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dc.creatorMoreno-Castillo E.
dc.creatorÁlvarez-Ginarte Y.M.
dc.creatorValdés-Tresanco M.E.
dc.creatorMontero-Cabrera L.A.
dc.creatorMoreno E.
dc.creatorValiente P.A.
dc.date2020
dc.date.accessioned2020-04-29T14:53:52Z
dc.date.available2020-04-29T14:53:52Z
dc.identifier.issn9523499
dc.identifier.urihttp://hdl.handle.net/11407/5749
dc.descriptionAlzheimer's disease is a progressive neurodegenerative disorder characterized by the abnormal processing of the Tau and the amyloid precursor proteins. The unusual aggregation of Tau is based on the formation of intermolecular ?-sheets through two motifs: 275VQIINK280 and 306VQIVYK311. Phenylthiazolyl-hydrazides (PTHs) are capable of inhibiting/disassembling Tau aggregates. However, the disaggregation mechanism of Tau oligomers by PTHs is still unknown. In this work, we studied the disruption of the oligomeric form of the Tau motif 306VQIVYK311 by PTHs through molecular docking, molecular dynamics, and free energy calculations. We predicted hydrophobic interactions as the major driving forces for the stabilization of Tau oligomer, with V306 and I308 being the major contributors. Nonpolar component of the binding free energy is essential to stabilize Tau-PTH complexes. PTHs disrupted mainly the van der Waals interactions between the monomers, leading to oligomer destabilization. Destabilization of full Tau filament by PTHs and emodin was not observed in the sampled 20 ns; however, in all cases, the nonpolar component of the binding free energy is essential for the formation of Tau filament-PTH and Tau filament-emodin. These results provide useful clues for the design of more effective Tau-aggregation inhibitors. © 2020 John Wiley & Sons Ltd
dc.language.isoeng
dc.publisherJohn Wiley and Sons Ltd
dc.relation.isversionofhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85082511416&doi=10.1002%2fjmr.2848&partnerID=40&md5=6582e54d594aa5958919a5de0c2dd520
dc.sourceJournal of Molecular Recognition
dc.subjectLIE
dc.subjectMM-GBSA
dc.subjectmolecular docking
dc.subjectmolecular dynamics
dc.subjectphenylthiazolyl-hydrazides
dc.subjectTau protein
dc.titleUnderstanding the disrupting mechanism of the Tau aggregation motif 306VQIVYK311 by phenylthiazolyl-hydrazides inhibitors
dc.typeArticleeng
dc.rights.accessrightsinfo:eu-repo/semantics/restrictedAccess
dc.publisher.programFacultad de Ciencias Básicas
dc.identifier.doi10.1002/jmr.2848
dc.publisher.facultyFacultad de Ciencias Básicas
dc.affiliationMoreno-Castillo, E., Faculty of Chemistry, University of Havana, La Habana, Cuba, Department of Molecular Signal Processing, Leibniz Institute of Plant Biochemistry, Halle (Saale), Germany; Álvarez-Ginarte, Y.M., Faculty of Chemistry, University of Havana, La Habana, Cuba; Valdés-Tresanco, M.E., Center of Protein Studies, Faculty of Biology, University of Havana, La Habana, Cuba, Department of Biological Sciences, University of Calgary, Calgary, AB, Canada; Montero-Cabrera, L.A., Faculty of Chemistry, University of Havana, La Habana, Cuba; Moreno, E., Faculty of Basic Sciences, Universidad de Medellín, Medellín, Colombia; Valiente, P.A., Center of Protein Studies, Faculty of Biology, University of Havana, La Habana, Cuba, Donnelly Centre for Cellular & Biomolecular Research University of Toronto, Toronto, ON, Canada
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dc.type.driverinfo:eu-repo/semantics/article


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