The circularization of amyloid fibrils formed by apolipoprotein C-II.
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 o...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2003
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| _version_ | 1826258614596141056 |
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| author | Hatters, D MacRaild, C Daniels, R Gosal, W Thomson, N Jones, J Davis, J MacPhee, C Dobson, C Howlett, G |
| author_facet | Hatters, D MacRaild, C Daniels, R Gosal, W Thomson, N Jones, J Davis, J MacPhee, C Dobson, C Howlett, G |
| author_sort | Hatters, D |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T18:36:44Z |
| format | Journal article |
| id | oxford-uuid:0b80db8b-4b92-4df8-96a3-32f365b926d8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:36:44Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:0b80db8b-4b92-4df8-96a3-32f365b926d82022-03-26T09:29:47ZThe circularization of amyloid fibrils formed by apolipoprotein C-II.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0b80db8b-4b92-4df8-96a3-32f365b926d8EnglishSymplectic Elements at Oxford2003Hatters, DMacRaild, CDaniels, RGosal, WThomson, NJones, JDavis, JMacPhee, CDobson, CHowlett, GAmyloid 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. |
| spellingShingle | Hatters, D MacRaild, C Daniels, R Gosal, W Thomson, N Jones, J Davis, J MacPhee, C Dobson, C Howlett, G The circularization of amyloid fibrils formed by apolipoprotein C-II. |
| title | The circularization of amyloid fibrils formed by apolipoprotein C-II. |
| title_full | The circularization of amyloid fibrils formed by apolipoprotein C-II. |
| title_fullStr | The circularization of amyloid fibrils formed by apolipoprotein C-II. |
| title_full_unstemmed | The circularization of amyloid fibrils formed by apolipoprotein C-II. |
| title_short | The circularization of amyloid fibrils formed by apolipoprotein C-II. |
| title_sort | circularization of amyloid fibrils formed by apolipoprotein c ii |
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