Amyloidosis of Alzheimer's Abeta peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies.
Aggregation cascade for Alzheimer's amyloid-beta 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 beta-amyloid fibrils are given. Recent progress in obtaining structural constraints on Abeta-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 Abeta(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.
Antzutkin
Oleg N
ON
Division of Chemistry, Luleå University of Technology, S-971 87 Luleå, Sweden. Oleg.Antzukin@km.luth.se
D000544:Alzheimer Disease / Q000473:pathology*; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure*; D000686:Amyloidosis / Q000473:pathology*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D018625:Microscopy, Atomic Force; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry
D016229:Amyloid beta-Peptides; D009498:Neurotoxins; D010446:Peptide Fragments