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* Department of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Australia; Cavendish Laboratory, University of Cambridge, Cambridge, United Kingdom; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; Department of Physics, Clarendon Laboratory, University of Oxford, Oxford, United Kingdom; ¶ Inorganic Chemistry Laboratory, University of Oxford, Oxford, United Kingdom; and || Department of Chemistry, University of Cambridge, Cambridge, United Kingdom
Correspondence: Address reprint requests to Dr. Cait E. MacPhee, Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE UK. Tel.: 44-0-122-333-7263; Fax: 44-0-122-333-7000; E-mail: cem48{at}cam.ac.uk.
Amyloid fibrils have historically been characterized by diagnostic dye-binding assays, their fibrillar morphology, and a "cross-ß" x-ray diffraction pattern. Whereas the latter demonstrates that amyloid fibrils have a common ß-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 
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-ß superstructure can, as a function of the protein constituent, give rise to great variation in the physical properties of amyloid fibrils.
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