Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers
The interaction of amyloid β-peptide (Aβ) with cell membranes is believed to play a central role in the pathogenesis of Alzheimer's disease. In particular, recent experimental evidence indicates that bilayer and monolayer membranes accelerate the aggregation and amyloid fibril formation rate of...
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2011
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1808_n1_p26_Izmitli http://hdl.handle.net/20.500.12110/paper_00052736_v1808_n1_p26_Izmitli |
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paper:paper_00052736_v1808_n1_p26_Izmitli2023-06-08T14:29:50Z Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers Schebor, Carolina C. Alzheimer's disease Amyloid beta peptide Membrane Monolayer Trehalose amyloid beta protein lipid trehalose alpha helix Alzheimer disease animal cell animal experiment aqueous solution article cell membrane controlled study enzyme kinetics isotherm Langmuir Blodgett film lipid monolayer mouse nonhuman priority journal protein conformation protein function protein interaction protein structure thermodynamics water temperature Alzheimer Disease Amyloid beta-Peptides Animals Anions Computer Simulation Humans Lipid Bilayers Mice Models, Molecular Molecular Conformation Peptides Phosphatidylglycerols Temperature Time Factors Trehalose The interaction of amyloid β-peptide (Aβ) with cell membranes is believed to play a central role in the pathogenesis of Alzheimer's disease. In particular, recent experimental evidence indicates that bilayer and monolayer membranes accelerate the aggregation and amyloid fibril formation rate of Aβ. Understanding that interaction could help develop therapeutic strategies for treatment of the disease. Trehalose, a disaccharide of glucose, has been shown to be effective in preventing the aggregation of numerous proteins. It has also been shown to delay the onset of certain amyloid-related diseases in a mouse model. Using Langmuir monolayers and molecular simulations of the corresponding system, we study several thermodynamic and kinetic aspects of the insertion of Aβ peptide into DPPG monolayers in water and trehalose subphases. In the water subphase, the insertion of the Aβ peptide into the monolayer exhibits a lag time which decreases with increasing temperature of the subphase. In the presence of trehalose, the lag time is completely eliminated and peptide insertion is completed within a shorter time period compared to that observed in pure water. Molecular simulations show that more peptide is inserted into the monolayer in the water subphase, and that such insertion is deeper. The peptide at the monolayer interface orients itself parallel to the monolayer, while it inserts with an angle of 50° in the trehalose subphase. Simulations also show that trehalose reduces the conformational change that the peptide undergoes when it inserts into the monolayer. This observation helps explain the experimentally observed elimination of the lag time by trehalose and the temperature dependence of the lag time in the water subphase. © 2010 Elsevier B.V.All rights reserved. Fil:Schebor, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1808_n1_p26_Izmitli http://hdl.handle.net/20.500.12110/paper_00052736_v1808_n1_p26_Izmitli |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Alzheimer's disease Amyloid beta peptide Membrane Monolayer Trehalose amyloid beta protein lipid trehalose alpha helix Alzheimer disease animal cell animal experiment aqueous solution article cell membrane controlled study enzyme kinetics isotherm Langmuir Blodgett film lipid monolayer mouse nonhuman priority journal protein conformation protein function protein interaction protein structure thermodynamics water temperature Alzheimer Disease Amyloid beta-Peptides Animals Anions Computer Simulation Humans Lipid Bilayers Mice Models, Molecular Molecular Conformation Peptides Phosphatidylglycerols Temperature Time Factors Trehalose |
| spellingShingle |
Alzheimer's disease Amyloid beta peptide Membrane Monolayer Trehalose amyloid beta protein lipid trehalose alpha helix Alzheimer disease animal cell animal experiment aqueous solution article cell membrane controlled study enzyme kinetics isotherm Langmuir Blodgett film lipid monolayer mouse nonhuman priority journal protein conformation protein function protein interaction protein structure thermodynamics water temperature Alzheimer Disease Amyloid beta-Peptides Animals Anions Computer Simulation Humans Lipid Bilayers Mice Models, Molecular Molecular Conformation Peptides Phosphatidylglycerols Temperature Time Factors Trehalose Schebor, Carolina C. Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers |
| topic_facet |
Alzheimer's disease Amyloid beta peptide Membrane Monolayer Trehalose amyloid beta protein lipid trehalose alpha helix Alzheimer disease animal cell animal experiment aqueous solution article cell membrane controlled study enzyme kinetics isotherm Langmuir Blodgett film lipid monolayer mouse nonhuman priority journal protein conformation protein function protein interaction protein structure thermodynamics water temperature Alzheimer Disease Amyloid beta-Peptides Animals Anions Computer Simulation Humans Lipid Bilayers Mice Models, Molecular Molecular Conformation Peptides Phosphatidylglycerols Temperature Time Factors Trehalose |
| description |
The interaction of amyloid β-peptide (Aβ) with cell membranes is believed to play a central role in the pathogenesis of Alzheimer's disease. In particular, recent experimental evidence indicates that bilayer and monolayer membranes accelerate the aggregation and amyloid fibril formation rate of Aβ. Understanding that interaction could help develop therapeutic strategies for treatment of the disease. Trehalose, a disaccharide of glucose, has been shown to be effective in preventing the aggregation of numerous proteins. It has also been shown to delay the onset of certain amyloid-related diseases in a mouse model. Using Langmuir monolayers and molecular simulations of the corresponding system, we study several thermodynamic and kinetic aspects of the insertion of Aβ peptide into DPPG monolayers in water and trehalose subphases. In the water subphase, the insertion of the Aβ peptide into the monolayer exhibits a lag time which decreases with increasing temperature of the subphase. In the presence of trehalose, the lag time is completely eliminated and peptide insertion is completed within a shorter time period compared to that observed in pure water. Molecular simulations show that more peptide is inserted into the monolayer in the water subphase, and that such insertion is deeper. The peptide at the monolayer interface orients itself parallel to the monolayer, while it inserts with an angle of 50° in the trehalose subphase. Simulations also show that trehalose reduces the conformational change that the peptide undergoes when it inserts into the monolayer. This observation helps explain the experimentally observed elimination of the lag time by trehalose and the temperature dependence of the lag time in the water subphase. © 2010 Elsevier B.V.All rights reserved. |
| author |
Schebor, Carolina C. |
| author_facet |
Schebor, Carolina C. |
| author_sort |
Schebor, Carolina C. |
| title |
Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers |
| title_short |
Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers |
| title_full |
Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers |
| title_fullStr |
Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers |
| title_full_unstemmed |
Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers |
| title_sort |
effect of trehalose on the interaction of alzheimer's aβ-peptide and anionic lipid monolayers |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1808_n1_p26_Izmitli http://hdl.handle.net/20.500.12110/paper_00052736_v1808_n1_p26_Izmitli |
| work_keys_str_mv |
AT scheborcarolinac effectoftrehaloseontheinteractionofalzheimersabpeptideandanioniclipidmonolayers |
| _version_ |
1768545858914091008 |