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dc.contributor.authorCoşkuner Weber, Orkide
dc.date.accessioned2021-01-08T21:51:32Z
dc.date.available2021-01-08T21:51:32Z
dc.date.issued2018
dc.identifier.issn2149-0120
dc.identifier.urihttps://doi.org/10.18596/jotcsa.424144
dc.identifier.urihttps://hdl.handle.net/20.500.12846/340
dc.description.abstractMetal ions and intrinsically disordered peptides amyloid-?40 and amyloid-?42 are at the center of Alzheimer´s disease pathology. Divalent copper ion binds to amyloid-?40 and amyloid-?42 peptides with varying coordination chemistries. Experiments face challenges in the measurements of divalent copper ion bound monomeric amyloid-?40 and amyloid-?42 in an aqueous solution medium because of fast conformational changes, rapid aggregation processes and solvent effects. Theoretical studies complement experiments and provide insights at the atomic and molecular levels with dynamics. However, until recently, potential functions for simulating divalent copper ion bound amyloid-?40 and amyloid-?42 peptides with varying coordination chemistries were lacking. Using new potential functions that were developed for divalent copper centers, Cu(II), including three histidine residues and an oxygen-ligated amino acid residue, the structures and thermodynamic properties of Cu(II)-bound amyloid-?40 and amyloid-?42 peptides in an aqueous solution medium were studied. For these purposes, extensive first principles calculations and replica exchange molecular dynamics simulations were conducted. In this study, the secondary and tertiary structural properties, conformational Gibbs free energy values, potential of mean force surfaces, salt bridges and aggregation propensities of aqueous Cu(II)-bound amyloid-?40 and amyloid-?42 peptides are presented. Different than previous findings in the literature, results clearly show that the coordination chemistry variations impact the structural and thermodynamic properties of divalent Cu(II) bound amyloid-? alloforms in water. Specificities about these differences are revealed in this study at the atomic level with dynamics. Results presented herein are the first to offer a comparison of the monomeric Cu(II)-bound amyloid-?40 and amyloid-?42 peptides with varying coordination chemistries using bonded model potential functions. © 2018, Turkish Chemical Society. All rights reserved.en_US
dc.language.isoengen_US
dc.publisherTurkish Chemical Societyen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAlzheimer´s diseaseen_US
dc.subjectAmyloid-?en_US
dc.subjectCoordination chemistryen_US
dc.subjectCopperen_US
dc.subjectReplica exchange molecular dynamics simulationsen_US
dc.titleRevisiting cu(II) bound amyloid-?40 and amyloid-?42 peptides: varying coordination chemistriesen_US
dc.typearticleen_US
dc.relation.journalJournal of the Turkish Chemical Society, Section A: Chemistryen_US
dc.identifier.volume5en_US
dc.identifier.issue3en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.contributor.departmentTAÜ, Fen Fakültesi, Moleküler Biyoteknoloji Bölümüen_US
dc.contributor.institutionauthorCoşkuner Weber, Orkide
dc.identifier.doi10.18596/jotcsa.424144
dc.identifier.startpage981en_US
dc.identifier.endpage1008en_US


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