“A structural model for Alzheimer’s β-amyloid fibrils based on experimental constraints from solid state NMR” Robert Tyckoet al. Proc. Natl. Acad. Sci. USA2002,99, 16742. doi:10.1073/pnas.262663499 (a) “Induction of peptide conformation at apolar/water interfaces: a study with model pe...
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The amyloid-β (Aβ) peptides that form the amyloid fibrils associated with Alzheimer’s disease are generated by sequential proteolysis of the amyloid precursor protein by β- and γ-secretase. The two predominant Aβ peptides, Aβ40 and Aβ42, differ by two amino acids, are soluble as ...
Amyloid fibrilscomposed of different proteins share a number of common structural features, despite the fact that these proteins, in their native states, vary widely in structure, cellular locations, and properties. For example, the amyloid proteintransthyretinis atetramerof subunits with a total molec...
One such process is the formation of amyloid fibrils, wherein these species are often masked by ensemble-averaging methods. This review focusses on the use of fluorescence-based single-molecule techniques to study amyloid fibrils: their formation, disaggregation, and the interactions that govern ...
High resolution structural information on amyloid fibrils is crucial for the understanding of their formation mechanisms and for the rational design of amyloid inhibitors in the context of protein misfolding diseases. The Src-homology 3 domain of phospha
Amyloid fibrils are mechanically robust and partly resistant to proteolytic degradation, making them potential candidates for scaffold materials in cell culture, tissue engineering, drug delivery and other applications. Such applications of amyloids would benefit from the possibility to functionalize the fibri...
Solid-state nuclear magnetic resonance (NMR) measurements have made major contributions to our understanding of the molecular structures of amyloid fibrils, including fibrils formed by the beta-amyloid peptide associated with Alzheimer's disease, by proteins associated with fungal prions, and by a varie...
Amyloid fibrils composed of different proteins share a number of common structural features, despite the fact that these proteins, in their native states, vary widely in structure, cellular locations, and properties. For example, the amyloid protein transthyretin is a tetramer of subunits with a tot...
Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which