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• W2012184588 abstract "Amyloid fibrils have historically been characterized by diagnostic dye-binding assays, their fibrillar morphology, and a cross-beta x-ray diffraction pattern. Whereas the latter demonstrates that amyloid fibrils have a common beta-sheet core structure, they display a substantial degree of morphological variation. One striking example is the remarkable ability of human apolipoprotein C-II amyloid fibrils to circularize and form closed rings. Here we explore in detail the structure of apoC-II amyloid fibrils using electron microscopy, atomic force microscopy, and x-ray diffraction studies. Our results suggest a model for apoC-II fibrils as ribbons approximately 2.1-nm thick and 13-nm wide with a helical repeat distance of 53 nm +/- 12 nm. We propose that the ribbons are highly flexible with a persistence length of 36 nm. We use these observed biophysical properties to model the apoC-II amyloid fibrils either as wormlike chains or using a random-walk approach, and confirm that the probability of ring formation is critically dependent on the fibril flexibility. More generally, the ability of apoC-II fibrils to form rings also highlights the degree to which the common cross-beta superstructure can, as a function of the protein constituent, give rise to great variation in the physical properties of amyloid fibrils." @default.
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• W2012184588 date "2003-12-01" @default.
• W2012184588 modified "2023-10-10" @default.
• W2012184588 title "The Circularization of Amyloid Fibrils Formed by Apolipoprotein C-II" @default.
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• W2012184588 doi "https://doi.org/10.1016/s0006-3495(03)74812-7" @default.
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