Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective
Aβ peptides are known to bind neural plasma membranes in a process leading to the deposit of Aβ-enriched plaques. These extracellular structures are characteristic of Alzheimer's disease, the major cause of late-age dementia. The mechanisms of Aβ plaque formation and deposition are far from bei...
| Autores: | , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2024 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/373287 |
| Acceso en línea: | http://hdl.handle.net/10261/373287 https://api.elsevier.com/content/abstract/scopus_id/85197247745 |
| 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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Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical PerspectiveAhyayauch, HasnaMasserini, MassimoAlonso, AliciaGoñi, Félix M.Aβ42β-amyloidAβ membrane bindingGangliosideSphingomyelinCholesterolIsothermal calorimetryLangmuir balanceAlzheimer’s diseaseAβ peptides are known to bind neural plasma membranes in a process leading to the deposit of Aβ-enriched plaques. These extracellular structures are characteristic of Alzheimer's disease, the major cause of late-age dementia. The mechanisms of Aβ plaque formation and deposition are far from being understood. A vast number of studies in the literature describe the efforts to analyze those mechanisms using a variety of tools. The present review focuses on biophysical studies mostly carried out with model membranes or with computational tools. This review starts by describing basic physical aspects of lipid phases and commonly used model membranes (monolayers and bilayers). This is followed by a discussion of the biophysical techniques applied to these systems, mainly but not exclusively Langmuir monolayers, isothermal calorimetry, density-gradient ultracentrifugation, and molecular dynamics. The Methodological Section is followed by the core of the review, which includes a summary of important results obtained with each technique. The last section is devoted to an overall reflection and an effort to understand Aβ-bilayer binding. Concepts such as Aβ peptide membrane binding, adsorption, and insertion are defined and differentiated. The roles of membrane lipid order, nanodomain formation, and electrostatic forces in Aβ-membrane interaction are separately identified and discussed.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.Peer reviewedMultidisciplinary Digital Publishing InstituteMinisterio de Ciencia, Innovación y Universidades (España)Agencia Estatal de Investigación (España)European CommissionEusko JaurlaritzaAlonso, Alicia [0000-0002-2730-7470]Goñi, Félix M. [0000-0001-6270-9216]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_dcae04bcPublisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/373287https://api.elsevier.com/content/abstract/scopus_id/85197247745reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-124461NB-I00http://dx.doi.org/10.3390/ijms25126401Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3732872026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| title |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| spellingShingle |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective Ahyayauch, Hasna Aβ42 β-amyloid Aβ membrane binding Ganglioside Sphingomyelin Cholesterol Isothermal calorimetry Langmuir balance Alzheimer’s disease |
| title_short |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| title_full |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| title_fullStr |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| title_full_unstemmed |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| title_sort |
Understanding Aβ Peptide Binding to Lipid Membranes: A Biophysical Perspective |
| dc.creator.none.fl_str_mv |
Ahyayauch, Hasna Masserini, Massimo Alonso, Alicia Goñi, Félix M. |
| author |
Ahyayauch, Hasna |
| author_facet |
Ahyayauch, Hasna Masserini, Massimo Alonso, Alicia Goñi, Félix M. |
| author_role |
author |
| author2 |
Masserini, Massimo Alonso, Alicia Goñi, Félix M. |
| author2_role |
author author author |
| dc.contributor.none.fl_str_mv |
Ministerio de Ciencia, Innovación y Universidades (España) Agencia Estatal de Investigación (España) European Commission Eusko Jaurlaritza Alonso, Alicia [0000-0002-2730-7470] Goñi, Félix M. [0000-0001-6270-9216] Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] |
| 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 |
Aβ peptides are known to bind neural plasma membranes in a process leading to the deposit of Aβ-enriched plaques. These extracellular structures are characteristic of Alzheimer's disease, the major cause of late-age dementia. The mechanisms of Aβ plaque formation and deposition are far from being understood. A vast number of studies in the literature describe the efforts to analyze those mechanisms using a variety of tools. The present review focuses on biophysical studies mostly carried out with model membranes or with computational tools. This review starts by describing basic physical aspects of lipid phases and commonly used model membranes (monolayers and bilayers). This is followed by a discussion of the biophysical techniques applied to these systems, mainly but not exclusively Langmuir monolayers, isothermal calorimetry, density-gradient ultracentrifugation, and molecular dynamics. The Methodological Section is followed by the core of the review, which includes a summary of important results obtained with each technique. The last section is devoted to an overall reflection and an effort to understand Aβ-bilayer binding. Concepts such as Aβ peptide membrane binding, adsorption, and insertion are defined and differentiated. The roles of membrane lipid order, nanodomain formation, and electrostatic forces in Aβ-membrane interaction are separately identified and discussed. |
| publishDate |
2024 |
| dc.date.none.fl_str_mv |
2024 2024 2024 |
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info:eu-repo/semantics/article http://purl.org/coar/resource_type/c_dcae04bc Publisher's version info:eu-repo/semantics/publishedVersion |
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article |
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publishedVersion |
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http://hdl.handle.net/10261/373287 https://api.elsevier.com/content/abstract/scopus_id/85197247745 |
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http://hdl.handle.net/10261/373287 https://api.elsevier.com/content/abstract/scopus_id/85197247745 |
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Inglés |
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Inglés |
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#PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-124461NB-I00 http://dx.doi.org/10.3390/ijms25126401 Sí |
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Multidisciplinary Digital Publishing Institute |
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Multidisciplinary Digital Publishing Institute |
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