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Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets

Amyloid- [Formula: see text] aggregates play a causative role in Alzheimer’s disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- [Formula: see text] pept...

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Detalles Bibliográficos
Autores principales: Khondker, Adree, Alsop, Richard J., Rheinstädter, Maikel C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618134/
https://www.ncbi.nlm.nih.gov/pubmed/28858214
http://dx.doi.org/10.3390/membranes7030049
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author Khondker, Adree
Alsop, Richard J.
Rheinstädter, Maikel C.
author_facet Khondker, Adree
Alsop, Richard J.
Rheinstädter, Maikel C.
author_sort Khondker, Adree
collection PubMed
description Amyloid- [Formula: see text] aggregates play a causative role in Alzheimer’s disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- [Formula: see text] peptides to nucleate and form well-ordered cross- [Formula: see text] sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- [Formula: see text] protein, [Formula: see text] , with the hydrophobicity, fluidity, and charge density of a lipid bilayer. We summarize recent biophysical studies of model membranes and relate these to the process of aggregation in physiological systems.
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spelling pubmed-56181342017-09-29 Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets Khondker, Adree Alsop, Richard J. Rheinstädter, Maikel C. Membranes (Basel) Review Amyloid- [Formula: see text] aggregates play a causative role in Alzheimer’s disease. These aggregates are a product of the physical environment provided by the basic neuronal membrane, composed of a lipid bilayer. The intrinsic properties of the lipid bilayer allow amyloid- [Formula: see text] peptides to nucleate and form well-ordered cross- [Formula: see text] sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- [Formula: see text] protein, [Formula: see text] , with the hydrophobicity, fluidity, and charge density of a lipid bilayer. We summarize recent biophysical studies of model membranes and relate these to the process of aggregation in physiological systems. MDPI 2017-08-31 /pmc/articles/PMC5618134/ /pubmed/28858214 http://dx.doi.org/10.3390/membranes7030049 Text en © 2017 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Khondker, Adree
Alsop, Richard J.
Rheinstädter, Maikel C.
Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
title Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
title_full Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
title_fullStr Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
title_full_unstemmed Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
title_short Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
title_sort membrane-accelerated amyloid-β aggregation and formation of cross-β sheets
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5618134/
https://www.ncbi.nlm.nih.gov/pubmed/28858214
http://dx.doi.org/10.3390/membranes7030049
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