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Fibrillization of β‐Amyloid Peptides via Chemically Modulated Pathway
Author(s) -
Guo ZhongHong,
Yang ChienI,
Ho ChengI,
Huang ShingJong,
Chen YinChung,
Tai HwanChing,
Chan Jerry Chun Chung
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201706001
Subject(s) - liposome , fibril , chemistry , peptide , monomer , amyloid (mycology) , biophysics , amyloid fibril , p3 peptide , nuclear magnetic resonance spectroscopy , residue (chemistry) , biochemistry , amyloid β , amyloid precursor protein , alzheimer's disease , stereochemistry , biology , organic chemistry , polymer , medicine , inorganic chemistry , disease , pathology
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.