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dc.contributor.author
Izmitli, Aslin
dc.contributor.author
Schebor, Carolina Claudia
dc.contributor.author
McGovern, Michael P.
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Reddy, Allam S.
dc.contributor.author
Abbott, Nicholas L.
dc.contributor.author
De Pablo, Juan J.
dc.date.available
2019-01-15T21:34:55Z
dc.date.issued
2011-01
dc.identifier.citation
Izmitli, Aslin; Schebor, Carolina Claudia; McGovern, Michael P.; Reddy, Allam S.; Abbott, Nicholas L.; et al.; Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1808; 1; 1-2011; 26-33
dc.identifier.issn
0005-2736
dc.identifier.uri
http://hdl.handle.net/11336/68094
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Alzheimer'S Disease
dc.subject
Amyloid Beta Peptide
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Membrane
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Monolayer
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Trehalose
dc.subject.classification
Otras Ciencias Químicas
dc.subject.classification
Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Effect of trehalose on the interaction of Alzheimer's Aβ-peptide and anionic lipid monolayers
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-14T18:05:32Z
dc.journal.volume
1808
dc.journal.number
1
dc.journal.pagination
26-33
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Izmitli, Aslin. University of Wisconsin Madison; Estados Unidos
dc.description.fil
Fil: Schebor, Carolina Claudia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: McGovern, Michael P.. University of Wisconsin Madison; Estados Unidos
dc.description.fil
Fil: Reddy, Allam S.. University of Wisconsin Madison; Estados Unidos
dc.description.fil
Fil: Abbott, Nicholas L.. University of Wisconsin Madison; Estados Unidos
dc.description.fil
Fil: De Pablo, Juan J.. University of Wisconsin Madison; Estados Unidos
dc.journal.title
Biochimica et Biophysica Acta - Biomembranes
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbamem.2010.09.024
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273610003391
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