Aggregation of Beta-Amyloid Peptides Proximal to Zwitterionic Lipid Bilayers
Journal
Chemistry - An Asian Journal
Journal Volume
10
Journal Issue
9
Pages
1967-1971
Date Issued
2015
Author(s)
Yang, C.-I.
Tsai, B.N.F.
Huang, S.-J.
Wang, T.-Y.
Tai, H.-C.
HWAN-CHING TAI
Abstract
One of the hallmarks of Alzheimers disease is the deposition of amyloid plaques, which consist of β-amyloid (Aβ) peptides in fibrillar states. Nonfibrillar Aβ aggregates have been considered as an important intermediate in the pathway of fibrillization, but little is known about the formation mechanism. The on-pathway β-sheet intermediates of Aβ40 peptides can be trapped by incubating the peptides in liposomes formed by zwitterionic lipids. The aggregates of Aβ40 peptides have been prepared at a peptide concentration of less than 10 μm. Solid-state NMR spectroscopy data show that the backbone conformation of the aggregates is almost identical to that of the fibrils formed in free solution. In contrast to anionic lipids, zwitterionic lipids, which are typical of neuronal soma, did not induce any significant conformational difference in Aβ40 fibrils. This liposome-Aβ system may serve as a useful model to study the fibril formation mechanism. Consensus of form: One of the hallmarks of Alzheimers disease is the deposition of amyloid plaques, which consist of β-amyloid (Aβ) peptides in fibrillar states. The bilayer membranes formed by zwitterionic phosphatidylcholine/phosphatidylethanolamine lipids do not affect the molecular structure of the aggregates of Aβ peptides. ? 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
SDGs
Other Subjects
Agglomeration; Aggregates; Glycoproteins; Lipid bilayers; Lipids; Liposomes; Neurodegenerative diseases; Nuclear magnetic resonance spectroscopy; Oligomers; Peptides; Alzheimers disease; Amyloid-beta peptides; Beta amyloid peptides; Conformational differences; Fibril formation; Formation mechanism; Solid-state NMR spectroscopy; Zwitterionic lipids; Proteins; amyloid beta protein; amyloid beta protein[1-40]; lipid bilayer; liposome; peptide fragment; protein aggregate; Alzheimer disease; chemistry; human; lipid bilayer; metabolism; protein secondary structure; ultrastructure; Alzheimer Disease; Amyloid beta-Peptides; Humans; Lipid Bilayers; Liposomes; Peptide Fragments; Protein Aggregates; Protein Structure, Secondary
Type
journal article