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dc.contributor.authorAhyayauch, Hasna
dc.contributor.authorDe la Arada Echevarría, Igor ORCID
dc.contributor.authorMasserini, Massimo E.
dc.contributor.authorRodríguez Arrondo, José Luis
dc.contributor.authorGoñi Urcelay, Félix María ORCID
dc.contributor.authorAlonso Izquierdo, Alicia ORCID
dc.date.accessioned2020-03-20T17:00:56Z
dc.date.available2020-03-20T17:00:56Z
dc.date.issued2020-02-29
dc.identifier.citationInternational Journal of Molecular Sciences 21(5) : (2020) // Article ID 1674es_ES
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/10810/42256
dc.description.abstractThe binding of Aβ42 peptide monomers to sphingomyelin/cholesterol (1:1 mol ratio) bilayers containing 5 mol% gangliosides (either GM1, or GT1b, or a mixture of brain gangliosides) has been assayed by density gradient ultracentrifugation. This procedure provides a direct method for measuring vesicle-bound peptides after non-bound fraction separation. This centrifugation technique has rarely been used in this context previously. The results show that gangliosides increase by about two-fold the amount of Aβ42 bound to sphingomyelin/cholesterol vesicles. Complementary studies of the same systems using thioflavin T fluorescence, Langmuir monolayers or infrared spectroscopy confirm the ganglioside-dependent increased binding. Furthermore these studies reveal that gangliosides facilitate the aggregation of Aβ42 giving rise to more extended β-sheets. Thus, gangliosides have both a quantitative and a qualitative effect on the binding of Aβ42 to sphingomyelin/cholesterol bilayers.es_ES
dc.description.sponsorshipThis work was supported in part by grants from the Spanish Ministry of Economy (grant FEDER MINECO PGC2018-099857-B-I00) and the Basque Government (grants No. IT1264-19 and IT1270-19).es_ES
dc.language.isoenges_ES
dc.publisherMDPIes_ES
dc.relationinfo:eu-repo/grantAgreement/MINECO/PGC2018-099857-B-I00es_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/
dc.subjectAβ42es_ES
dc.subjectbeta-amyloides_ES
dc.subjectmembrane bindinges_ES
dc.subjectdensity gradient ultracentrifugationes_ES
dc.subjectgangliosidees_ES
dc.subjectsphingomyelines_ES
dc.subjectcholesteroles_ES
dc.titleThe Binding of Aβ42 Peptide Monomers to Sphingomyelin/Cholesterol/Ganglioside Bilayers Assayed by Density Gradient Ultracentrifugationes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.date.updated2020-03-13T13:09:41Z
dc.rights.holder© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)es_ES
dc.relation.publisherversionhttps://www.mdpi.com/1422-0067/21/5/1674es_ES
dc.identifier.doi10.3390/ijms21051674
dc.departamentoesBioquímica y biología molecular
dc.departamentoeuBiokimika eta biologia molekularra


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© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)
Except where otherwise noted, this item's license is described as © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)