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Amyloidosis of Alzh...
Amyloidosis of Alzheimer's A peptides : solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
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- Antzutkin, Oleg (author)
- Luleå tekniska universitet,Industriell miljö- och processteknik
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(creator_code:org_t)
- 2004-01-14
- 2004
- English.
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In: Magnetic Resonance in Chemistry. - : Wiley. - 0749-1581 .- 1097-458X. ; 42:2, s. 231-246
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https://urn.kb.se/re...
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Abstract
Subject headings
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- 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 1H,13C 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 27Al NMR techniques, are also presented.
Subject headings
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
Keyword
- Chemistry of Interfaces
- Gränsytors kemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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