Transition metal Ion interactions with disordered Amyloid-beta Peptides in the pathogenesis of Alzheimer's disease: insights from computational chemistry studies

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dc.contributor.authorStrodel, Birgit
dc.contributor.authorWeber, Orkide Coşkuner
dc.date.accessioned2021-01-08T21:51:22Z
dc.date.available2021-01-08T21:51:22Z
dc.date.issued2019
dc.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.descriptionCoskuner, Orkid/0000-0002-0772-9350; Strodel, Birgit/0000-0002-8734-7765en_US
dc.descriptionWOS:000469884900011en_US
dc.descriptionPubMed: 30933519en_US
dc.description.abstractMonomers and oligomers of the amyloid-beta peptide aggregate to form the fibrils found in the brains of Alzheimer's disease patients. These monomers and oligomers are largely disordered and can interact with transition metal ions, affecting the mechanism and kinetics of amyloid-beta aggregation. Due to the disordered nature of amyloid-beta, its rapid aggregation, as well as solvent and paramagnetic effects, experimental studies face challenges in the characterization of transition metal ions bound to amyloid-beta monomers and oligomers. The details of the coordination chemistry between transition metals and amyloid-beta obtained from experiments remain debated. Furthermore, the impact of transition metal ion binding on the monomeric or oligomeric amyloid-beta structures and dynamics are still poorly understood. Computational chemistry studies can serve as an important complement to experimental studies and can provide additional knowledge on the binding between amyloid-beta and transition metal ions. Many research groups conducted first-principles calculations, ab initio molecular dynamics simulations, quantum mechanics/classical mechanics simulations, and classical molecular dynamics simulations for studying the interplay between transition metal ions and amyloid-beta monomers and oligomers. This review summarizes the current understanding of transition metal interactions with amyloid-beta obtained from computational chemistry studies. We also emphasize the current view of the coordination chemistry between transition metal ions and amyloid-beta. This information represents an important foundation for future metal ion chelator and drug design studies aiming to combat Alzheimer's disease.
dc.identifier.doi10.1021/acs.jcim.8b00983
dc.identifier.endpage1805en_US
dc.identifier.issn1549-9596
dc.identifier.issn1549-960X
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85064984333
dc.identifier.scopusqualityQ1
dc.identifier.startpage1782en_US
dc.identifier.urihttp://doi.org/10.1021/acs.jcim.8b00983
dc.identifier.urihttps://hdl.handle.net/20.500.12846/192
dc.identifier.volume59en_US
dc.identifier.wosWOS:000469884900011
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorWeber, Orkide Coşkuner
dc.language.isoen
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal Of Chemical Information And Modeling
dc.relation.publicationcategoryother
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectAlzheimer's Diseaseen_US
dc.subjectAmyloid-Betaen_US
dc.subjectZincen_US
dc.subjectCopperen_US
dc.subjectIronen_US
dc.subjectDensity Functional Theoryen_US
dc.subjectQuantum Mechanics/Molecular Mechanicsen_US
dc.subjectAb Initio Molecular Dynamics Simulationsen_US
dc.subjectClassical Molecular Dynamics Simulationsen_US
dc.titleTransition metal Ion interactions with disordered Amyloid-beta Peptides in the pathogenesis of Alzheimer's disease: insights from computational chemistry studies
dc.typeReview Article

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