SMALL ANGLE X-RAY SCATTERING STUDY OF INSULIN FIBRILS

被引：0
作者：
Romanova, M. V. [1 ]
Maliyov, I. L. [1 ]
Girych, M. S. [1 ]
Vus, E. A. [1 ]
Svergun, D. I. [2 ]
Kikhney, Al. [2 ]
Jeffries, C. [2 ]
机构：
[1] Kharkov Natl Univ, Dept Nucl & Med Phys, 4 Svobody Sq, UA-61022 Kharkov, Ukraine
[2] EMBL, D-22603 Hamburg, Germany
来源：
EAST EUROPEAN JOURNAL OF PHYSICS | 2014年 / 1卷 / 04期
关键词：
amyloid fibrils; insulin; small angle X-ray scattering; Thioflavin T;
D O I：
暂无
中图分类号：
O4 [物理学];
学科分类号：
0702 ;
摘要：
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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页码：96 / 99
页数：4
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