Fibrillization of β-Amyloid Peptides via Chemically Modulated Pathway
Journal
Chemistry - A European Journal
Journal Volume
24
Journal Issue
19
Pages
4939-4943
Date Issued
2018
Author(s)
Guo, Z.-H.
Yang, C.-I.
Ho, C.-I.
Huang, S.-J.
Chen, Y.-C.
Tai, H.-C.
Chan, J.C.C.
Abstract
The aggregation of β-amyloid peptides is closely associated with Alzheimer's disease. We have used liposomes to modulate the early aggregation events of 40-residue β-amyloid peptides. The spatial confinement provided by liposomes leads to the formation of nonfibrillar aggregates of β-amyloid peptides. These on-pathway β-sheet intermediates were used to seed the fibrillization of the monomer peptides. Solid-state NMR spectroscopy revealed that the resultant fibrils have a more uniform structure than those formed in liposome-free solution. ? 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
SDGs
Other Subjects
Glycoproteins; Liposomes; Neurodegenerative diseases; Nuclear magnetic resonance spectroscopy; Nucleation; Peptides; Polymorphism; Self assembly; Alzheimer's disease; Beta amyloid peptides; Fibrillization; Peptidic fibrils; Seeding effects; Solid-state NMR spectroscopy; Spatial confinement; Uniform structure; Proteins; amyloid beta protein; liposome; peptide; Alzheimer disease; chemistry; cytoskeleton; human; protein secondary structure; Alzheimer Disease; Amyloid beta-Peptides; Cytoskeleton; Humans; Liposomes; Peptides; Protein Structure, Secondary
Type
journal article