Structural Polymorphism of Alzheimer’s β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study
نویسندگان
چکیده
منابع مشابه
Structural characterization of polyglutamine fibrils by solid-state NMR spectroscopy.
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides below, at, and above the toxicity limit of around 37 glutamine residues using solid-state NMR and electron microscopy. Experimental data are consistent with a dry fibril core of at least 70-80 Å ...
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Formation of senile plaques containing amyloid fibrils of Aβ (amyloid β-peptide) is a pathological hallmark of Alzheimer's disease. Unlike globular proteins, which fold into unique structures, the fibrils of Aβ and other amyloid proteins often contain multiple polymorphs. Polymorphism of amyloid fibrils leads to different toxicity in amyloid diseases and may be the basis for prion strains, but ...
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We present a structural model for amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)), based on a set of experimental constraints from solid state NMR spectroscopy. The model additionally incorporates the cross-beta structural motif established by x-ray fiber diffraction and satisfies constraints on Abeta(1-40) fibril dimensions and ma...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2016
ISSN: 0002-7863,1520-5126
DOI: 10.1021/jacs.6b03715