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...
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MDPI AG
2024-03-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/14/3/298 |
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| author | Hasna Ahyayauch Massimo E. Masserini Félix M. Goñi Alicia Alonso |
| author_facet | Hasna Ahyayauch Massimo E. Masserini Félix M. Goñi Alicia Alonso |
| author_sort | Hasna Ahyayauch |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-24T18:29:52Z |
| format | Article |
| id | doaj.art-2f47dfde54d24cd5b970faf8696a9dc3 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-04-24T18:29:52Z |
| publishDate | 2024-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-2f47dfde54d24cd5b970faf8696a9dc32024-03-27T13:27:53ZengMDPI AGBiomolecules2218-273X2024-03-0114329810.3390/biom14030298The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered StateHasna Ahyayauch0Massimo E. Masserini1Félix M. Goñi2Alicia Alonso3Departamento de Bioquímica, Instituto Biofisika (CSIC, UPV/EHU), Universidad del País Vasco, 48940 Leioa, SpainSchool of Medicine and Surgery, University of Milano-Bicocca, 20900 Monza, ItalyDepartamento de Bioquímica, Instituto Biofisika (CSIC, UPV/EHU), Universidad del País Vasco, 48940 Leioa, SpainDepartamento de Bioquímica, Instituto Biofisika (CSIC, UPV/EHU), Universidad del País Vasco, 48940 Leioa, SpainThe 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.https://www.mdpi.com/2218-273X/14/3/298Aβ42β-amyloidAβ membrane bindinggangliosidesphingomyelincholesterol |
| spellingShingle | Hasna Ahyayauch Massimo E. Masserini Félix M. Goñi Alicia Alonso The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State Biomolecules Aβ42 β-amyloid Aβ membrane binding ganglioside sphingomyelin cholesterol |
| title | 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_short | The Influence of Lipid Electric Charge on the Binding of Aβ(1–42) Amyloid Peptide to Bilayers in the Liquid-Ordered State |
| title_sort | influence of lipid electric charge on the binding of aβ 1 42 amyloid peptide to bilayers in the liquid ordered state |
| topic | Aβ42 β-amyloid Aβ membrane binding ganglioside sphingomyelin cholesterol |
| url | https://www.mdpi.com/2218-273X/14/3/298 |
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