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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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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. |
format | Online Article Text |
id | pubmed-5618134 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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