The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State
dc.contributor.author | Ahyayauch, Hasna | |
dc.contributor.author | Masserini, Massimo E. | |
dc.contributor.author | Goñi Urcelay, Félix María ![]() | |
dc.contributor.author | Alonso Izquierdo, Alicia ![]() | |
dc.date.accessioned | 2024-04-08T16:32:16Z | |
dc.date.available | 2024-04-08T16:32:16Z | |
dc.date.issued | 2024-03-01 | |
dc.identifier.citation | Biomolecules 14(3) : (2024) // Article ID 298 | es_ES |
dc.identifier.issn | 2218-273X | |
dc.identifier.uri | http://hdl.handle.net/10810/66555 | |
dc.description.abstract | The amyloidogenic Aβ peptides are widely considered as a pathogenic agent in Alzheimer’s disease. Aβ(1-42) would form aggregates of amyloid fibrils on the neuron plasma membranes, thus perturbing neuronal functionality. Conflicting data are available on the influence of bilayer order on Aβ(1-42) binding to membranes. In the present study, a biophysical approach was used in which isothermal calorimetry and surface pressure measurements were applied to explore the interaction of Aβ(1-42) in either monomeric, oligomeric, or fibrillar form with model membranes (bilayers or monolayers) in the liquid-ordered state that were either electrically neutral or negatively charged. In the latter case, this contained phosphatidic acid, cardiolipin, or ganglioside. The calorimetric studies showed that Aβ(1-42) fibrils, oligomers, and monomers could bind and/or be inserted into bilayers, irrespective of electric charge, in the liquid-ordered state, except that monomers could not interact with electrically neutral bilayers. The monolayer studies in the Langmuir balance demonstrated that Aβ(1-42) aggregation hindered peptide insertion into the monolayer, hindered insertion in the decreasing order of monomer > oligomer > fibril, and that lipid composition did not cause large differences in insertion, apart from a slight facilitation of monomer and oligomer insertion by gangliosides. | es_ES |
dc.description.sponsorship | This work was funded in part by the Spanish Ministry of Science, Innovation, and Universities (MCIU), Agencia Estatal de Investigación (AEI), Fondo Europeo de Desarrollo Regional (FEDER) (grant No. PID2021-124461NB-I00), the Basque Government (grant No. IT1625-22), Fundación Ramón Areces (CIVP20A6619), Fundación Biofísica Bizkaia, and the Basque Excellence Research Centre (BERC) program of the Basque Government. H.A. was supported by funds from Fundación Ramón Areces. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | MDPI | es_ES |
dc.relation | info:eu-repo/grantAgreement/MICINN/PID2021-124461NB-I00 | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/es/ | |
dc.subject | Aβ42 | es_ES |
dc.subject | β-amyloid | es_ES |
dc.subject | Aβ membrane binding | es_ES |
dc.subject | ganglioside | es_ES |
dc.subject | sphingomyelin | es_ES |
dc.subject | cholesterol | es_ES |
dc.subject | isothermal calorimetry | es_ES |
dc.subject | Langmuir balance | es_ES |
dc.subject | Alzheimer’s disease | es_ES |
dc.title | The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.date.updated | 2024-03-27T13:16:01Z | |
dc.rights.holder | © 2024 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 (https://creativecommons.org/licenses/by/ 4.0/). | es_ES |
dc.relation.publisherversion | https://www.mdpi.com/2218-273X/14/3/298 | es_ES |
dc.identifier.doi | 10.3390/biom14030298 | |
dc.departamentoes | Bioquímica y biología molecular | |
dc.departamentoeu | Biokimika eta biologia molekularra |
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Except where otherwise noted, this item's license is described as © 2024 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 (https://creativecommons.org/licenses/by/ 4.0/).