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Amyloidosis of Alzheimer's Aβ peptides: solid‐state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
Author(s) -
Antzutkin Oleg N.
Publication year - 2004
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1341
Subject(s) - chemistry , transmission electron microscopy , solid state nuclear magnetic resonance , electron paramagnetic resonance , scanning transmission electron microscopy , crystallography , amyloid (mycology) , fibril , nuclear magnetic resonance , nanotechnology , materials science , biochemistry , inorganic chemistry , physics
Aggregation cascade for Alzheimer's amyloid‐β peptides, its relevance to neurotoxicity in the course of Alzheimer's disease and experimental methods useful for these studies are discussed. Details of the solid‐phase peptide synthesis and sample preparation procedures for Alzheimer's β‐amyloid fibrils are given. Recent progress in obtaining structural constraints on Aβ‐fibrils from solid‐state NMR and scanning transmission electron microscopy (STEM) data is discussed. Polymorphism of amyloid fibrils and oligomers of the ‘Arctic’ mutant of Aβ(1–40) was studied by 1 H, 13 C solid‐state NMR, transmission electron microscopy (TEM) and atomic force microscopy (AFM), and a real‐time aggregation of different polymorphs of the peptide was observed with the aid of in situ AFM. Recent results on binding of Cu(II) ions and Al–citrate and Al–ATP complexes to amyloid fibrils, as studied by electron paramagnetic resonance (EPR) and solid‐state 27 Al NMR techniques, are also presented. Copyright © 2004 John Wiley & Sons, Ltd.