The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State
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) bin...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2024 |
| País: | España |
| Institución: | Universidad del País Vasco |
| Repositorio: | Addi. Archivo Digital para la Docencia y la Investigación |
| OAI Identifier: | oai:addi.ehu.eus:10810/66555 |
| Acceso en línea: | http://hdl.handle.net/10810/66555 |
| Access Level: | acceso abierto |
| Palabra clave: | Aβ42 β-amyloid Aβ membrane binding ganglioside sphingomyelin cholesterol isothermal calorimetry Langmuir balance Alzheimer’s disease |
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The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered StateAhyayauch, HasnaMasserini, Massimo E.Goñi Urcelay, Félix MaríaAlonso Izquierdo, AliciaAβ42β-amyloidAβ membrane bindinggangliosidesphingomyelincholesterolisothermal calorimetryLangmuir balanceAlzheimer’s diseaseThe 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.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.MDPI2024202420242024info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/66555reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoInglésinfo:eu-repo/grantAgreement/MICINN/PID2021-124461NB-I00/https://www.mdpi.com/2218-273X/14/3/298info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/es/© 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/).oai:addi.ehu.eus:10810/665552026-06-18T09:23:17Z |
| dc.title.none.fl_str_mv |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| title |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| spellingShingle |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State Ahyayauch, Hasna Aβ42 β-amyloid Aβ membrane binding ganglioside sphingomyelin cholesterol isothermal calorimetry Langmuir balance Alzheimer’s disease |
| title_short |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| title_full |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| title_fullStr |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| title_full_unstemmed |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| title_sort |
The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| dc.creator.none.fl_str_mv |
Ahyayauch, Hasna Masserini, Massimo E. Goñi Urcelay, Félix María Alonso Izquierdo, Alicia |
| author |
Ahyayauch, Hasna |
| author_facet |
Ahyayauch, Hasna Masserini, Massimo E. Goñi Urcelay, Félix María Alonso Izquierdo, Alicia |
| author_role |
author |
| author2 |
Masserini, Massimo E. Goñi Urcelay, Félix María Alonso Izquierdo, Alicia |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
Aβ42 β-amyloid Aβ membrane binding ganglioside sphingomyelin cholesterol isothermal calorimetry Langmuir balance Alzheimer’s disease |
| topic |
Aβ42 β-amyloid Aβ membrane binding ganglioside sphingomyelin cholesterol isothermal calorimetry Langmuir balance Alzheimer’s disease |
| description |
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. |
| publishDate |
2024 |
| dc.date.none.fl_str_mv |
2024 2024 2024 2024 |
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info:eu-repo/semantics/article |
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article |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10810/66555 |
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http://hdl.handle.net/10810/66555 |
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Inglés |
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Inglés |
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info:eu-repo/grantAgreement/MICINN/PID2021-124461NB-I00/ https://www.mdpi.com/2218-273X/14/3/298 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/es/ |
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openAccess |
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http://creativecommons.org/licenses/by/4.0/es/ |
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