key":"10.3233\/JAD-200185_ref115","doi-asserted-by":"crossref","first-page":"5259","DOI":"10.1002\/chem.201704654","article-title":"Towards high-throughput modelling of copper reactivity induced by structural disorder in amyloid peptides","volume":"24","author":"La Penna","year":"2018","journal-title":"Chemistry"},{"key":"10.3233\/JAD-200185_ref116","doi-asserted-by":"crossref","first-page":"26952","DOI":"10.1074\/jbc.M111.220863","article-title":"Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-\u03b2 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One"},{"key":"10.3233\/JAD-200185_ref120","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1002\/ajmg.b.30087","article-title":"APOE and other loci affect age-at-onset in Alzheimer\u2019s disease families with PS2 mutation","volume":"132B","author":"Wijsman","year":"2005","journal-title":"Am J Med Genet B Neuropsychiatr Genet"},{"key":"10.3233\/JAD-200185_ref121","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/S1074-5521(96)90118-0","article-title":"Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides","volume":"3","author":"Ashburn","year":"1996","journal-title":"Chem Biol"},{"key":"10.3233\/JAD-200185_ref122","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.neulet.2007.09.042","article-title":"Anti-amyloidogenic activity of S-allyl-l-cysteine and its activity to destabilize Alzheimer\u2019s \u03b2-amyloid fibrils in vitro","volume":"429","author":"Gupta","year":"2007","journal-title":"Neurosci 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conformers","volume":"19","author":"Mitra","year":"2018","journal-title":"Chembiochem"},{"key":"10.3233\/JAD-200185_ref132","doi-asserted-by":"crossref","first-page":"16190","DOI":"10.1038\/s41598-018-33935-5","article-title":"Copper redox cycling inhibits a\u03b2 fibre formation and promotes fibre fragmentation, while generating a dityrosine A\u03b2 dimer","volume":"8","author":"Gu","year":"2018","journal-title":"Sci Rep"},{"key":"10.3233\/JAD-200185_ref133","doi-asserted-by":"crossref","first-page":"2317","DOI":"10.1080\/07391102.2015.1113890","article-title":"Zinc-induced heterodimer formation between metal-binding domains of intact and naturally modified amyloid-beta species: Implication to amyloid seeding in Alzheimer\u2019s disease?","volume":"34","author":"Mezentsev","year":"2016","journal-title":"J Biomol Struct Dyn"},{"key":"10.3233\/JAD-200185_ref134","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep21734","article-title":"Interplay of histidine residues of the Alzheimer\u2019s disease A\u03b2 peptide governs its Zn-induced oligomerization","volume":"6","author":"Istrate","year":"2016","journal-title":"Sci Rep"},{"key":"10.3233\/JAD-200185_ref135","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.3233\/JAD-2010-1338","article-title":"Trace copper(II) or zinc(II) ions drastically modify the aggregation behavior of Amyloid-\u03b21-42: An AFM study","volume":"19","author":"Innocenti","year":"2010","journal-title":"J Alzheimers Dis"},{"key":"10.3233\/JAD-200185_ref136","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ccr.2018.04.004","article-title":"An inorganic overview of natural A\u03b2 fragments: Copper(II) and zinc(II)-mediated pathways","volume":"369","author":"Lanza","year":"2018","journal-title":"Coord Chem Rev"},{"key":"10.3233\/JAD-200185_ref137","doi-asserted-by":"crossref","first-page":"4820","DOI":"10.1021\/cr900377t","article-title":"Polymorphism in Alzheimer A\u03b2 amyloid organization reflects conformational selection in a rugged energy landscape","volume":"110","author":"Miller","year":"2010","journal-title":"Chem Rev"},{"key":"10.3233\/JAD-200185_ref138","doi-asserted-by":"crossref","first-page":"9490","DOI":"10.1073\/pnas.0913114107","article-title":"Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states","volume":"107","author":"Miller","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3233\/JAD-200185_ref139","doi-asserted-by":"crossref","first-page":"7243","DOI":"10.1021\/acs.jpcb.8b03983","article-title":"Copper binding induces polymorphism in amyloid-\u03b2 peptide: Results of computational models","volume":"122","author":"Pham","year":"2018","journal-title":"J Phys Chem B"},{"key":"10.3233\/JAD-200185_ref140","doi-asserted-by":"crossref","first-page":"2871","DOI":"10.1016\/j.jmb.2014.05.015","article-title":"Factors influencing compact-extended structure equilibrium in oligomers of A\u03b21-40 peptide\u2014an ion 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