SMALL ANGLE X-RAY SCATTERING STUDY OF INSULIN FIBRILS
The small-angle X-ray scattering technique was employed to determine low-resolution 3D structure of insulin amyloid fibrils. This object is of particular interest since amyloid deposits of insulin causes insulin injection amyloidosis. Structural characterization of amyloid fibrils as a particular cl...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
V.N. Karazin Kharkiv National University Publishing
2015-03-01
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| Series: | East European Journal of Physics |
| Online Access: | https://periodicals.karazin.ua/eejp/article/view/1518 |
| Summary: | The small-angle X-ray scattering technique was employed to determine low-resolution 3D structure of insulin amyloid fibrils. This object is of particular interest since amyloid deposits of insulin causes insulin injection amyloidosis. Structural characterization of amyloid fibrils as a particular class of linear highly ordered protein aggregates is of utmost importance for deeper understanding of the molecular etiology of conformational diseases and development of effective therapeutic strategies. The small-angle X-ray scattering pattern analysis showed that the maximum dimension of the insulin fibril cross-section reaches 24±2.4 nm, while gyration radius of the cross-section is about 6 nm. |
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| ISSN: | 2312-4334 2312-4539 |