{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,18]],"date-time":"2026-10-18T02:56:28Z","timestamp":1792292188169,"version":"4.4.0"},"reference-count":118,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,10,1]],"date-time":"2023-10-01T00:00:00Z","timestamp":1696118400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100007724","name":"Wuhan University of Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007724","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22173070"],"award-info":[{"award-number":["22173070"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Advances in Colloid and Interface Science"],"published-print":{"date-parts":[[2023,10]]},"DOI":"10.1016\/j.cis.2023.103009","type":"journal-article","created":{"date-parts":[[2023,9,25]],"date-time":"2023-09-25T17:11:05Z","timestamp":1695661865000},"page":"103009","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"special_numbering":"C","title":["Metal ion mediated aggregation of Alzheimer's disease peptides and proteins in solutions and at surfaces"],"prefix":"10.1016","volume":"320","author":[{"given":"Jiahao","family":"Feng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yifei","family":"She","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chongjia","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lei","family":"Shen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cis.2023.103009_bb0005","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1152\/physrev.2001.81.2.741","article-title":"Alzheimer\u2019s disease: genes, proteins, and therapy","volume":"81","author":"Selkoe","year":"2001","journal-title":"Physiol Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0010","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1038\/nature02621","article-title":"Pathways towards and away from Alzheimer\u2019s disease","volume":"430","author":"Mattson","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.cis.2023.103009_bb0015","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1126\/science.1132814","article-title":"A century of Alzheimer\u2019s disease","volume":"314","author":"Goedert","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.cis.2023.103009_bb0020","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/s41593-022-01222-2","article-title":"Insights into Alzheimer\u2019s disease from single-cell genomic approaches","volume":"26","author":"Murdock","year":"2023","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0025","series-title":"The global impact of dementia \u2013 an analysis of prevalence, incidence, cost and trends","author":"World Alzheimer Report 2015","year":"2019"},{"key":"10.1016\/j.cis.2023.103009_bb0030","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1126\/science.1072994","article-title":"Medicine \u2013 the amyloid hypothesis of Alzheimer\u2019s disease: Progress and problems on the road to therapeutics","volume":"297","author":"Hardy","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.cis.2023.103009_bb0035","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1126\/science.1566067","article-title":"Alzheimers disease \u2013 the amyloid Cascade hypothesis","volume":"256","author":"Hardy","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.cis.2023.103009_bb0040","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1586\/14737175.6.5.711","article-title":"Metal homeostasis in Alzheimer\u2019s disease","volume":"6","author":"White","year":"2006","journal-title":"Exp Rev Neurotherap"},{"key":"10.1016\/j.cis.2023.103009_bb0045","doi-asserted-by":"crossref","first-page":"1995","DOI":"10.1021\/cr040410w","article-title":"Copper homeostasis and neurodegenerative disorders (Alzheimer\u2019s, prion, and Parkinson\u2019s diseases and amyotrophic lateral sclerosis)","volume":"106","author":"Gaggelli","year":"2006","journal-title":"Chem Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0050","doi-asserted-by":"crossref","first-page":"2271","DOI":"10.1016\/j.ccr.2012.05.003","article-title":"Metal ions and amyloid fiber formation in neurodegenerative disease. Copper, zinc and iron in Alzheimer\u2019s, Parkinson\u2019s and prion diseases","volume":"256","author":"Viles","year":"2012","journal-title":"Coord Chem Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0055","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.1039\/B813398K","article-title":"Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide","volume":"7","author":"Faller","year":"2009","journal-title":"Dalton Trans"},{"key":"10.1016\/j.cis.2023.103009_bb0060","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0022-510X(98)00092-6","article-title":"Copper, iron and zinc in Alzheimer\u2019s disease senile plaques","volume":"158","author":"Lovell","year":"1998","journal-title":"J Neurol Sci"},{"key":"10.1016\/j.cis.2023.103009_bb0065","doi-asserted-by":"crossref","first-page":"2768","DOI":"10.1021\/bi0272151","article-title":"Metal binding and oxidation of amyloid-\u03b2 within isolated senile plaque cores: Raman microscopic evidence","volume":"42","author":"Dong","year":"2003","journal-title":"Biochemistry."},{"key":"10.1016\/j.cis.2023.103009_bb0070","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jsb.2005.09.004","article-title":"Synchrotron-based infrared and X-ray imaging shows focalized accumulation of cu and Zn co-localized with \u03b2-amyloid deposites in Alzheimer\u2019s disease","volume":"155","author":"Miller","year":"2006","journal-title":"J Struct Biol"},{"key":"10.1016\/j.cis.2023.103009_bb0075","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/S0896-6273(01)00317-8","article-title":"Treatment with a copper-zinc chelator markedly and rapidly inhibits \u03b2-amyloid accumulation in Alzheimer\u2019s disease transgenic mice","volume":"30","author":"Cherny","year":"2001","journal-title":"Neuron."},{"key":"10.1016\/j.cis.2023.103009_bb0080","doi-asserted-by":"crossref","first-page":"6289","DOI":"10.1021\/bi3006169","article-title":"Copper and oxidative stress in the pathogenesis of Alzheimer\u2019s disease","volume":"51","author":"Eskici","year":"2012","journal-title":"Biochemistry."},{"key":"10.1016\/j.cis.2023.103009_bb0085","doi-asserted-by":"crossref","first-page":"5107","DOI":"10.1039\/C7SC00809K","article-title":"Identification of key structural features of the elusive cu- A\u03b2 complex that generates ROS in Alzheimer\u2019s disease","volume":"8","author":"Cheignon","year":"2017","journal-title":"Chem Sci"},{"key":"10.1016\/j.cis.2023.103009_bb0090","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":"10.1016\/j.cis.2023.103009_bb0095","doi-asserted-by":"crossref","first-page":"33444","DOI":"10.1038\/srep33444","article-title":"Copper(II) ions affect the gating dynamics of the 20S proteasome: a molecular and in cell study","volume":"6","author":"Santoro","year":"2019","journal-title":"Sci Rep"},{"key":"10.1016\/j.cis.2023.103009_bb0100","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1021\/acs.accounts.9b00248","article-title":"Metal ions in Alzheimer\u2019s disease: a key role or not?","volume":"52","author":"Liu","year":"2019","journal-title":"Acc Chem Res"},{"key":"10.1016\/j.cis.2023.103009_bb0105","doi-asserted-by":"crossref","first-page":"525","DOI":"10.2174\/0929867324666170518094404","article-title":"Repurposing of cooper(II)-chelating drugs for the treatment of neurodegenerative diseases","volume":"25","author":"Lanza","year":"2018","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0110","doi-asserted-by":"crossref","first-page":"3390","DOI":"10.1021\/ja1072178","article-title":"Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer\u2019s \u03b2 by solid-state NMR spectroscopy","volume":"133","author":"Parthasarathy","year":"2011","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cis.2023.103009_bb0115","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1021\/ja808073b","article-title":"Pleomorphic copper coordination by Alzheimer\u2019s disease amyloid-\u03b2 peptide","volume":"131","author":"Drew","year":"2009","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cis.2023.103009_bb0120","doi-asserted-by":"crossref","first-page":"9260","DOI":"10.1021\/ja046032u","article-title":"NMR reveals anomalous copper(II) binding to the amyloid a beta peptide of Alzheimer\u2019s disease","volume":"128","author":"Hou","year":"2006","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cis.2023.103009_bb0125","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1002\/anie.201005838","article-title":"Copper(II) coordination to amyloid \u03b2: murine versus human peptide","volume":"50","author":"Eury","year":"2011","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cis.2023.103009_bb0130","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1038\/nmat2442","article-title":"Understanding biophysicochemical interactions at the Nano-bio Interface","volume":"8","author":"Nel","year":"2009","journal-title":"Nat Mater"},{"key":"10.1016\/j.cis.2023.103009_bb0135","doi-asserted-by":"crossref","first-page":"w14021","DOI":"10.4414\/smw.2014.14021","article-title":"Toxic oligomer species of amyloid-\u03b2 in Alzheimer\u2019s disease, a timing issue","volume":"144","author":"Lesne","year":"2014","journal-title":"Swiss Med Wkly"},{"key":"10.1016\/j.cis.2023.103009_bb0140","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1111\/j.1471-4159.2010.07081.x","article-title":"Alpha-secretase in Alzheimer\u2019s disease: molecular identity, regulation and therapeutic potential","volume":"116","author":"Lichtenthaler","year":"2011","journal-title":"J Neurochem"},{"key":"10.1016\/j.cis.2023.103009_bb0145","first-page":"12787","article-title":"The \u03b2-secretase enzyme BACE in health and Alzheimer\u2019s disease: regulation, cell biology, function, and therapeutic potential","volume":"29","author":"Vassar","year":"2009","journal-title":"J Neurochem"},{"key":"10.1016\/j.cis.2023.103009_bb0150","doi-asserted-by":"crossref","first-page":"292","DOI":"10.15698\/cst2018.11.162","article-title":"Making the final cut: pathogenic amyloid-\u03b2 peptide generation by \u03b3-secretase","volume":"2","author":"Steiner","year":"2018","journal-title":"Cell Stress"},{"key":"10.1016\/j.cis.2023.103009_bb0155","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S1534-5807(02)00189-2","article-title":"Curtis, aph-1 and pen-2 are required for notch pathway signaling, gamma-secretase cleavage of beta APP, and presenilin protein accumulation","volume":"3","author":"Francis","year":"2002","journal-title":"Dev Cell"},{"key":"10.1016\/j.cis.2023.103009_bb0160","doi-asserted-by":"crossref","first-page":"29639","DOI":"10.1074\/jbc.R800016200","article-title":"Structural classification of toxic amyloid oligomers","volume":"283","author":"Glabe","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0165","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1074\/jbc.R800036200","article-title":"Amyloid \u03b2-protein assembly and Alzheimer disease","volume":"284","author":"Roychaudhuri","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0170","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu Rev Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0175","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer\u2019s amyloid \u03b2-peptide","volume":"8","author":"Haass","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.cis.2023.103009_bb0180","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.cis.2023.103009_bb0185","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature04533","article-title":"A specific amyloid-\u03b2 protein assembly in the brain impairs memory","volume":"440","author":"Lesn\u00e9","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.cis.2023.103009_bb0190","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1038\/416535a","article-title":"Naturally secreted oligomers of amyloid \u03b2 protein potently inhibit hippocampal long-term potentiation in vivo","volume":"416","author":"Walsh","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.cis.2023.103009_bb0195","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0006-8993(01)03058-X","article-title":"Soluble oligomers of \u03b2 amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus","volume":"924","author":"Wang","year":"2002","journal-title":"Brain Res"},{"key":"10.1016\/j.cis.2023.103009_bb0200","first-page":"167","article-title":"Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?","volume":"39","author":"Lashuel","year":"2006","journal-title":"Q Rev Biol"},{"key":"10.1016\/j.cis.2023.103009_bb0205","doi-asserted-by":"crossref","first-page":"5066","DOI":"10.3390\/molecules27165066","article-title":"A\u03b2 and tau interact with metal ions, lipid membranes and peptide-based amyloid inhibitors: are these common features relevant in Alzheimer\u2019s disease?","volume":"27","author":"Di Natale","year":"2022","journal-title":"Molecules"},{"issue":"10","key":"10.1016\/j.cis.2023.103009_bb0210","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1038\/s41593-020-0687-6","article-title":"Synergy between amyloid-\u03b2 and tau in Alzheimer\u2019s disease","volume":"23","author":"Busche","year":"2020","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0215","first-page":"247","article-title":"Metal ions affecting the neurological system","volume":"8","author":"Pohl","year":"2011","journal-title":"Met Ions Life Sci"},{"key":"10.1016\/j.cis.2023.103009_bb0220","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1002\/jnr.23143","article-title":"Copper signaling in the mammalian nervous system: synaptic effects","volume":"91","author":"Gaier","year":"2012","journal-title":"J Neurosci Res"},{"key":"10.1016\/j.cis.2023.103009_bb0225","doi-asserted-by":"crossref","first-page":"94","DOI":"10.2174\/1871527319666200303121016","article-title":"Oxidative stress in the pathogenesis of Alzheimer\u2019s disease and cerebrovascular disease with therapeutic implications","volume":"19","author":"Jurcau","year":"2020","journal-title":"CNS Neurol Disord Drug Targets"},{"key":"10.1016\/j.cis.2023.103009_bb0230","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.ccr.2011.07.012","article-title":"Copper(II) interaction with amyloid-\u03b2: affinity and speciation","volume":"256","author":"Arena","year":"2012","journal-title":"Coord Chem Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0235","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1021\/bi0620961","article-title":"Concentration dependent Cu2+ induced aggregation and dityrosine formation of the Alzheimer\u2019s disease amyloid-\u03b2 peptide","volume":"46","author":"Smith","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.cis.2023.103009_bb0240","doi-asserted-by":"crossref","first-page":"4033","DOI":"10.1002\/ange.200700318","article-title":"The aggregated state of amyloid-\u03b2 peptide in vitro depends on Cu2+ ion concentration","volume":"119","author":"Jun","year":"2007","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cis.2023.103009_bb0245","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":"10.1016\/j.cis.2023.103009_bb0250","doi-asserted-by":"crossref","first-page":"8914","DOI":"10.1074\/jbc.RA119.011955","article-title":"Copper stabilizes antiparallel \u03b2-sheet fibrils of the amyloid-\u03b240 (A\u03b240)-Iowa variant","volume":"295","author":"Crooks","year":"2020","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0255","doi-asserted-by":"crossref","first-page":"18169","DOI":"10.1074\/jbc.M313572200","article-title":"Copper binding to the amyloid-\u03b2 (A\u03b2) peptide associated with Alzheimer\u2019s disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of A\u03b2-(1\u201328): insights from a range of complementary spectroscopic techniques","volume":"279","author":"Syme","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0260","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0147488","article-title":"Effect of copper and zinc on the single molecule self-affinity of Alzheimer\u2019s amyloid-\u03b2 peptide","volume":"11","author":"Hane","year":"2016","journal-title":"PloS One"},{"key":"10.1016\/j.cis.2023.103009_bb0265","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/j.peptides.2005.09.002","article-title":"Copper binding properties of a tau peptide associated with Alzheimer\u2019s disease studied by CD, NMR, and MALDI-TOF MS","volume":"27","author":"Ma","year":"2006","journal-title":"Peptides"},{"key":"10.1016\/j.cis.2023.103009_bb0270","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/2047-9158-3-24","article-title":"Modulation of tau phosphorylation by environmental copper","volume":"3","author":"Voss","year":"2014","journal-title":"Trans Neurodegener"},{"key":"10.1016\/j.cis.2023.103009_bb0275","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1186\/s13195-021-00931-3","article-title":"For the K R G. Serum zinc levels and in vivo beta-amyloid deposition in the human brain","volume":"13","author":"Kim","year":"2021","journal-title":"Alzheimer\u2019s Res Ther"},{"key":"10.1016\/j.cis.2023.103009_bb0280","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1097\/NEN.0b013e3182417387","article-title":"Alteration of the cerebral zinc Pool in a mouse model of Alzheimer disease","volume":"71","author":"Lee","year":"2012","journal-title":"J Neuropath Exp Neuro"},{"key":"10.1016\/j.cis.2023.103009_bb0285","doi-asserted-by":"crossref","first-page":"e838","DOI":"10.1038\/tp.2016.83","article-title":"Obesity and age-related alterations in the gene expression of zinc-transporter proteins in the human brain","volume":"6","author":"Olesen","year":"2016","journal-title":"Transl Psychiatry"},{"key":"10.1016\/j.cis.2023.103009_bb0290","doi-asserted-by":"crossref","first-page":"10405","DOI":"10.1021\/ic9012334","article-title":"Metal loading capacity of A\u03b2 N-terminus: a combined potentiometric and spectroscopic study of zinc(II) complexes with A\u03b2(1-16), its short or mutated peptide fragments and its polyethylene glycolylated analogue","volume":"48","author":"Damante","year":"2009","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0295","doi-asserted-by":"crossref","first-page":"7225","DOI":"10.1074\/jbc.RA120.012738","article-title":"Metal ion coordination delays amyloid-\u03b2 peptide self-assembly by forming an aggregation-inert complex","volume":"295","author":"Wallin","year":"2020","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0300","doi-asserted-by":"crossref","first-page":"5342","DOI":"10.1021\/ic101537m","article-title":"Zn2+\u2019s ability to alter the distribution of Cu2+ among the available binding sites of A\u03b2(1-16)-polyethylenglycol-ylated peptide: implications in Alzheimer\u2019s disease","volume":"50","author":"Damante","year":"2011","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0305","first-page":"1058","article-title":"Bimodal modulation of tau protein phosphorylation and conformation by extracellular Zn2+ in human-tau transfected cells","volume":"2009","author":"Boom","year":"1793","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"10.1016\/j.cis.2023.103009_bb0310","doi-asserted-by":"crossref","first-page":"34648","DOI":"10.1074\/jbc.M109.058883","article-title":"Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322","volume":"284","author":"Mo","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0315","doi-asserted-by":"crossref","first-page":"e91","DOI":"10.1038\/cddis.2010.73","article-title":"Dietary zinc supplementation of 3xTg-AD mice increases BDNF levels and prevents cognitive deficits as well as mitochondrial dysfunction","volume":"1","author":"Corona","year":"2010","journal-title":"Cell Death Dis"},{"key":"10.1016\/j.cis.2023.103009_bb0320","doi-asserted-by":"crossref","first-page":"4248","DOI":"10.1074\/jbc.M110.158980","article-title":"Iron promotes the toxicity of amyloid \u03b2 peptide by impeding its ordered aggregation","volume":"286","author":"Liu","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0325","doi-asserted-by":"crossref","first-page":"994","DOI":"10.3390\/ijms20040994","article-title":"Targeting the iron-response elements of the mRNAs for the Alzheimer\u2019s amyloid precursor protein and ferritin to treat acute lead and manganese neurotoxicity","volume":"20","author":"Rogers","year":"2019","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.cis.2023.103009_bb0330","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1006\/nbdi.2000.0364","article-title":"Lysosomal membrane damage in soluble A\u03b2-mediated cell death in Alzheimer\u2019s disease","volume":"8","author":"Ditaranto","year":"2001","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.cis.2023.103009_bb0335","doi-asserted-by":"crossref","first-page":"6865","DOI":"10.1021\/ic201069v","article-title":"Exploring the reactions of \u03b2-amyloid (A\u03b2) peptide 1\u201328 with AlIII and FeIII ions","volume":"50","author":"Valensin","year":"2011","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0340","doi-asserted-by":"crossref","first-page":"9024","DOI":"10.1021\/ic201233b","article-title":"Iron (II) binding to amyloid-\u03b2, the Alzheimer\u2019s peptide","volume":"50","author":"Bousejra-ElGarah","year":"2011","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0345","doi-asserted-by":"crossref","first-page":"9646","DOI":"10.1074\/jbc.M110.177246","article-title":"Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-\u03b2 stability, oligomerization, and aggregation","volume":"286","author":"Chen","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0350","doi-asserted-by":"crossref","first-page":"5328","DOI":"10.1021\/bi800012e","article-title":"Influence of multiple metal ions on \u03b2-amyloid aggregation and dissociation on a solid surface","volume":"47","author":"Ryu","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.cis.2023.103009_bb0355","doi-asserted-by":"crossref","first-page":"2247","DOI":"10.1093\/jn\/nxz168","article-title":"High dietary Iron disrupts Iron homeostasis and induces amyloid-\u03b2 and Phospho-\u03c4 expression in the Hippocampus of adult wild-type and APP\/PS1 transgenic mice","volume":"149","author":"Chen","year":"2019","journal-title":"J Nutr"},{"key":"10.1016\/j.cis.2023.103009_bb0360","doi-asserted-by":"crossref","first-page":"753","DOI":"10.3233\/JAD-200551","article-title":"The Iron Chelator Deferiprone improves the phenotype in a mouse model of Tauopathy","volume":"77","author":"Rao","year":"2020","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.cis.2023.103009_bb0365","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.neuint.2012.12.005","article-title":"Deferoxamine inhibits iron induced hippocampal tau phosphorylation in the Alzheimer transgenic mouse brain","volume":"62","author":"Guo","year":"2013","journal-title":"Neurochem In"},{"key":"10.1016\/j.cis.2023.103009_bb0370","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1046\/j.1471-4159.2002.t01-1-01061.x","article-title":"Iron (III) induces aggregation of hyperphosphorylated \u03c4 and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer\u2019s disease","volume":"82","author":"Yamamoto","year":"2002","journal-title":"J Neurochem"},{"key":"10.1016\/j.cis.2023.103009_bb0375","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S0166-2236(03)00067-5","article-title":"The Metallobiology of Alzheimer\u2019s disease","volume":"26","author":"Bush","year":"2003","journal-title":"Trends Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0380","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1007\/s10534-005-5918-5","article-title":"Chronological changes in tissue copper, zinc and iron in the toxic milk mouse and effects of copper loading","volume":"19","author":"Allen","year":"2006","journal-title":"Biometals"},{"key":"10.1016\/j.cis.2023.103009_bb0385","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1038\/nature08300","article-title":"Metalloproteins and metal sensing","volume":"460","author":"Waldron","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.cis.2023.103009_bb0390","doi-asserted-by":"crossref","first-page":"43","DOI":"10.3389\/fnins.2019.00043","article-title":"The role of NMDA receptors in Alzheimer\u2019s disease","volume":"13","author":"Liu","year":"2019","journal-title":"Front Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0395","doi-asserted-by":"crossref","first-page":"475","DOI":"10.2174\/187152709789824606","article-title":"Glutamate receptors as therapeutic targets for Parkinsons disease","volume":"8","author":"Johnson","year":"2009","journal-title":"CNS Neurol Disorder"},{"issue":"5961","key":"10.1016\/j.cis.2023.103009_bb0400","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/308734a0","article-title":"Release of endogenous Zn2+ from brain tissue during activity","volume":"308","author":"Assaf","year":"1984","journal-title":"Nature"},{"key":"10.1016\/j.cis.2023.103009_bb0405","doi-asserted-by":"crossref","first-page":"2890","DOI":"10.1523\/JNEUROSCI.5093-08.2009","article-title":"Synaptically released zinc triggers metabotropic signaling via a zinc-sensing receptor in the Hippocampus","volume":"29","author":"Besser","year":"2009","journal-title":"J Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0410","doi-asserted-by":"crossref","first-page":"15749","DOI":"10.1073\/pnas.1512296112","article-title":"AMPA receptor inhibition by synaptically released zinc","volume":"112","author":"Kalappa","year":"2015","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.cis.2023.103009_bb0415","doi-asserted-by":"crossref","first-page":"879","DOI":"10.3233\/JAD-2009-1010","article-title":"Iron toxicity in diseases of aging: Alzheimer\u2019s disease, Parkinson\u2019s disease and atherosclerosis","volume":"16","author":"Altamura","year":"2009","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.cis.2023.103009_bb0420","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.jinorgbio.2011.10.017","article-title":"The inorganic perspectives of neurotrophins and Alzheimer\u2019s disease","volume":"111","author":"Travaglia","year":"2012","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cis.2023.103009_bb0425","doi-asserted-by":"crossref","first-page":"5085","DOI":"10.3390\/ijms22105085","article-title":"Nerve growth factor peptides bind copper(II) with high affinity: a thermodynamic approach to unveil overlooked neurotrophin roles","volume":"22","author":"Magr\u00ec","year":"2021","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.cis.2023.103009_bb0430","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1016\/j.neuroscience.2006.08.054","article-title":"Metallothionein-I and -III expression in animal models of Alzheimer disease","volume":"143","author":"Carrasco","year":"2006","journal-title":"Neurosci."},{"key":"10.1016\/j.cis.2023.103009_bb0435","doi-asserted-by":"crossref","first-page":"9142","DOI":"10.1523\/JNEUROSCI.1447-18.2018","article-title":"The divalent metal transporer 1 (DMT1) is required for iron uptake and normal development of oligodendrocyte progenitor cells","volume":"38","author":"Cheli","year":"2018","journal-title":"J Neurosci"},{"key":"10.1016\/j.cis.2023.103009_bb0440","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/S0021-9673(00)96090-4","article-title":"Differential interactions of peptides and proteins surface structures with free metal ions and surface-immobilized metal ions","volume":"500","author":"Hutchens","year":"1990","journal-title":"J Chromatogr"},{"key":"10.1016\/j.cis.2023.103009_bb0445","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.bpc.2010.02.014","article-title":"Influence of the hydrophobic interface and transition metal ions on the conformation of amyloidogenic model peptides","volume":"150","author":"Hoernke","year":"2010","journal-title":"Biophys Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0450","doi-asserted-by":"crossref","first-page":"2225","DOI":"10.1002\/cphc.201100215","article-title":"Amyloidogenic peptides at hydrophobic-hydrophilic interfaces: coordination affinities and the chelate effect dictate the competitive binding of Cu2+ and Zn2+","volume":"12","author":"Hoernke","year":"2011","journal-title":"ChemPhysChem"},{"key":"10.1016\/j.cis.2023.103009_bb0455","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1128\/AEM.65.3.1092-1098.1999","article-title":"Enhanced bioaccumulation of heavy metal ions by bacterial cells due to surface display of short metal binding peptides","volume":"65","author":"Kotrba","year":"1999","journal-title":"Appl Environ Microbiol"},{"key":"10.1016\/j.cis.2023.103009_bb0460","first-page":"3135","article-title":"Cholesterol and clioquinol modulation of A\u03b2(1-42) interaction with phospholipid bilayers and metals","volume":"2007","author":"Lau","year":"1768","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.cis.2023.103009_bb0465","doi-asserted-by":"crossref","first-page":"105085","DOI":"10.1016\/j.chemphyslip.2021.105085","article-title":"Tau\/A\u03b2 chimera peptides: a thioflavin-T and MALDI-TOF study of A\u03b2 amyloidosis in the presence of Cu(II) or Zn(II) ions and total lipid brain extract (TLBE) vesicles","volume":"237","author":"Sciacca","year":"2021","journal-title":"Chem Phys Lipids"},{"key":"10.1016\/j.cis.2023.103009_bb0470","doi-asserted-by":"crossref","first-page":"110996","DOI":"10.1016\/j.jinorgbio.2020.110996","article-title":"Tau\/A\u03b2 chimera peptides: evaluating the dual function of metal coordination and membrane interaction on one sequence","volume":"205","author":"Sciacca","year":"2020","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cis.2023.103009_bb0475","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1002\/cbic.200700656","article-title":"How metal ions affect amyloid formation: Cu2+\u2212 and Zn2+\u2212sensitive peptides","volume":"9","author":"Pagel","year":"2008","journal-title":"ChemBioChem"},{"key":"10.1016\/j.cis.2023.103009_bb0480","doi-asserted-by":"crossref","first-page":"13313","DOI":"10.1073\/pnas.0702669104","article-title":"Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity","volume":"104","author":"Dong","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.cis.2023.103009_bb0485","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1515\/pac-2018-1017","article-title":"Mechanism of amyloid protein aggregation and the role of inhibitors","volume":"91","author":"Sara","year":"2019","journal-title":"Pure Appl Chem"},{"key":"10.1016\/j.cis.2023.103009_bb0490","doi-asserted-by":"crossref","first-page":"9758","DOI":"10.1073\/pnas.1218402110","article-title":"Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism","volume":"110","author":"Cohen","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.cis.2023.103009_bb0495","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1021\/acs.langmuir.1c02322","article-title":"Effect of surface-chelated Cu2+ on amyloid-\u03b2 peptide fibrillation","volume":"38","author":"Wen","year":"2022","journal-title":"Langmuir"},{"key":"10.1016\/j.cis.2023.103009_bb0500","doi-asserted-by":"crossref","first-page":"93","DOI":"10.3390\/ph12020093","article-title":"Cellular senescence and Iron Dyshomeostasis in Alzheimer\u2019s disease","volume":"12","author":"Masaldan","year":"2019","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.cis.2023.103009_bb0505","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1124\/pr.57.4.2","article-title":"The evolution of Iron chelators for the treatment of Iron overload disease and Cancer","volume":"57","author":"Kalinowski","year":"2005","journal-title":"Pharmacol Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0510","doi-asserted-by":"crossref","first-page":"101716","DOI":"10.1016\/j.pneurobio.2019.101716","article-title":"Revisiting the intersection of amyloid, pathologically modified tau and iron in Alzheimer\u2019s disease from a ferroptosis perspective","volume":"184","author":"Derry","year":"2020","journal-title":"Prog Neurobiol"},{"key":"10.1016\/j.cis.2023.103009_bb0515","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.jtemb.2014.10.001","article-title":"Chelation in metal intoxication\u2014principles and paradigms","volume":"31","author":"Aaseth","year":"2015","journal-title":"J Trace Elem Med Biol"},{"key":"10.1016\/j.cis.2023.103009_bb0520","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1067\/mhj.2000.107548","article-title":"Chelation therapy for coronary heart disease: an overview of all clinical investigations","volume":"140","author":"Ernst","year":"2000","journal-title":"Am Heart J"},{"key":"10.1016\/j.cis.2023.103009_bb0525","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1517\/13543784.13.12.1585","article-title":"Metal-protein attenuating compounds and Alzheimer\u2019s disease","volume":"13","author":"Ritchie","year":"2005","journal-title":"Expert Opin Investig Drugs"},{"key":"10.1016\/j.cis.2023.103009_bb0530","doi-asserted-by":"crossref","DOI":"10.1002\/14651858.CD005380.pub4","article-title":"Metal protein attenuating compounds for the treatment of Alzheimer\u2019s dementia","volume":"5","author":"Sampson","year":"2012","journal-title":"Cochrane Database Syst Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0535","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1016\/j.jinorgbio.2010.08.014","article-title":"Hydroxyquinoline based binders: promising ligands for chelatotherapy?","volume":"105","author":"Budimir","year":"2011","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cis.2023.103009_bb0540","doi-asserted-by":"crossref","first-page":"494","DOI":"10.2174\/1567205011310050005","article-title":"Efficacy and toxicity of Clioquinol treatment and A-beta42 inoculation in the APP\/PSI mouse model of Alzheimer\u2019s disease","volume":"10","author":"Zhang","year":"2013","journal-title":"Curr Alzheimer Res"},{"key":"10.1016\/j.cis.2023.103009_bb0545","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.neuron.2008.06.018","article-title":"Rapid restoration of cognition in Alzheimer\u2019s transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial A\u03b2","volume":"59","author":"Adlard","year":"2008","journal-title":"Neuron"},{"key":"10.1016\/j.cis.2023.103009_bb0550","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ccr.2017.06.004","article-title":"The double faced role of copper in A\u03b2 homeostasis: a survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration","volume":"347","author":"Grasso","year":"2017","journal-title":"Coord Chem Rev"},{"key":"10.1016\/j.cis.2023.103009_bb0555","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/S1474-4422(08)70167-4","article-title":"Safety, efficacy, and biomarker findings of PBT2 in targeting A\u03b2 as a modifying therapy for Alzheimer\u2019s disease: a phase IIa, double-blind, randomised, placebo-controlled trial","volume":"7","author":"Lannfelt","year":"2008","journal-title":"Lancet Neurol"},{"key":"10.1016\/j.cis.2023.103009_bb0560","doi-asserted-by":"crossref","first-page":"81","DOI":"10.2174\/187152712799960709","article-title":"Nanoparticle delivery of transition-metal chelators to the brain: oxidative stress will never see it coming!","volume":"11","author":"Bonda","year":"2012","journal-title":"CNS Neurol Disord Drug Targets"},{"key":"10.1016\/j.cis.2023.103009_bb0565","first-page":"246","article-title":"Nanoparticle and other metal chelation therapeutics in Alzheimer disease","volume":"2005","author":"Liu","year":"1741","journal-title":"Biochim Biophys Acta Mol Basis Dis"},{"key":"10.1016\/j.cis.2023.103009_bb0570","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1016\/j.progpolymsci.2007.05.014","article-title":"Nanomedicine in the diagnosis and therapy of neurodegenerative disorders","volume":"32","author":"Kabanov","year":"2007","journal-title":"Prog Polym Sci"},{"key":"10.1016\/j.cis.2023.103009_bb0575","doi-asserted-by":"crossref","first-page":"2177","DOI":"10.1039\/B919237A","article-title":"Minding metals: tailoring multifunctional chelating agents for neurodegenerative disease","volume":"39","author":"Perez","year":"2010","journal-title":"Dalton Trans"},{"key":"10.1016\/j.cis.2023.103009_bb0580","doi-asserted-by":"crossref","first-page":"3075","DOI":"10.1007\/s11095-012-0770-0","article-title":"Surface-engineered nanoliposomes by chelating ligands for modulating the neurotoxicity associated with \u03b2-amyloid aggregates of Alzheimer\u2019s disease","volume":"29","author":"Mufamadi","year":"2012","journal-title":"Pharm Res"},{"key":"10.1016\/j.cis.2023.103009_bb0585","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.neulet.2006.07.020","article-title":"Nanoparticle iron chelators: a new therapeutic approach in Alzheimer disease and other neurologic disorders associated with trace metal imbalance","volume":"406","author":"Liu","year":"2006","journal-title":"Neurosci Lett"},{"key":"10.1016\/j.cis.2023.103009_bb0590","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41531-019-0105-5","article-title":"Emerging regenerative medicine and tissue engineering strategies for Parkinson\u2019s disease","volume":"6","author":"Harris","year":"2020","journal-title":"NPJ Parkinsons Dis"}],"container-title":["Advances in Colloid and Interface Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0001868623001768?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0001868623001768?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,11]],"date-time":"2025-09-11T01:52:42Z","timestamp":1757555562000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0001868623001768"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,10]]},"references-count":118,"alternative-id":["S0001868623001768"],"URL":"https:\/\/doi.org\/10.1016\/j.cis.2023.103009","relation":{},"ISSN":["0001-8686"],"issn-type":[{"value":"0001-8686","type":"print"}],"subject":[],"published":{"date-parts":[[2023,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Metal ion mediated aggregation of Alzheimer's disease peptides and proteins in solutions and at surfaces","name":"articletitle","label":"Article Title"},{"value":"Advances in Colloid and Interface Science","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cis.2023.103009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"103009"}}