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

Amyloid- β 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- β peptides to nucleate and form...

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Main Authors:	Adree Khondker, Richard J. Alsop, Maikel C. Rheinstädter
Format:	Article
Language:	English
Published:	MDPI AG 2017-08-01
Series:	Membranes
Subjects:	Alzheimer’s disease amyloid-β hydrophobic fragment cross-β sheet
Online Access:	https://www.mdpi.com/2077-0375/7/3/49

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spelling	doaj-fd6c1aeb88e1462a973e0dc3d44c21502020-11-24T20:59:45ZengMDPI AGMembranes2077-03752017-08-01734910.3390/membranes7030049membranes7030049Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β SheetsAdree Khondker0Richard J. Alsop1Maikel C. Rheinstädter2Department of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, CanadaDepartment of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, CanadaDepartment of Physics and Astronomy, McMaster University, 1280 Main Street West, Hamilton, ON L8S 4M1, CanadaAmyloid- β 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- β peptides to nucleate and form well-ordered cross- β sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- β protein, A β 25 - 35 , 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.https://www.mdpi.com/2077-0375/7/3/49Alzheimer’s diseaseamyloid-βhydrophobic fragmentcross-β sheet
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Adree Khondker Richard J. Alsop Maikel C. Rheinstädter
spellingShingle	Adree Khondker Richard J. Alsop Maikel C. Rheinstädter Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets Membranes Alzheimer’s disease amyloid-β hydrophobic fragment cross-β sheet
author_facet	Adree Khondker Richard J. Alsop Maikel C. Rheinstädter
author_sort	Adree Khondker
title	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_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_sort	membrane-accelerated amyloid-β aggregation and formation of cross-β sheets
publisher	MDPI AG
series	Membranes
issn	2077-0375
publishDate	2017-08-01
description	Amyloid- β 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- β peptides to nucleate and form well-ordered cross- β sheets within the membrane. Here, we correlate the aggregation of the hydrophobic fragment of the amyloid- β protein, A β 25 - 35 , 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.
topic	Alzheimer’s disease amyloid-β hydrophobic fragment cross-β sheet
url	https://www.mdpi.com/2077-0375/7/3/49
work_keys_str_mv	AT adreekhondker membraneacceleratedamyloidbaggregationandformationofcrossbsheets AT richardjalsop membraneacceleratedamyloidbaggregationandformationofcrossbsheets AT maikelcrheinstadter membraneacceleratedamyloidbaggregationandformationofcrossbsheets
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Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets

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